Title of Invention

A FUSION PROTEIN CAPABLE OF ACTIVATING THE COMPLEMENT SYSTEM

Abstract

A fusion protein capable of activating the complement system The present invention relates to a fusion protein capable of activating the complement system, the fusion protein comprising a first polypeptide sequence derived from a lectin-complement pathway activating protein or a functional homologue thereof; and a second polypeptide sequence derived from a collectin or a functional homologue thereof; wherein said complement activating protein is not a collectin. A preferred fusion protein comprises amino acids of the L-ficolin sequence of figure 1 and amino acids of the MBL sequence shown in figure 2. The fusion protein is suitable for use in treatment consisting of creation, reconstitution, enhancing and/or stimulating the opsonic and /or bactericidal activity of the complement system, i.e. enhancing the ability of the immune defence to recognize and kill microbial pathogens, and accordingly, the invention relates to a medicament comprising the fusion protein, methods for producing said fusion protein and method for treating diseases, in particular infections.

Full Text

Field of invention The present invention relates to a fusion protein capable of activating the,comple-ment system, methods for producing said fusion protein as well as pharmaceutiai composition comprising said fusion protein and methods for treating diseases, in particular infections, with said fusion protein. Background of invention Animals have developed different complex strategies to protect themselves against infections. The immune responses can be divided into to main groups, the adaptive immune response, in which an adaptation has taken place and in which ceils play a . dominant part and the innate immune response, which is available instantly and which primarily is based on molecules present in the body fluids. The innate immune system is operational at time of birth, in contrast to the adaptive immune defence which only during infancy obtains its full power of protecting the body (Janeway et a/., 1999). Bacteria entering the body at mucosal surfaces or through broken skin are immedi¬ately recognised by collectins, a family of soluble proteins that recognise distinctive carbohydrate configurations that are present on the surfaces of microbes and ab¬sent from the cells of the multicellular organism. Collectins thus belong to the large and diverse group of pattern recognition receptors of the innate immune system. In humans, three collectins are known, although others may exist: cows for example have more. Collectins target the particles to which they bind either for uptake by phagocytes or for activation of the complement cascade, and in these ways can mediate their destruction. Collectins all exhibit the following architecture: they have an N-terminal cysteine-rich region that appears to form inter-chain disulfide bonds, followed by a collagen-like region, an a-helical coiled-coil region and finally a C-type lectin domain which is the pattern-recognizing region and is referred to as the carbohydrate recognition domair (CRD). The name collectin is derived from the presence of both collagen ana lecnn domains. The ohelical coiled-coil region initiates trimerisatiori of the individual poly-petides to form collagen triple coils, thereby generating collectin subunits each con¬sisting of 3 individual polypeptides, whereas the N-terminal region mediates forma¬tion of oligomers of subunits. Different collectins exhibit distinctive higher order structures, typically either tetramers of subunits or hexamers of subunits. The grouping of large numbers of binding domains allows collectins to bind with high avidity to microbial cell walls, despite a relatively low intrinsic affinity of each individ¬ual CRD for carbohydrates. C-type CRDs are found in proteins with a widespread occurrence, both in phyloge-netic and functional perspective. The different CRDs of the different collectins en¬able them to recognise a range of distinct microbial surface components exposed on different microorganisms. The terminal CRDs are distributed in such a way that all three domain target surfaces that present binding sites has a spacing of approxi¬mately 53 A (Sheriff et a/., 1994; Weis & Drickamer, 1994). This property of 'pattern recognition' may contribute further to the selectively binding of microbial surfaces. The collagenous region or possibly the N-terminal tails of the collectins, are recog¬nised by specific receptors on phagocytes, and is the binding site for associated proteases that are activated to initiate the complement cascade upon binding of the CRD domain to a target Mannan-binding lectin (MBL) also termed mannose-binding lectin or mannose bind¬ing protein is a collectin which has gained great interest as an important part of the innate immune system. MBL binds to specific carbohydrate structures found on the surface of a range of microorganisms including bacteria, yeast, parasitic protozoa and viruses, and has been found to exhibit antibacterial activity through killing medi¬ated by activation of the terminal, lytic complement components or through promo¬tion of phagocytosis. MBL deficiency is associated with susceptibility to frequent infections by a variety of microorganisms in childhood, and possibly also in adults. . The CRD of MBL recognises preferentially hexoses with equatorial 3- and 4-OH groups, such as mannose, glucose, /V-acetyimannasamin and A/-acetyi glucoseamin while carbohydrates which do not fulfil this sterical requirement, such as galactose and D-fucose, are not bound (Weis et a/., 1992). The carbohydrate selectivity is ob- viously an important aspect of the self/non-self discrimination by MBL ana is prooa-bly mediated by the difference in prevalence of mannose and N-acetyl glucoseamin residues on microbial surfaces, one example being the high content of mannose'in the cell wall of yeasts such as Saccharomyces cerevisiae and Candida albicans. Carbohydrate structures in glycosylation of mammalian proteins are usually com¬pleted with sialic acid, which prevents binding of MBL to these oligomeric carbohy¬drates and thus prevents MBL recognition of 'self surfaces. Also, the trimeric struc¬ture of each MBL subunit may be of importance for target recognition. Complement is a group of proteins present in blood plasma and tissue fluid that aids the body's defences following an infection. The complement system is being acti¬vated through at least three distinct pathways, designated the classical pathway, the alternative pathway, and the MBLectin pathway (Janeway et a/., 1999). The classi¬cal pathway is initiated when complement factor 1 (C1) recognises surface-bound immunoglobulin. The C1 complex is composed of two proteolytic enzymes, C1r and C1s, and a non-enzymatic part, C1q, which contains immunoglobulin-recognising. domains. C1q and MBL shares structural features, both molecules having a bou¬quet-like appearance when visualised by electron microscopy. Also, like C1q, MBL is found in complex with two proteolytic enzymes, the mannan-binding lectin associ¬ated proteases (MASP). The three pathways all generate complement factor 3 (C3) convertase, which ensures the binding of C3b to the surface of the activating sur¬face, Le. the targeted microbial pathogen. Conversion of C3 into surface bound C3b is pivotal in the process of eliminating the microbial pathogen by phagocytosis or lysis (Janeway et a/., 1999). Certain O-antigen specific oligosaccharides of Salmonella have been reported to activate complement in C4-deficient guinea-pig serum and Salmonella serogroup C was later shown to react with MBL and hence activate complement by the MBLectin pathway, which is also termed the MBL pathway of complement activation or the lectin pathway. It has for some time.been speculated that the innate immune system may collabo¬rate with the adaptive immune system in the generation of specific immune re¬sponses as exemplified by the antibody response after infection or vaccination. Fearon's group have shown that the attachment of the C3d fragment of complement factor C3 onto a protein antigen through fusion by gene technology can in crease the immunogenecity of the antigen 1000 fold or more. Practical applications of this technique, or any number of modifications, are still awaited. The importance of the complement system for normal immune responses was first suggested by Pepys, who found impaired antibody responses to sheep erythrocytes, a thymus-dependent antigen, in mice that were C3-depleted with cobra venom fac¬tor. The idea of a link between innate and adaptive immunity was supported by re¬ports demonstrating reduced primary antibody responses to thymus dependent anti¬gens and impaired IgM to IgG switching in patients and experimental animals with deficiencies of C4, C2 and C3. The mechanism may involve the generation of C3-derived iigands for binding of antigen or antigen-containing complexes to comple¬ment receptors on B lymphocytes or antigen-presenting cells. Thus, blocking of CR1 (CD35) and CR2 (CD21) in mice with specific anti CR1 and anti-CR2 antibodies or with soluble receptor protein reduced antibody responses to immunisation and ex¬periments with CR1 and CR2-deficient knock-out mice show the requirement of these receptors for responses to thymus-dependent antigens. In addition, patients with leucocyte adhesion deficiency, who lack the CD11/CD18 adhesion molecule CR3, demonstrate impaired antibody responses and failure to switch from IgM to IgG. The C3-derived fragment C3d, a specific CR2 iigand, as mentioned above, show a strong dose-dependent adjuvant effect Deficiencies of the classical complement pathway (C1, C2, C4 and C3) are associ¬ated with infections by encapsulated bacteria. The main reason for this is probably the reduced efficiency of opsonic and bactericidal defence mechanisms caused by complement dysfunction. However, impaired immune responses to polysaccharide antigens might also be considered. The influence of complement on responses to thymus-independent antigens has not been extensively studied, and the available information is contradictory. Thus, low antibody responses to thymus-independent antigens have been clearly documented in C3-depleted mice and C3-deficient dogs. On the other hand, some reports find that C3-deficient patients appear to respond normally to immunisation with polysaccharide vaccines. Ficolins, like MBL, are lectins that contain a collagen-like domain. Unlike MBL, how¬ever, they have a fibrinogen-iike domain, which is similar to fibrinogen P- and y- chains. Ficolins also forms oligomers of structural subunits, each of which is com¬posed of three identical 35 kDa' polypeptides. Each subunit is composed of an amino-terminal, cysteine-rich region; a collagen-like domain that consists of tandem repeats of Gly-Xaa-Yaa triplet sequences (where Xaa and Yaa represent any amino acid); a neck region; and'a fibrinogen-like domain. The oligomers of ficolins com¬prises two or more subunits, especially a tetrameric form of ficolin has been ob¬served. Some of the ficolins triggers the activation of the complement system substantially in similar way as done by MBL. This triggering of the complement system results in the activation of novel serine proteases (MASPs) as described above. The fibrinogen-like domain of several lectins has a similar function to the CRD of C-type lectins including MBL, and hereby function as pattern-recognition receptors to discriminate pathogens from self. Serum ficolins have a common binding specificity for GlcNAc (N-acetyl-glucosamine), elastin or GalNAc (N-acetyl-galactosamine). The fibrinogen-like do¬main is responsible for the carbohydrate binding. In human serum, two types of fico¬lin, known as L-ficolin (P35, ficolin L, ficolin 2 or hucolin) and H-ficolin (Hakata anti¬gen, ficolin 3 or thermolabile b2-macroglycoprotein), have been identified, and both of them have lectin activity. L-ficolin recognises GlcNAc and H-ficolin recognises GalNAc. Another ficolin known as M-ficolin (P35-related protein, Ficolin 1 or Ficolin A) is not considered to be a serum protein and is found in leucocytes and in the lungs. L-ficolin and H-ficolin activate the lectin-complement pathway in association with MASPs. M-Ficolint L-ficolin and H-ficolin has calcium-independent lectin activ¬ity. MASPs (MBL-associated serine proteases) comprising MASP-1, MASP-2 and MASP-3 are proteolytic enzymes that are responsible for activation of the lectin pathway. The overall structure of MASPs resembles that of the two proteolytic com¬ponents of the first factor in the classical complement pathway, CI r and C1s. The lectin pathway is initiated when MBL or a ficolin associated with MASP-1, MASP-2, MASP-3 and sMAP binds to a carbohydrate structure of the surfaces-of e.g. bacte¬ria, yeast, parasitic protoxoa, viruses. MASP-2 is the enzyme component that - like C1s in the classical pathway - cleaves the complement components C4 and C2 to form the C3 convertase C4bC2a, which is common to both the lectin- and classical-pathway activation routes. MASP-1, MASP-2, MASP-3 and sMAP are encoded by two genes; sMAP is a trun¬cated form of MASP-2, and MASP-3 is produced from the MASP-1 gene by alterna¬tive splicing. The MASP-1 gene has an H-chain-encoding region that is common to MASP-1 and MASP-3, which is followed by tandem repeats of protease-domain-encoding regions that are specific to MASP-3 and MASP-1. The MASP family can be divided into two phylogenetic lineages - TCN-type and AGY-type lineages. The TCN-type lineage, which includes MASP-1, has a TCN co-don (where N denotes A, G, C or T) that encodes the active-site serine, the pres¬ence of a histidine-loop disulphide bridge and split exons. By contrast, the AGY-type lineage, which includes MASP-2, MASP-3, C1r and C1s, is characterised by an AGY codon (where Y denotes C or T) that encodes the active-site serine, the ab¬sence of a histidine-loop and a single exon. MASP-1, MASP-2, MASP-3, C1r and C1s consist or six domains: two C1r/C1s/Uegf/bone morphogenetic protein 1 (CUB) domains; an epidermal growth factor (EGF)-like domain; two complement control protein (CCP) domains or short consensus repeats (SCRs), and a serine-protease domain. Histidine (H), aspartic acid (D) and serine (S) residues are essential for the formation of the active centre in the serine-protease domain. Only MASP-1 has two additional cysteine residues in a light chain, which form a histidine.loop disulphide bridge (S-S), as is found in tryp¬sin andchymotrypsin. On binding of MBL and ficolins to carbohydrate on the-surface of a pathogen, the pro-enzyme form of a MASP is cleaved between the second CCP and the protease domain, which results in an active form that consists of two poly¬peptides - heavy and light chains (also known as A and B chains). Summary of invention . The present invention relates to fusion proteins capable of activating the comple¬ment system. Accordingly, the present invention relates to a fusion protein.compris¬ing a first polypeptide sequence derived from a lectin-complement pathway activating . protein (=cornplement activating protein) or a functional homoiogue thereof; and a second polypeptide sequence derived from a coliectin or a functional homoiogue thereof; wherein said complement activating protein is not a coliectin. The fusion protein is suitable for use in treatment consisting of creation, reconstitu-tion, enhancing and/or stimulating the opsonic and/or bactericidal activity of the complement system, i.e. enhancing the ability of the immune defence to recognise and kill microbial pathogens, and accordingly, the invention relates to a medicament comprising the fusion protein. Also, in another aspect the invention relates to a method of treatment of a clinical condition in an individual in need thereof comprising administering to said individual the fusion protein as defined above. In another aspect the invention relates to a method of treatment or prophylaxis of a clinical condition, such as infection, in an individual in need thereof comprising ad¬ministering to said individual a the fusion protein a first polypeptide sequence de¬rived from a protein capable of forming oligomers of structural units; and -a second polypeptide sequence derived from a mannose binding lectin (MBL, wherein said first polypeptide sequence and said second peptide sequence is not derived from the same protein, and said fusion protein is capable of associating with mannose-associated serine protease (MASP). The first polypeptide sequence is preferably derived from a protein capable of forming tetramers, pentamers, and/or hexamers of a structural unit. In a preferred embodiment the first polypeptide se¬quence and the second polypeptide sequence are as described below. In a further aspect the invention relates to use of the fusion protein as defined above for the preparation of a medicament for the treatment of a clinical condition in an individual in need thereof. Furthermore the invention relates to a method for producing the fusion protein, as well as an isolated nucleic acid sequence encoding the fusion protein, a vector comprising the sequence and a cell comprising the vector. Drawings Figure 1 shows the sequence of L ficolin Figure 2 shows the sequence of MBL • Figure 3 shows an example of a fusion protein Figures 4-8 show plasmids as described in Example 1 Figure 9 shows an alignment of fusion proteins described in Example 1 Figure 10 shows two Western blots as discussed in Example 2. Definitions Collectins: A family of structurally related, carbohydrate-recognising proteins of in¬nate immunity, including mannan-binding lectin (MBL) and surfactant proteins A and D. The name refers to the .presence of a collagen-like region and a C-type lectin domain. Complement A group of proteins present in blood plasma and tissue fluid that aids the body's defences following an infection. Complement is involved in destroying foreign cells and attracting phagocytes to the area of conflict in the body. Conjugated: An association formed between two compounds for example between an immunogenic determinant and a collectin and/or collectin homologue or between an immunogenic determinant and a saccharide. The association may be a physical association generated e.g. by the formation of a chemical bond, such as e.g. a co-valent bond. ' CRD: Carbohydrate recognition domain, a C-type lectin domain that is found at the C-terrninus of collectins. Immunogenic determinant: A molecule, or a part thereof, containing one or more epitopes that will stimulate the immune system of a host organism to make a secre- tory, humoral and/or cellular antigen-specific response, or a DNA molecule which is capable of producing such an immunogen in a vertebrate. Immune response: Response to a immunogenic composition comprising an immu¬nogenic determinant An immune response involves the development in the host of a cellular- and/or humoral immune response to the administered composition or vaccine in question. An immune response generally involves the action of one or more of i) the antibodies raised, ii) B cells, iii) helper T cells, iv) suppressor T cells, v) cytotoxic T cells and iv) complement directed specifically or unspeciftcally to an immunogenic determinant present in an administered immunogenic composition. Lectin: Proteins that specifically bind carbohydrates. MASP: Mannose-associated serine protease MBL: Mannan-binding lectin or mannose-binding lectin. Subunit complex=structural unit: complex of three individual fusion proteins, like the subunit complex discussed above for MBL and ficoiins. Detailed description of the invention An object of the present invention is to provide afusion protein capable of activating the complement system in order to aid in preventing or treating diseases, in particu¬lar infectious diseases. The fusion protein is composed of a first polypeptide sequence derived from a lectin-complement pathway activating protein (=compiement activating protein) or from a functional homologue thereof; and a second polypeptide sequence derived from a coilectin or from a functional homo¬logue thereof; wherein said complement activating protein is not a collectin. By combining-a polypeptide sequence derived from a lectin-complement pathway activating protein and a polypeptide sequence derived from a collectin it is possible to design a fusion protein having binding affinity for a variety of carbohydrates, pref¬erably bacterial and viral carbohydrates and at the same time having complement system activating activity. First polypeptide sequence The first polypeptide sequence may be derived from any lectin-complement path¬way activating protein. Said lectin-complement pathway activating protein may be naturally occurring lectin-complement pathway activating protein as well as variants or homologues to said lectin-complement pathway activating proteins, wherein said variants or homologues have maintained the lectin-complement pathway activating activity. It is preferred that the fusion protein is capable of forming subunit complexes, each consisting of 3 individual fusion proteins as defined above. Also the first polypeptide sequence is preferably capable of forming oligomeric com¬plexes with the first polypeptide sequence of another fusion protein, wherein said another fusion protein may be identical to the first fusion protein. Thereby an oli¬gomeric complex of two or more fusion proteins or two or more subunit complexes may be provided, said oligomeric complex having a higher binding avidity for bacte¬ria! or viral carbohydrates than the monomeric fusion protein. In a preferred em¬bodiment the oligomeric complex is a dimeric subunit complex, more preferably a trimeric subunit complex, more preferably a tetrameric subunit complex. In a preferred, embodirhent the lectin-complement pathway activating protein .is a ficolin as defined above. Said ficolin may be L-ficolin, H-ficolin or M-ficolin or vari¬ants or homologues thereof. In a preferred embodiment the lectin-complement pathway activating protein is L-ficoiin. In another embodiment the first polypeptide sequence comprises me TiDnnogen ao-main of the lectin, and/or the neck region of a lectin, such as a ficolin or a homo¬logue or a variant thereof. When the first polypeptide sequence is derived from ficolin or from a variant or a homologue of ficolin, it is preferred that the first polypeptide sequence comprises the collagen-like domain from ficolin or from a variant or homologue of ficolin. In another embodiment it is preferred that the first polypeptide sequence comprises the Cystein rich domain from ficolin or from a variant or homologue of ficolin. it is even more preferred that the first polypeptide sequence comprises the collagen-like domain and the Cystein rich domain from ficolin or from a variant or homologue of ficolin. It is more preferred that the first polypeptide sequence comprises the collagen-like domain from L-ficolin or from a variant or homologue of L-ficolin. In another em¬bodiment it is more preferred that the first polypeptide sequence comprises the Cystein rich domain from L-ficolin or from a variant or homologue of L-ficolin. It is even more preferred that the first polypeptide sequence comprises the N-terminal region of L-ficolin including two Cystein amino acid residues. It is even more preferred that the first polypeptide sequence comprises the collagen¬like domain and the Cystein rich domain from L-ficolin or from a variant or homo¬logue of L-ficolin. In a particular preferred embodiment the ficolin has one of the sequences listed be¬low with reference to their database and accession No. For each of the sequences the Cystein rich region and the collagen-like region is described. NP_003656. ficolin 3 precursor; ficolin (collagen/fibrinogen domain-containing) 3 (Hakata antigen) [Homo sapiens] [gi:4504331] 90..299 /region_name="pfam00147, fibrinogen_C, Fibrinogen beta and gamma chains, C-terminal globular domain" 90..299 /region jiame="smart00186, FBG, Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous" 1 mdllwilpsl wllllggpac Iktqehpscp gpreleaskv vllpscpgap gspgekgapg 61 pqgppgppgk mgpkgepgdp vnllrcqegp rncreilsqg atlsgwyhlc Ipegralpvf 121 cdmdtegggw Ivfqrrqdgs vdffrswssy ragfgnqese fwlgnenlhq Itlqgnwelr 181 veledfngnr tfahyatfrl Igevdhyqla Igkfsegtag dslslhsgrp fttydadhds 241 snsncavivh gawwyascyr snlngryavs daaahkygid wasgrgvghp yrrvrmmlr XPjl 16792. similar to Ficoiin 2 precursor (Collagen/fibrinogen domain-containing protein 2) (Ficoiin-B) (Ficoiin B) (Serum lectin P35) (EBP-37) (Hucolin) (L-Ficolin) [Homo sapiens] [gi:20477458] 91..168 /region_name=npfam00147, fibrinogen_C, Fibrinogen beta and gamma chains, C-terminal globular domain" gi-.ies/region^name^'smartOOIse, FBG, Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous" 1 mgpallalsf Iwtmaltedt cpamleyval nsepgmaskn psrrhglsll vvdqgpgarg 61 vrtdqgpsga dpgslelhge cpifpseqvi Ithhnnypfs tedqdndrda encavhyqga 121 wwyaschlsh Ingvylggar dsftnginwk sgkgnnysyk vsemkvrpt 000602. Ficoiin 1 precursor (Collagen/fibrinogen domain-containing protein 1) (Fi-colin-A) (Ficoiin A) (M-Ficolin) [gi:20455484] 1..29 /gene=MFCN1" /region_name="Signar /note="POTENTlAL" 30..326 /gene="FCN1" /region_name="Mature chain" /note="FICOLIN 1." 55..93 /gene="FCN1" /region_name=MDomain" /note="COLLAGEN-LIKE." 133 /gene="FCN1" /region_name="Conflict" /note=T -> N (IN REF. 1)." 144..290 /gene=TCN1" /region_name="DomainH /note="FIBRINOGEN C-TERMINAL" 287 /gene="FCN1" /region_name="Conflict" /note="N -> S (IN REF. 1)." 305 /gene="FCN1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (PO¬TENTIAL)." 1 melsgatmar glavllvlfl hiknlpaqaa dtcpevkwg legsdkltil rgcpglpgap 61 gpkgeagvig ergerglpga pgkagpvgpk gdrgekgmrg ekgdagqsqs catgprnckd 121 lldrgyflsg whtiylpdcr pltvlcdmdt dgggwtvfqr rmdgsvdfyr dwaaykqgfg 181 sqlgefwlgn dnihaltaqg sselrvdlvd fegnhqfaky ksfkvadeae kyklvlgafv 241 ggsagnsltg hnnnffstkd qdndvsssnc aekfqgawwy adchasnlng lylmgphesy 301 anginwsaak gykysykvse mkvrpa // 075636. Ficoiin 3 precursor (Collagen/fibrinogen domain-containing protein 3) (Collagen/fibrinogen domain-containing lectin 3 P35) (Hakata antigen) [gi:13124185 1..21 /gene="FCN3H /region_name="Signar /note="POTENT!ALn 22..299 /gene="FCN3" /region_name=H Mature chain" /note="FICOLIN 3." 48.. 80 /gene="FCN3" /region_name="Domain" /note=nCOLLAGEN4JKE.n 50 /gene="FCN3" /site_type="hydroxylation" 53 /gene="FCN3" /siteJype="hydroxylation" 59 /gene="FCN3" /siteJype="hydroxylation" 65 /gene="FCN3" /siteJype="hydroxylation" 68 /gene="FCN3" /site_type="hydroxylation" 77 /gene="FCN3" /siteJype="hydroxylation" 19..265 /gene="FCN3" /region name="Domain" /note="FIBRINOGEN C- ERMINAL" 89 /gene="FCN3" /site type="glycosylation" /note="N-LINKED (GLCNAC.) (PO- "ENTIAL)." 1 mdllwilpsl wllllggpac Iktqehpscp gpreleaskv vllpscpgap gspgekgapg 61 pqgppgppgk mgpkgepgdp vnllrcqegp rncrellsqg atlsgwyhlc Ipegralpvf 121 cdmdtegggw Ivfqrrqdgs vdffrswssy ragfgnqese fwlgnenlhq Itlqgnwelr 181 veledfngnr tfahyatfrl lgevdhyqla Igkfsegtag dslslhsgrp fttydadhds 241 snsncavivh gawwyascyr snlngryavs daaahkygid wasgrgvghp yrrvrmmlr XP_13Q120. similar to Ficolin 2 precursor (Collagen/fibrinogen domain-containing protein 2) (Ficolin-B) (Ficolin B) (Serum lectin P35) (EBP-37) (Hucolin) [Mus mus- culus] [gi:20823464] . • 59..95 /region_name=,lCollagen triple helix repeat (20 copies)* /note="CoIlagen" /db xref="CDD:pfam0139T' 59..89 /region_name="Collagen triple helix repeat (20 copies)" /note="CoIiagen" /db xref=,tCDD:Dfam01391H 60..95 /region_name="ColIagen triple helix repeat (20 copies)" /note=,,CoIlagen" /db_xref=MCDD:efam01391" 60..95 /regionjiame="Collagen triple helix repeat (20 copies)" /note="Collagen" /db_xref=XDD:EfanT01391" 60..95 /region_name="Collagen triple helix repeat (20 copies)" /note-'Collagen" /db xref="CDP:pfam0139T' 60..95 /region_name="Collagen triple helix repeat (20 copies)'1 /note="Collagen" /db xref=BCDD:pfam01391" 60..95 /region_name="CoIlagen triple helix repeat (20 copies)" /note="Collagen" /db xref="CDD:pfam0139r 61..95 /region_name="Collagen triple helix repeat (20 copies)" /note=HCollagen" /db xref="CDD:pfam01391" 61..95 /regionjiame="Collagen triple helix repeat (20 copies)" /note-'Collagen" /db xref="CPD:pfam01391" 61 ..95 /region_name="Collagen triple helix repeat (20 copies)" /note="Collagen" /db xref="CDD:pfam01391" 103..312 /regionjtarne="Fibrinogen beta and gamma chains, C-terminai globular . domain" /note="fibrinogen_CH /db xref="CDD:pfam0014r 103..312 /regionjiame="Fibrinogen-related domains (FReDs)" /note="FBG" /db xref="CDD:smart00186" 1 malgsaalfv Itltvhaagt cpelkvldle gykqltilqgcpglpgaagp kgeagakgdr 61 gesglpgipg kegptgpkgn qgekgirgek gdsgpsqsca tgprtckell tqghfltgwy 121 tiylpdcrpl tvlcdmdtdg ggwtvfqrrl dgsvdffrdw tsykrgfgsq Igefwlgndn 181 ihalttqgts elrvdlsdfe gkhdfakyss fqiqgeaeky klilgnflgg gagdsltphn 241 nrlfstkdqd ndgstsscam gyhgawwysqchtsnlngly Irgphksyan gvnwkswrgy 301 nysckvsemk vrli NPJ356654. ficolin 2%isoform d precursor; ficolin (collagen/fibrinogen domain-containing lectin) 2 (hucolin); ficolin (collagen/fibrinogen domain-containing lectin) 2; hucolin [Homo sapiens] [gi:8051590] 39..95 /region_name="collagen-like domain" 1 meldravgvi gaatlllsfl gmawalqaad tcpevkmvgl egsdkltilr gcpglpgapg 61 dkgeagtngk rgergppgpp gkagppgpng apgepqpcitgd IMPJD56653. ficolin 2 isoform c precursor; ficolin (collagen/fibrinogen domain-containing lectin) 2 (hucolin); ficolin (collagen/fibrinogen domain-containing lectin) 2; hucolin [Homo sapiens] [gi:8051588] 39..95 /region_name=McolIagen-like domain" 102..143 /regionjiame="Fibrinogen beta and gamma chains, C-terminal globular domain" /note="fibrinogenJ3" /db xref="CPD:pfam00147w 102..143 /regionjiame="Fibrinogen-related domains (FReDs)" /note="FBG" /db xref="CDD:smart00186" 1 meldravgvi gaatlllsfl gmawalqaad tcpevkmvgl egsdkltilr gcpglpgapg 61 dkgeagtngk rgergppgpp gkagppgpng apgepqpclt gprtckdlld rghflsgwht 121 iylpdcrplt vlcdmdtdgg gwtvsvglgr ggqpgspggq aahlvgehtl efsillvgds 181 qr NPJD56652. ficolin 2 isoform b precursor; ficolin (collagen/fibrinogen domain-containing lectin) 2 (hucolin); ficolin (collagen/fibrinogen domain-containing lectin) 2; hucolin [Homo sapiens] [gi:8051586] sig peptide 1..25 mat peptide 26..275 60..275/region_name="FBG domain"/note="fibrinogen beta/gamma homology" 64..275 /region_name="Fibrinogen-related domains (FReDs)" /note="FBG" /db xref="CDD:smart00186n 64..274 /region_name="Fibrinogen beta and gamma chains, C-terminal globular domain" /note=nfibrinogen_C" /db xref="CDD:pfam00147n 1 meldravgvi gaatlllsfl gmawalqaad tcpgergppg ppgkagppgp ngapgepqpc 61 Itgprtckdl Idrghflsgw htiylpdcrp Itvlcdmdtd gggwtvfqrr vdgsvdfyrd 121 watykqgfgs rlgefwlgnd nihaltaqgt selrvdlvdf ednyqfakyr sfkvadeaek 181 ynlvlgafve gsagdsltfh nnqsfstkdq dndlntgnca vmfqgawwyk nchvsnlngr 241 ylrgthgsfa nginwksgkg ynysykvsem kvrpa NP_001994. ficolin 1 precursor; ficolin (collagen/fibrinogen domain-containing) 1 [Homo sapiens] [gi:8051584] sig peptide 1..27 mat peptide 28..326 40..108 /region_name="collagen-like domain" 50..105 /region_name="Collagen triple helix repeat (20 copies)" /note=MCoIlagen" /db xref=,,CDD:pfam01391" 51 ..107 /region__name="Collagen triple helix repeat (20 copies)" /note^Collagen" /db xref="CDD.:pfam01391" . 52..106 /region jiame="Collagen triple helix repeat (20 copies)" /note="Collagen" /db xref="CDD:pfam01391" 115..326 /regionjiame="FBG domain" /note=,lfibrinogen beta/gamma homology" 115.-326 /region_name="Fibrinogen-related domains (FReDs)" /note="FBG" /db xref="CDD:smart00186n 15..325 /region_name="Fibrinogen beta and gamma chains, C-terminai gioDuiai omain" /note="fibrinogen_C,f /db xref=nCDD:pfam00147" variation 315 db xref="dbSNP:1128428" variation 316/db xref="dbSNP: 1128429" variation 317 db xref="dbSNP: 1128430" 1 melsgatmar glavllvlfl hiknlpaqaa dtcpevkwg legsdkltil rgcpglpgap 61 gpkgeagvig ergerglpga pgkagpvgpk gdrgekgmrg ekgdagqsqs catgprnckd 121 lldrgyflsg whtiylpdcr pltvlcdmdt dgggwtvfqr rmdgsvdfyr dwaaykqgfg 181 sqlgefwlgn dnihaltaqg sselrvdlvd fegnhqfaky ksfkvadeae kyklvlgafv 241 ggsagnsltg hnnnffstkd qdndvsssnc aekfqgawwy adchasnlng lylmgphesy 301 anginwsaak gykysykvse mkvrpa NPJ304099. ficolin 2 isoform a precursor; ficolin (collagen/fibrinogen .domain-containing lectin) 2 (hucolin); ficolin (collagen/fibrinogen domain-containing lectin) 2; hucolin [Homo sapiens] [gi:4758348] sig peptide 1..25 mat peptide 26,.313 39..95 /region_name="collagen~Iike domain" 98..313 /region_name="FBG domain" /note="fibrinogen beta/gamma homology" 102..313 /region_name=Tibrinogen-related domains (FReDs)" /note=nFBG" /db xref="CDD:smart00186" 102..312 /region_name="Fibrinogen beta and gamma chains, C-terminai globular domain" /note=ufibrinogen_C" /db xref="CDD:pfam00147 1 meldravgvl gaatlllsfl gmawalqaad tcpevkmvgl egsdkltilr gcpglpgapg 61 dkgeagtngk rgergppgpp gkagppgpng apgepqpclt gprtckdlld rghflsgwht 121 iylpdcrplt vlcdmdtdgg gwtvfqrrvd gsvdfyrdwa tykqgfgsri gefwlgndni 181 haitaqgtse Irvdlvdfed nyqfakyrsf kvadeaekyn Ivlgafvegs agdsltfhnn 241 qsfstkdqdn dlntgncavm fqgawwyknc hvsnlngryl rgthgsfang inwksgkgyn 301 ysykvsemkv rpa Q9WTS8. Ficolin 1 precursor (Collagen/fibrinogen domain-containing protein 1) (Fh colin-A) (Ficolin A) (M-Ficolin) [gi:13124116] 1..22 /gene="FCN1" /region jiame="Signar/note=TOTENTlALn 23..335 /gene="FCN1" /regionjiame="Mature chain" /note="Fl COLIN 1." 50..88 /gene="FCN1" /region_name="DomainM /note="COLLAGEN-LlKE.B 152..298 /gene="FCN1" /regionjiame^Domain" /note="FlBRINOGEN C-TERMINAL" 271 /gene="FCN1" /siteJype="glycosylationn /note="N-UNKED (GLCNAC.) (PO¬TENTIAL)." 1 mwwpmlwafp vllclcssqa Igqesgacpd vkivglgaqd kvaviqscps fpgppgpkge 61 pgspagrger glqgspgkmg ppgskgepgt mgppgvkgek gergtasplg qkelgdalcr' 121 rgprsckdll trgifltgwy tiylpdcrpl tvlcdmdvdg ggwtvfqrrv dgsinfyrdw 181 dsykrgfgnl gtefwlgndy Ihlltangnq elrvdirefq gqtsfakyss fqvsgeqeky 241 kltlgqfleg.tagdsltkhn nmafsthdqd ndtnggknca alfhgawwyh dchqsnlngr 301 ylpgshesya dginwlsgrg hrysykvaem kiras Q15485. Ficolin 2 precursor (Collagen/fibrinogen domain-containing protein 2) (Fi-colin-B) (Ficolin B) (Serum lectin P35) (EBP-37) (Hucolin) (L-Ficolin) [gi:13124203] 1 ..25 /gene="FCN2" /region_name="Signal" /note="PU I tN i IAL." 26..313 /gene="FCN2" /region_name="Mature chain" /note="FICOLIN 2." 54..92 /gene="FCN2" /regidn_name="Domain" /note^'COLLAGEN-UKE." 131 ..277 /gene="FCN2" /region name="Domain" /note="FIBRINOGEN C-TERMINAL" 240 /gene="FCN2" /site_type="glycosylation- /note="N-LINKED (GLCNAC.) (PO¬ TENTIAL)." 300 /gene="FCN2" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (PO¬ TENTIAL)." 1 meldravgvl gaatlllsfl gmawalqaad tcpevkmvgl egsdkitilr gcpglpgapg 61 dkgeagtngk rgergppgpp gkagppgpng apgepqpclt gprtckdlld rghflsgwht 121 iylpdcrplt vlcdmdtdgg gwtvfqrrvd gsydfyrdwa tykqgfgsrl gefwigndni 181 haltaqgtse Irvdlvdfed nyqfakyrsf kvadeaekyn Ivigafvegs agdsltfhnn 241 qsfstkdqdn dlntgncavm fqgawwyknc hvsnlngryl rgthgsfang inwksgkgyn 301 ysykvsemkv rpa 070497. Ficolin 2 precursor (Collagen/fibrinogen domain-containing protein 2) (Fi-colin-B) (Ficolin B) (Serum lectin P35) (EBP-37) (Hucolin) [gi:13124181] 306 /gene="FCN2" /region_name="Mature chain" /note="FICOLIN 2." 41..79 /gene="FCN2" /region_name="Domain" /note="COLLAGEN-LIKE." 130..276 /gene="FCN2" /region_name="Domain" /note="FIBRINOGEN C-TERMINAL." 299 /gene="FCN2" /site_type=nglycosylation" /note="N-LINKED (GLCNAC.) (PO¬TENTIAL)." 1 Igsaalfvlt Itvhaagtcp elkvldlegy kqltilqgcp glpgaagpkg eagakgdrge 61 sglpgipgke gptgpkgnqg ekgirgekgd sgpsqscatg prtckelltq ghfltgwyti 121 ylpdcrpmtv Icdmdtdggg wtvfqrrldg svdffrdwts ykrgfgsqlg efwlgndnih 181 alttqgtsel rvdlsdfegk hdfakyssfq iqgeaekykl ilgnflggga gdsltphnnr 241 Ifstkdqdnd gstsscamgy hgawwysqch tsnlnglylr gphksyangv nwkswrgyny 301 sckvse 070165. Ficolin 1 precursor (Collagen/fibrinogen domain-containing protein 1) (Fi-colin-A) (Ficolin A) (M-Ficolin) [gi:13124179] 1 ..22 /gene="FCN1" /region_name="Signaln /note^POTENTIAL" 23..334 /gene="FCN1" /region_name="Mature chain" /note="FICOLIN 1." 50..88 /gene="FCN1" /region_name="Domain" /note="COLLAGEN-LlKE." 152..298 /gene="FCN1" /region_name="Domain" /note="FIBRINOGEN C-TERMINAL" 261 /gene="FCN1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (PO¬TENTIAL)." 1 rhqwptlwafs gllclcpsqa Igqergacpd vkwglgaqd kwviqscpg fpgppgpkge 61 pgspagrger gfqgspgkmg pagskgepgt mgppgvkgek gdtgaapsig ekelgdtlcq 121. rgprsckdll trgifltgwy tihlpdcrpl tvlcdmdvdg ggwtvfqrrv dgsidffrdw 181 dsykrgfgnl gtefwlgndy Ihlltangnq elrvdlqdfq gkgsyakyss fqvseeqeky 241 kltlgqfleg tagdsltkhn nmsftthdqd ndansmncaa Ifhgawwyhn chqsnlngry 301 Isgshesyad ginwgtgqgh hysykvaemk iras D57756. Ficolin 2 precursor (Collagen/fibrinogen domain-containing protein */ 1 ..22 /gene="FCN2" /region_name="Signai" /note="POTENTlAL" 23..319 /gene="FCN2rt /region_name=="Mature chain" /note="FICOLIN 2." 48..86 /gene="FCN2" /region_name="Domain,, /note="COLLAGEN-LIKE." 137..283 /gene=nFCN2"7region_name="Domain" /note="FIBRINOGEN C-TERMINAL" 306 /gene=nFCN2" /site_type=ngIycosy!ation" /note="N-L!NKED (GLCNAC.) (PO¬TENTIAL)." 1 mvlgsaaifv Isicvteltl haadtcpevk vldlegsnkl tilqgcpglp galgpkgeag 61 akgdrgesgl pghpgkagpt gpkgdrgekg vrgekgdtgp sqscatgprt ckelftrgyf 121 Itgwytiylp dcrpltvicd mdtdgggwtv fqrridgtvd ffrdwtsykq gfgsqlgefw 181 Igndnihalttqgtnelrvd.ladfdgnhdf akyssfqiqg eaekyklilg nflgggagds 241 Itsqnnmlfs tkdqdndqgs sncavryhga wwysdchtsn Inglylrglh ksyangvnwk 301 swkgynysyk vsemkvrli JC5980: ficolin-A precurs - mouse [gi:7513652] 1..21 /region jiame="domain"/note="signal sequence" 50..64 /regionjiame="domain" /note="collagen-Iike" 68..106 /region_name=Hdomain" /note="colIagen-like" 123..334/region_name=ndomain" /note="fibrinogen beta/gamma homology #label FBG" 1 mqwptlwafs gllclcpsqa lgqergacpd vkwglgaqd kvwiqscpg fpgppgpkge 61 pgspagrger gfqgspgkmg pagskgepgt mgppgvkgek gdtgaapslg ekelgdtlcq 121 rgprsckdll trgifltgwy tihlpdcrpl tvlcdmdvdg ggwtvfqrrv dgsidffrdw 181 dsykrgfgnl gtefwlgndy Ihlltangnq elrvdlqdfq gkgsyakyss fqvseeqeky 241 kltlgqfleg tagdsltkhn nmsftthdqd ndansmncaa tfhgawwyhn chqsnlngry 301 Isgshesyad ginwgtgqgh hysykvaemk iras S61517. ficolin-1 precurs-human [gi:2135116] 1..326 /note="36K HLA-cross-reactive plasma protein; hucolin, 35K" 1..22 /region_name="domainn /note="signal sequence" 52..108 /regionjiame="region" /note="collagen-like" 115..326 /region_name=ndomain" /note="fibrinogen beta/gamma homology #label FBG" 305 /site_type="binding" /note="carbohydrate (Asn) (covalent)" 1 melsgatmarglavllvlfl hiknlpaqaa dtcpevkwg legsdkltil rgcpglpgap 61 gpkgeagvig ergerglpga pgkagpvgpk gdrgekgmrg ekgdagqsqs catgpmckd 121 lldrgyflsg whniylpdcr pltvlcdmdt dgggwtvfqr rmdgsvdfyr dwaaykqgfg 181 sqlgefwlgn dnihaltaqg sselrvdlvd fegnhqfaky ksfkvadeae kyklvlgafv 241 ggsagnsltg hnnnffstkd qdndvsssnc aekfqgawwy adchasslng lylmgphesy 301 anginwsaak gykysykvse mkvrpa A47172. transforming growth factor-beta 1-binding protein homolog ficolin-alpha -pig [gi:423206] 112..323 /region_name="domain" /note="fibrinogen beta/gamma.homology #Iabel FBG" 1 mdtrgvaaam rplvllvafl ctaapaldtc pevkvvgleg sdklsilrgc pglpgaagpk 61 geagasgpkg gqgppgapge pgppgpkgdr gekgepgpkg esweteqclt gprtckellt 121 rghilsgwht iylpdcqplt vlcdmdtdgg gwtvfqrrsd gsvdfyrdwa aykrgfgsql 181 gefwlgndhi haltaqgtne Irvdlvdfeg nhqfakyrsf qvadeaekym Ivigafvegn 241 agdsltshnn slfttkdqdn dqyasncavl yqgawwynsc hvsnlngryl ggshgsfang 301' vnwssgkgyn ysykvsemkf rat JC4942. ficoiin-1 precursor- human [gi:2135117] 1.22 /region_name=Mdomain" /note="signal sequence" 45.. 101 /regianjiame^'YegionVnote^'collagen-like' 108..319 /region_name=Mdomainn /note="fibrinogen beta/gamma homology #label FBG" 111 ..315 /region_name=nregionM /note="fibrinogen-like" 298 /site_type="binding" /note="carbohydrate (Asn) (covalent)" 1 marglavllv Iflhiknlpa qaadtcpevk vvglegsdkl tilrgcpglp gapgpkgeag 61 vigergergl pgapgkagpv gpkgdrgekg mrgekgdagq sqscatgprn ckdlldrgyf 121 Isgwhtiylp dcrpltvlcd mdtdgggwtv fqrrmdgsvd fyrdwaaykq gfgsqlgefw 181 Igndnihalt aqgsselrvd Ivdfegnhqf akyksfkvad eaekykMg afvggsagns 241 Itghnnnffs tkdqdndvss sncaekfqga wwyadchasn Inglylmgph esyanginws 301 aakgykysyk vsemkvrpa AAF44911. symbbl=BG:DS00929...[gi:7287873] 1 mkscffvlfl wtllfevgqs sphtcpsgsp ngihqlmlpe eepfqvtqck tlardwiviq 61 rrldgsvnfn qswfsykdgf gdpngeffig iqklyimtre qphelfiqlk hgpgatvyah 121 fddfqvdset elyklervgk ysgtagdslr yhinkrfstf drdndesskn caaehgggww 181 fhsclsr The first polypeptide preferably comprises at least 10, such as at least 12, for exam¬ple at least .15, such as at least 20, for example at least 25, such as at least 30, for example at least 35, such as at least 40, for example at least 50 consecutive amino acid residues of the complement activating protein or of a variant or a homologue to said protein. Such a variant or homologue is preferably at least 70%, such as 80%, for example 90%, such as 95% identical to the complement activating protein. The first polypeptide sequence of the fusion protein is preferably capable of activat¬ing the lectin-complement pathway when bound directly or indirectly to a target, such as a bacteria or a virus. In a preferred embodiment the first polypeptide se¬quence is capable of associating-with at least one MASP protein, such as a MASP protein selected from the group consisting of MASP-1, MASP-2 and MASP-3 or functional homologues or variants hereof. In particular the first polypeptide is capa¬ble of associating with said at least one MASP protein when being part of the fusion >rotein. Thereby the first polypeptide sequence is capable or proviaing me ILKXUU protein with complement system activating activity. In a particular preferred embodiment the first polypeptide sequence comprises at least the amino acid residues corresponding to 1-54 of L-ficolin sequence of Figure 1, such as 1-55 of L-ficolih sequence of Figure 1, such as 1-69 of L-ficolin sequence of Figure 1, such as 1-77 of L-ficolin sequence of Figure 1, such as 1-90 of L-ficolin sequence of Figure 1, such as 1-93 of L-ficolin sequence of Figure 1, such as 1-131 of L-ficolin sequence of Figure 1, such as 1-207 of L-ficolin sequence of Figure 1. In particular the first polypeptide sequence comprises the amino acid residues selected from: 1-55 of L-ficolin sequence of Figure 1, 1-54 of L-ficolin sequence of Figure 1, 1-50, or 1-77 of L-ficolin sequence of Figure 1. In a more preferred embodiment the first polypeptide sequence has the amino acid residues selected from: 1-55 of L-ficolin sequence of Figure 1,1-54 of L-ficolin sequence of Figure 1, 1-50, or 1-77 of L-ficolin sequence of Figure 1. In another embodiment the first polypeptide se¬quence comprises at least the amino acid residues corresponding to 60-90 of L-ficolin sequence of Figure 1, such as 55-90 of L-ficolin sequence of Figure 1, such as 54-92 of L-ficolin sequence of Figure 1. ■ It is preferred the first polypeptide sequence and the second polypeptide sequence are selected to include the motif X-X-G'-X-X-G at least 5 times, such as at least 7 times, preferably in a consecutive sequence. It is more preferred to select the first polypeptide sequence and the second polypeptide sequence so that the aforemen¬tioned motif is substituted once with the motif X-X-G-X-G. In the motifs X means any amino acid different from Glycine, and G means Glycine. Second polypeptide sequence The second polypeptide sequence is preferably capable of associating with one or more carbohydrates. This may be accomplished by incorporating at least the carbo¬hydrate recognizing domain of the collectin in question. Accordingly, the second polypeptide sequence preferably comprises the CRD domain of a collectin or a homologue or a variant thereof. Preferably the collectin is selected from the group consisting 01 IVIDU yiiai nIUOC-binding lectin), SP-A (lung surfactant protein A), SP-D (lung surfactant protein D), BK (or BC, bovine conglutinin) and CL-43 (collectin-43). Most preferably the collectin is MBL. In a particular preferred embodiment the collectin has one of the sequences listed below with reference to their database and accession No. Collectins SEQ ID NO: 42 Q9NPY3 Complement component C1q receptor precursor (Complement component 1, q subcomponent, receptor 1) (C1qRp) (C1qR(p)) (C1q/MBL/SPA receptor) (CD93 antigen) (CDw93) gi|21759074|sp|Q9NPY3|CD93_HUMAN[21759074] FEATURES Location/Qualifiers source 1..652 /organism="Homo sapiens" /db_xref="taxon:9606" gene 1 ..652 /gene="C1 QR1" /note="CD93" Protein 1..652 /gene="C1QR1" /product-'Complement component C1q receptor precursor" Region 1...21 /gene="C1QR1"/region_name="Signal" Region 22..652/gene=nC1QR1"/region_name="Mature chain" /note="COMPLEMENT COMPONENT C1Q RECEPTOR." Region 22 /gene="C1QR1" /region_name="Conflict" /note="T -> V (IN AA SE¬QUENCE)." Region 24..580 /gene="C1QR1" /region_name="Domainn /note="EXTRACELLULAR (POTENTIAL)." Region 32.. 174 /gene="C1QR1" /region_name="Domain" /note="C-TYPE LECTIN." Region 36 /gene="C1QR1" /region_jiame="Confiict" /note="C -> T (IN AA SE¬QUENCE)." Region 3S..39 /gene="C1QR1" /region_name="Conflict" /note='TA -> Rl (IN AA SEQUENCE)." Region 155 /gene="C1QR1" /region_name="Conf!ict" /note="S -> N (IN REF. 1)." Region 186 /gene="C1QR1" /region_name="Conflict" /note="G -> A (IN AA SE¬QUENCE).". Region 260..301 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 1." Bond bond(264,275) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(271,285) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(287,300) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Region 302..344 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 2." Bond bond(306,317) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(311,328) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." legion 318 /gene=nC1QR1" /region_name="Variant" /note="V -> A. FTId=VAR_013573." >ite 325 /gene="C1QR1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) POTENTIAL)." 3ond bond(330,343) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR-TY." Region 345..384 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 3, :ALCIUM-BINDING (POTENTIAL)." 3ond bond(349,358) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(354,367) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(369,383) /gene="C1QR1" /bond_type="disuifide" /note="BY SIMILAR¬ITY." Region 385..426 /gene=nC1QR1" /region_name="Domain" /note="EGF-LIKE 4, CALCIUM-BINDING (POTENTIAL)." Bond bond(389,400) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(396,409) /gene="C1QR1n /bondJype="disulfide" /note="BY SIMILAR¬ITY." Bond bond(411,425) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Region 427..468 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL)." Bond bond(431,443) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Bond bond(439,452) /gene="C1QR1" /bond_type=ndisulfide" /note="BY SIMILAR¬ITY." Bond bond(454,467) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILAR¬ITY." Region 492 /gene="C1QR1" /region_name="Conflict" /note="S -> A (IN AA SE¬QUENCE)." Region 496 /gene="C1QR1" /region_name="Conflicf /note="R -> Q (IN AA SE¬QUENCE)." Region 504 /gene="C1QR1" /region_name="Conflict" /note="R -> G (IN AA SE¬QUENCE)." Region 541 /gene="C1QR1" /region_name="Conflicf /note="P -> S (IN REF. 1)." Region 581..601 /gene="C1QR1" /region_name="Transmembrane region" /note="POTENTIAL." Region 594..601 /gene="C1QR1"/region_name="Domain" /note="POLY-LEU." Region 602..652 /gene="C1QR1" /region_name="Domain" /note="CYTOPLASMIC (POTENTIAL)." ORIGIN 1 matsmgllll llllltqpga gtgadteaw cvgtacytah sgklsaaeaq nhcnqnggnl 61 atvkskeeaq hvqrvlaqll rreaaltarm skfwiglqre kgkcldpslp Ikgfswvggg 121 edtpysnwhk elrnsciskr cvsllldlsq pllpsrlpkw segpcgspgs pgsniegfvc 181 kfsfkgmcrp lalggpgqvt yttpfqttss sleavpfasa anvacgegdk detqshyflc 241 kekapdvfdw gssgplcvsp kygcnfnngg chqdcfeggd gsflcgcrpg frilddlvtc 301 asrnpcsssp crggatcvlg phgknytcrc pqgyqldssq Idcvdvdecq dspcaqecvn 361 tpggfrcecw vgyepggpge gacqdvdeca Igrspcaqgc tntdgsfhcs ceegyvlage 421 dgtqcqdvde cvgpggplcd slcfntqgsf hcgclpgwvl apngvsctmg pvslgppsgp 481 pdeedkgeke gstvpraata sptrgpegtp katpttsrps Issdapitsa plkmiapsgs 541 pgvwrepsih hataasgpqe paggdssvat qnndgtdgqk lllfyilgtv vaillllala 601 Igllvyrkrr akreekkekk pqnaadsysw vperaesram enqysptpgt dc SEQ ID NO: 43 BAC05523 collectin placenta 1 [Mus musculus] gi|21901969[dbj|BAC05523.1|[21901969] FEATURES Location/Qualifiers source 1..742 /organism="Mus musculus" /db_xref="taxon: 10090" /tissueJib="Liver" Protein 1..742/product="collectin placenta 1" CDS 1 ..742 /gene="CL-P1" /coded_by="AB078434.1:92..2320n ORIGIN 1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi vllyilcall titvailgyk 61 wekmdnvtd gmetshqtyd nkltavesdl kklgdqagkkalstnselstfrsdildlrq 121 qlqeitekts knkdtleklq angdslvdrq sqlketlqnn sflittvnkt Iqayngyvtn 181 Iqqdtsvlqg nlqsqmysqs wimnlnnln Itqvqqrnii snfqqsvddt slaiqriknd 241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql ssftgqmdni 301 ttisqaneqs Ikdlqdlhkd tenrtavkfs qleerfqvfe tdivnfisni sytahhlrtl 361 tsnlndvrtt ctdtltrhtd dltslnntlv nirldsislr mqqdmmrskl dtevanlsw 421 meemklvdsk hgqliknfti Iqgppgprgp kgdrgsqgpp gptgnkgqkg ekgepgppgp 481 agergtigpv gppgergskg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkdglpgp 541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgame plalqneptp 601 asevngcpph wknftdkcyy fslekeifed aklfcedkss hlvfinsree qqwikkhtvg 661 reshwigltd seqesewkwl dgspvdyknw kagqpdnwgs ghgpgedcag li- yagqwndT 721 qcdeinnfic ekereavpss il SEQ ID NO: 45 AAM34742 46-kDa collectin precursor [Bos taurus] gi|21105685|gb|MM34742.1| AF509589J [21105685] sig_peptide 1..20 Region .67..245 /region_name="coIIagen-like region" Region 245..371 /fegionjiame-'carbohydrate recognition domain" CDS 1..371 /gene=,,CL-46"/coded_by="join(AF509589.1:1454..1652, AF509589.1:5950..6066,AF509589.1:6402..6509, AF509589.1:6823..6930,AF509589.1:7289..7405, AF509589.1:8021..8104,AF509589.1:10318..10700)" ORIGIN 1 mlllplsvll lltqpwrslg aemkiysqkt langctlwc rppegglpgr dgqdgregpq 61 gekgdpgspg pagragrpgp agpigpkgdn gsagepgpkg dtgppgppgm pgpagregps 121 gkqgsmgppg tpgpkgdtgp kggmgapgmq gspgpaglkg ergapgelga pgsagvagpa 181 gaigpqgpsg argppglkgd rgdpgergak gesgladvna Ikqrvtileg qlqrlqnafs 241 rykkavlfpd gqavgkkifk tagavksysd aqqlcreakg qlasprsaae neavaqlvra 301 knndaflsmn.distegkfty ptgeslvysn wasgepnnnn agqpencvqi yregkwndvp •361 csepllvicef SEQ ID NO: 47 XP_139613 similar to collectin sub-family member 10; collectin Irver 1; collectin 34 [Mus musculus] gi|20903807|ref|XP_139613.11[20903807] FEATURES Location/Qualifiers source 1..420 /organism="Mus musculus" /strain="C57BL/6JM /db_xref="taxon: 10090" /chrgmosome="15n Protein 1..420 /product="similarto collectin sub-family member 10; collectin liver 1; collectin 34" Region 152..269/region_name="C-type lectin (CTL) orcaiDonyarate-recoginuuii domain (CRD)" /note="CLECT" /db_xref="CDD:smart00034" Region 165..269 /region name="Lectin C-type domain" /note="lectin_c" /db_xref=nCDD:pfam000~59" Region 362..419 /regionjiame="Ubiquitin-conjugating enzyme E2, catalytic domain homologues" /note="UBCc" /dbjcref^CDD:smart00212" Region 363..419 /region jiame="Ubiquitin-conjugating enzyme" /note="UQ_con" /db_xref="CDD:pfam00179" CDS 1 ..420 /gene="LOC239447" /coded_by="XM_139613.1:1.. 1263" /db_xref="lnterimiD:239447" ORIGIN 1 mngfrvllrs nlsmllllal Ihfqslgldv dsrsaaevca thtispgpkg ddgergdtge 61 egkdgkvgrq gpkgvkgelg dmgaqgnigk sgpigkkgdk gekgflgipg ekgkagticd 121 cgryrkvvgq Idisvarlkt smkfiknvia gireteekfy yivqeeknyr eslthcrirg 181 gmlampkdev vntliadyva ksgffrvfig vndleregqy vftdntplqn ysnwkeeeps 241 dpsghedcve mlssgrwndt echltmyfvs slqedliedc lreqgllvqv tpanqellfg 301 idtflgpmsc vyqrtgtkqk lysqcrlwdg lakkqtneta niatfckgae pnrgsrpcgq 361 kqemmtlmms gnkgittfpe sdnlfkwvgt mlgaagtide dlkyklslns pwtliihpq SEQIDNO:'48 XP_123211 similar to collectin sub-family member 12 [Mus musculus] gi|20876566|ref |XP_123211.11[20876566] FEATURES Location/Qualifiers source 1..742 /6rganism="Mus musculus" /strain="C57BL/6J" /db„xref="taxon: 10090" /chromosome="18M Protein 1..742 /product="similarto collectin sub-family member 12" Region 79..320 /region_name="V-type ATPase 116kDa subunit family" • /note="V_ATPase_sub„a,7db_xref="CDD:pfam01496" Region 92..337 /regionjiame=,,lntermediate filament protein" /note=llfilament" /db_xref="CDD:pfam00038" Region 607..731 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref="CDD:smart00034" Region 624.732 /region_name="Lectin C-type domain" /note="lectin_c" /db_xref="CDD:pfam00059" CDS 1 ..742 /gene="LOC225157M /coded_by="XMJ23211.1:77..2305n /dbjcref^InterimlD^SISr ORIGIN 1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi vllyilcall titvailgyk 61 wekmdnvtd gmetshqtyd nkltavesdl kklgdqagkk alstnselstfrsdildlrq 121 qlqeitekts knkdtleklq angdslvdrq sqlketiqnn sflittvnkt Iqayngyvtn 181 Iqqdtsvlqg nlqsqmysqs wimnlnnln Itqvqqrnli sniqqsvddt slaiqriknd 241 fqnlqqvfiq akkdtdwlke kvqsiqtlaa nnsalakann dtledmnsql ssftgqmdni 301 ttisqaneqs Ikdlqdlhkd tenrtavkfs qleerfqvfe.tdivniisni sytahhlrtl 361 tsnlndvrtt ctdtltrhtd dltslnntlv nirldsislr mqqdmmrskl dtevanlsw 421 meemklvdsk hgqliknfti Iqgppgprgp kgdrgsqgpp gptgnkgqkg ekgepgppgp 481 agergtigpv gppgergskg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkdglpgp 541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgame plaiqneptp 601 asevngcpph wknftdkcyy fslekeifed aklfcedkss hlvfinsree qqwikkhtvg 661 reshwigltd seqesewkwl dgspvdyknw kagqpdnwgs ghgpgedcag Ii- yagqwndf 72T qcdeinnfic ekereavpss il SEQ ID NO: 49 NP_571645 mannose binding-like lectin [Danio rerio] gi|18858997|ref|NP_571645.1|[18858997] sig_peptide 1 ..23 nat_peptide 24..251 /product="mannose binding-like lectin" Region 24..36 /regionjiame="N-terminal segment" Region 33..70 /region_name="Collagen triple helix repeat (20 copies)" taote="Coliagen" /db_xref="CDD:pfam01391" Region 33..70 /region_name="Collagen triple helix repeat (20 copies)" /note="Collagen" /db_xref="CDD:pfam01391" Region 37.. 101 /region_name="collagen-like structure" Region 37..70 /region_name="Coilagen triple helix repeat (20 copies)" /note="Collagen" /db_xref="CDD:pfam01391" Region 71..74 /region_name="break in collagen structure" Region 102..132 /region_name="neck region" Region 133..251 /regionjiame="carbohydrate recognition domain" /note="CRD" Region 134..247 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECr7db_xref=,,CDD:smart00034M Region 146..247 /region_name="Lectin C-type domain" /note=nlectin_c" /db_xref="CDD:pfam00059" CDS 1..251 /gene^'^br/coded^y^NMJ31570.1:68..823,7note=,,collectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for ga!actose;mannose binding-like lectin" /db_xref="LocuslD:58091H ORIGIN 1 mallklflga llllqlvlql magaadpqsl ncpayagvpg tpghnglpgr dgrvgrdgan 61 gpkgekgepg vnvqgppgka gppgpagakg ergpsglpgq dcmsdslkse Iqklsdkial 121 iekwnfktf kkvgqkyyvtddveetfdkg mqycssngga Ivlprtleen allkvfvssa 181 fkrlfiritd rekegefvdtdrkkltftnwgpnqpdnykg aqdcgaiads glwddvscds 241 lypiiceiei k SEQ ID NO: 50 NP_569057 collectin sub-family member 12, isoform I; scavenger receptor with C- type lectin; collectin placenta 1 [Homo sapiens] gi| 18641360|ref|NP_569057.11[18641360] FEATURES Location/Qualifiers source 1..742 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="18" /map="18pter-p11.3" Protein 1..742 /product="collectin sub-family member 12, isoform I" /note="isoform I is encoded by transcript variant I; scavenger receptor with-C-type lectin; collectin placenta 1" Region 79..328 /region name="V-type ATPase 116kDa subunit family" /note="V_ATPase_subja" /db_xref="CDD:pfam01496fl Region 443..5S9 /region_name="collagen-Iike domain" Region 607..731 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref=nCDD:smart00034n Region 624..732 /region_name="Lectin C-type domain" /note="lectin_c" /db_xref="CDD:pfam00059" Region 668..719 /regionjiame-'Beta-lactamase" /note="beta-lactamase" /db_xref="CDD:pfam00144" CDS 1 ..742 /gene="COLEC12" /coded_by="NMJ 30386.1:172..2400" /db_xref-"LocuslD:81035" ORIGIN 1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi illyilcall titvailgyk 61 wekmdnvtg gmetsrqtyd dkltavesdl kkigdqtgkk aistnselst frsdildlrq 121 qlreitekts knkdtleklq asgdalvdrq sqlketlenn sflittvnkt Iqayngyvtn 181 Iqqdtsvlqg nlqnqmyshn wimnlnnln Itqvqqmli tnlqrsvddt sqaiqriknd 241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql nsftgqmeni 301 ttisqaneqn Ikdlqdlhkd aenrtalkfn qleerfqlfe tdivniisni sytahhlrtl 361 tsnlnevrtt ctdtltkhtd dltslnntla nirldsvslr mqqdlmrsrl dtevanlsvi 421 meemklvdsk hgqliknfti Iqgppgprgp rgdrgsqgppgptgnkgqkg ekgepgppgp 481 agergpigpa gppgerggkg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkeglpgp 541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgaw plalqneptp 601 apedngcpph wknftdkcyy fsvekeifed aklfcedkss hlvfintree qqwikkqmvg ' 661 reshwigltd serenewkwl dgtspdyknw kagqpdnwgh ghgpgedcag liyagqwndf 721 qcedvnnfic ekdretvlss al SEQ ID NO: 51 NP_110408 collectin sub-family member 12, isoform II; scavenger receptor with C- type lectin; collectin placenta 1 [Homo sapiens] gi|18641358|refjNPJ10408.2|[18641358] FEATURES Location/Qualifiers source 1..622 /organism="Homo sapiens" /db_xref="taxon:9606u /chromosome^ 18" /map-'18pter-p11.3" Protein 1..622 /product="coIlectin sub-family member 12, isoform II" /note="isoform II is encoded by transcript variant II; scavenger receptor with C-type lectin; collectin placenta 1" Region 79..328 /region_name="V-type ATPase 116kDa subunit family" /note=,,V_ATPase_sub-a"/db^xref=MCDD:pfam01496" Region 443..589 /region_name="collagen-like domain" CDS 1..622 /gene="COLEC12" /coded_by="NM_030781.2:172..2040" /dbjcref="LocusID:81035H ORIGIN 1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi illyilcall titvailgyk 61. wekmdnvtg gmetsrqtyd dkltavesdl kkigdqtgkk aistnselst frsdildlrq 121 qlreitekts knkdtleklq asgdalvHrn 181 Iqqdtsvlqg nlqnqrnyshn vvimninnln Itqvqqrnli tnlqrsvddt sqaiqriknd 241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql nsftgqmeni 301 ttisqaneqn Ikdlqdlhkd aenrtaikfn qleerfqlfe tdivniisni sytahhlrtl 361 tsnlnevrtt ctdtltkhtd ditsinntla nirldsvslr mqqdlmrsrl dtevanlsvi 421 meemklvdsk hgqliknfti Iqgppgprgp rgdrgsqgpp gptgnkgqkg ekgepgppgp 481 agergpigpa gppgerggkg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkeglpgp 541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgaw plalqneptp 601 apednskskp slqpggqgsa ca SEQIDNO:52 NP_569716 collectin sub-family member 12 [Mus muscuius] gi|1'8485494|refINP_569716.1|[18485494] FEATURES Location/Qualifiers source 1..742 /organism="Mus muscuius" /db_xref="taxon:10090" Protein 1..742 /product-'collectin sub-family member 12" Region 79..320 /region_name="V-type ATPase 116kDa subunit family" /note=MV_ATPase_sub_a,7db_xref="CDD:pfam01496" Region 607..731 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECr /db_xref=MCDD:smart00034" Region 629..732 /region_name="Lectin C-type domain" /note="lectin-c" /db_xref=nCDD:pfam00059" CDS 1..742/gene="Colec12"/coded by=nNM_130449.1:77..2305" /db_xref=TocuslD:140792Vdb_xref="MGD:2152907" ORIGIN 1 mkddfaeeee vqsfgykrfg ihegtqctkc innwalkfsi vllyilcall titvailgyk 61 wekmdnvsd gmetshqtyd nkltavesdl kklgdqagkk alstnselst frsdiidlrq 121 qlqeitekts knkdtieklq angdslvdrq sqlketlqnn sflittvnkt Iqayngyvtn 181 Iqqdtnvlqg nlqsqmysqs wimnlnnln Itqvqqrnli snlqqsvddt slaiqriknd 241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql ssftgqmdni 301 ttisqaneqs Ikdlqdlhkd tenrtavkfs qleerfqvfe tdivniisni sytahhlrtl 361 tsnlndvwtt ctdtltrhtd dltslnntlv nirldsislr mqqdmmrskl dtevanlsw 421 meemklvdsk hgqliknfti Iqgppgprgp kgdrgsqgpp gptgnkgqkg ekgepgppgp 481 agergtigpv gppgergskg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkdglpgp 541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgame plalqneptp 601 asevngcpph wknftdkcyy fslekeiled aklfcedkss hlvfinsree qqwikkhtvg 661 reshwigltd seqesewkwl dgspvdyknw kagqpdnwgs ghgpgedcag li- yagqwndf 721 qcdeinnfic ekereavpss il SEQ ID NO: 53 AAL61856 43kDa collectin precursor [Bos taurus] gi|18252111 |gb|AAL61856.11[18252111] FEATURES Location/Qualifiers source 1.321 /organism="Bos taurus" /db_xref=Mtaxon:9913n Protein 1..3217product="43kDa collectin precursor" /name="CL-43; conglutinin; SP- P" Region 1..166/region_name="coliagen-like" Region 167.. 193 /regionjname="alpha-helical neck" Region 195..321 /region_name="carbohydrate-recognttion domain" CDS 1..321 /gene=nCL43"/coded_by="join(AY071822.1:2945..3143, AY071822.1:5843..5950,AY071822.1;6273..6344, AY071822.1:6734..6850,AY071822.1:7039..7122,AY071822.1:9525..9910)H ORIGIN 1 mlplplsill lltqsqsflg eemdvysekt ltdp'ctlwc appadslrgh dgrdgkegpq 61 gekgdpgppg mpgpagregp sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk 121 gergtpgpgg aigpqgpsga mgppglkgdr gdpgekgarg etsvlevdtl rqrmrnlege 181 vqrlqnivtq yrkavlfpdg qavgekifktagavksysda eqlcreakgq lasprssaen 241 eavtqlvrak nkhaylsmnd iskegkftyp tggsidysnw apgepnnrak degpenclei ■ 301 ysdgnwndie creerlvice f SEQ ID NO: 44 AAL61855 43kDa collectin precursor [Bos taurus] gi| 18252109|gb|AAL61855.11[18252109] FEATURES Location/Qualifiers source 1.321 /organism="Bos taurus" /db_xref="taxon:9913" /tissueJype="Iiver" Protein 1 ..321 /product="43kDa collectin precursor" /name="CL-43; conglutinin; SP-D" CDS 1..321 /gene=MCL43n/coded_by=nAY071821.1:172..1137" ORiGIN 1 mlplplsill lltqsqsflg eemdvysekt ltdpctlwc appadslrgh dgrdgkegpq 61 gekgdpgppg mpgpagregp sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk 121 gergtpgpgg aigpqgpsga mgppglkgdr gdpgekgarg etsvlevdtl rqrmrnlege 181 vqrlqnivtq yrkavlfpdg qavgekifkt agavksysda eqlcreakgq lasprssaen 241 eavtqlvrak nkhaylsmnd iskegkftyp tggsidysnw apgepnnrak degpenclei '301 ysdgnwndie creerlvice f SEQ ID NO: 46 BAB22581 data source:SPTR, source key:Q9Y6Z7, evidence:ISS~homolog to COLLECTIN 34~putative [Mus musculus] gi|12833584|dbj|BAB22581.1|[12833584] FEATURES Location/Qualifiers source 1..272 /organism="Mus musculus" /strain='lC57BL/6J,7db_xref=,fFANTOM_DB:1010001H16,, /db_xref="MGD:1904296l7db-xref=,,taxon:10090,,/clone=f,1010001H16" /sex="male" /tissue_type="heart" /cloneJib-'RIKEN full-length enriched mouse cDNA library" /dev_stage="adult" Protein 1..272 /name="data source:SPTR, source key:Q9Y6Z7, evidence:ISS ho- molog to COLLECTIN 34 putative" CDS 1..272 /coded_by="AK003121.1:81..899" /db_xref="MGD: 1918943" ORIGIN 1 mmmrdlalag mlislaflsl Ipsgcpqqtt edacsvqilv pglkgdagek gdkgapgrpg 61 rvgptgekgd mgdkgqkgtv grhgkigpig akgekgdsgd igppgpsgep gipcecsqlr 121 kaigemdnqv tqlttelkfi knavagvret eskiyllvke ekryadaqls cqarggtlsm 181 pkdeaanglm asylaqagla rvfigindle kegafvysdr spmqtfnkwr sgepnnayde 241 edcvemvasg gwndvachit myfmcefdke nl ■ SEQ ID NO: 54 NPJ334905 mannose binding lectin, liver (A) [Mus musculus] gi|6"754654|ref|NPJ)34905.1 [[6754654] FEATURES Location/Qualifiers source 1..239 /organism=ftMus musculus" /db_xref="taxon; 10090" /chromosome="14" /map="14 15.0 cM" Protein 1.239 /product="mannose binding lectin, liver (A)" miscjeature 19..239 /partial /note="mature protein based on homology to rat MPB- A" Region 126..236 /region name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref="CDD:smart00034" Region 135..237 /region name="Lectin C-type domain" /note="lectin_c" /db_xref=,,CDD:pfam00d59n CDS 1..239/gene=HMbir/coded_by="NM 010775.1:121..840" /db_xref="LocuslD:17194,7db_xref=,,MGD:96923" ORIGIN 1 mlllpllpvl Icwsvsssg sqtcedtlkt csviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeiriikskl qltnklhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaiprnae enkaiqevat giaflgitde 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQ ID NO: 55 NPJ334906 mannose binding lectin, serum (C) [Mus musculus] gi|6754656|ref|NP_034906.1 [[6754656] sig_peptide 1 ..18 Region 120..241 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref="CDD:smart00034n Region 140..242 /region_name="Lectin C-type domain" /note="lectin_c" /db_xref=nCDD:pfam00059" CDS 1 ..244 /gene="Mbl2" /coded_by=,,NM_010776.1:177..911" /note="polysaccharide-binding component of RaRF; sequence similarity to man-nose-binding proteins" /db_xref="LocuslD:17195" /db_xref="MGD:96924" ORIGIN 1 rrisiftsflll cwtvvyaet Itegvqnscp vvtcsspgln gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa Irselralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat prnaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcw ilgngkwndv pcsdsflaic 241 efsd SEQ ID NO: 56 NPJD06429 collectin sub-family member 10; collectin liver 1; collectin 34 [Homo sapiens] gi|5453619|ref|NPJ)06429.1|[5453619] FEATURES Location/Qualifiers source 1..277 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="8" /map="8q23-q24.1" Protein 1..277 /product="coIlectin sub-family member 10" /note-"collectin liver 1; collectin 34" Region 152..271 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT' /db_xref="CDD:smart00034n Region 165..272/region_name="Lectin C-type domain" /note="lectin_c" /db_xref="CDD:pfam00059" CDS 1 ..277 /gene="COLEC10" /coded_by=,,NM_006438.2:76..909M /db_xref="LocusID:10584" ORIGIN 1 mngfasllrr nqfillvlfl Iqiqslgldi dsrptaevca thtispgpkg ddgekgdpge 61 egkhgkvgrm gpkgikgelg dmgdrgnigk tgpigkkgdk gekgllgipg ekgkagtvcd 121 cgryrkfvgq Idisiarlkt smkfvknvia gireteekfy yivqeeknyr eslthcrirg 181 gmlampkdea antliadyva ksgffrvfig vndieregqy mftdntplqn ysnwnegeps 241 dpyghedcve mlssgrwndt echltmyfvc efikkkk SEQ ID NO: 57 BAB72147 collectin placenta 1 [Homo sapiens] gi|17026101|dbj|BAB72147.1 [[17026101] FEATURES Location/Qualifiers source 1..742/organism="Homo sapiens" /db_xref="taxon:9606" /sex="female" /tissuejib="placenta" Protein 1..742/product="collectin placenta 1" CDS 1.742/gene=,,CL-P1"/coded-by="AB005145.1:71..2299" ORIGIN 1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi illyilcall titvailgyk . 61 wekmdnvtg gmetsrqtyd dkltavesdl kklgdqtgkk aistnselst frsdildlrq 121 qlreitekts knkdtleklq asgdalvdrq sqlketlenn sflittvnkt Iqayngyvtn 181 Iqqdtsvlqg nlqnqmyshn wimnlnnln Itqvqqrnli tnlqrsvddt sqaiqriknd 241 fqnlqqvfiq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql nsftgqmeni 301 ttisqaneqn Ikdlqdlhkd aenrtaikfn qleerfqlfe tdivniisni sytahhlrtl 361 tsnlnevrtt ctdtltkhtd dltslnntla nirldsvslr mqqdlmrsrl dtevanisvi 421 meemklvdsk hgqliknfti Iqgppgprgp rgdrgsqgpp gptgnkgqkg ekgepgppgp 481 agergpigpa gppgerggkg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkeglpgp 541 qgppgfqglq gtvgepgvpg prgipglpgv pgmpgpkgpp gppgpsgaw plalqneptp 601 apedngcpph wknftdkcyy fsvekeifed aklfcedkss hlvfintree qqwikkqmvg 661 reshwigltd serenewkwl dgtspdyknw kagqpdnwgh ghgpgedcag liyagqwndf 721 qcedvnnfic ekdretvlss al SEQ ID NO: 58 AAF63470 mannose binding-like lectin precursor [Carassius auratus] gi|7542474|gb|AAF63470.1|AF227739_1 [7542474] sig_peptide Region 14..25 /region_name="N-terminal segment" Region 26..93 /region_name="collagen-like structure" Region 60..63 /region_name="break in collagen structure" Region 94..124 /region_name="neck region" Region 125..246 /region_name="carbohydrate recognition domain" /note=,,CRD" CDS 1..246 /gene="MBL" /coded J>y="AF227739.1: structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 llllqfalql Idgaepqnln cpayggvpgt pghnglpgrd grdgkdgaig pkgekgesgv 61 svqgppgkag ppgtagekge rgpsgpqgsp gsesyleslk seiqqlkaki atfekvssvc 121 hfrkvgqkyy itdgwgnfd qgikscmefg gtmvsprtsa enqallklw ssglgskkpy 18t igvtdrkteg qfvdtegkql tftnwgpgqp ddykglqdcg viedtglwdd ggcgdirpim 241 ceidik SEQ ID NO: .59 AAF63469 mannose binding-like lectin precursor [Danio rerio] gi[7542472|gb|AAF63469.1|AF227738_1[7542472] sig_peptide 1..23 mat_peptide 24..251 /product="mannose binding-like lectin" Region 24..36 /regionjiame="N-terrninal segment" Region 37..101 /region_name="coliagen-Iike structure" Region 71..74 /region_name="break in collagen structure" Region 102..132 /regionjiame="neck region" Region 133..251 /region_name=,.'carbohydrate recognition domain" /note="CRDM CDS 1 ..251 /gene="mb!" /coded_by="AF227738.1:68..823" /note=nco!lectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 mallklflga llllqlvlql magaadpqsl ncpayagvpg tpghngipgr dgrvgrdgan 61 gpkgekgepg vnvqgppgka gppgpagakg ergpsglpgq dcmsdslkse Iqklsdkial 121 iekwnfktf kkvgqkyyvt ddveetfdkg mqycssngga Ivlprtleen allkvfvssa 181 fkrlfiritd rekegefvdtdrkkltftnwgpnqpdnvka aadcaaiads alwddvscds 241 lypiiceiei k SEQ ID NO: 60 AAF63468 mannose binding-like lectin precursor [Cyprinus carpio] gi|7542470|gb|AAF63468.1 (AF227737J [7542470] sig_peptide 1 ..23 mat_peptide 24..256 /product="mannose binding-like lectin" Region 24..35 /region_name="N-terminal segment" Region 36.. 103 /region_name="collagen-like structure" Region 70..73 /region_name=nbreak in collagen structure" Region 104.. 134 /region_name="neck region" Region 135..256 /region_name="carbohydrate recognition domainn /note="CRDn CDS 1..256 /gene="MBL" /coded_by="AF227737.1:67..837" /note="collectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 malfklfigt Hllqfalql Idgaepqnln cpayggvpgt pghnglpgrd grdgkdgaig 61 pkgekgesgv svqgppgkag ppgpagekge rgptgsqgsp gsesvleslk seiqqlkaki 121 atfekvasvg hfrqvgqkyy itdgwgtfd qglkfckdfg gtmvfprtsa enqallklw 181 ssglsskkpy igvtdreteg rfvntegkql tftnwgpgqp ddykglqdcg viedsglwdd 241 gscgdirpim ceidnk SEQ ID NO: 61 AAK97540 surfactant protein A precursor [Gallus gallus] gi|15420996|gb|AAK97540.1 |AF411083 J [15420996] sigjDeptide 1 ..18 Region 19.-34 /region_name="N-terminal segment" Region 35..43 /region_name="putative collagen structure" Region 44..76 /region_name="putative coil structure" Region 77..97 /regionjiame^'alpha-helical coil-coil structure; neck region" Region 98..222 /region_name="carbohydrate recognition domain" Site 121.. 123 /site_type="glycosylation" Site 181..183 /site_type="glycosylation" /note="conserved" CDS 1 ..222 /gene="SP-A" /coded_by="AF411083.1:61.729" ORIGIN 1 mlsysfcmia aavailtpch aqncagapel psipgvsgll glgalkryfg sllwpygeek 61 Ipecqwlqrq qdlstssdde Ignvllnlrq rilqlegvla Idgkitkvge kifasngkev 121 nfssalesce etggtlatpm neeenkaimg ivkqynryay Igikesdtag qfkyvnnqpl 181 nytswqqyep ngkgtekcve mytdgnwkdr kcnlyrltvc ey SEQ ID NO: 62 JN0450 conglutinin precursor - bovine gi|346501 |pir]|JN0450[346501] FEATURES Location/Qualifiers source 1..371 /organism="Bos taurus" /db_xref="taxon:9913M Protein 1..371 /product="conglutinin precursor"/note="C3b-binding protein" Region 1..20 /region_name="domain" /note=wsignal sequence" Region 21..371 /region_name="product" /note="conglutininn Region 46..214 /region_name="regionM /note="collagen-like" Site 63 /site_type="binding" /note="carbohydrate (Lys) (covalent)" Site 63 /site_type="modifiedn /note="5-hydroxylysine 0-ys)" Region 75..371 /region_name="product" /note="conglutinin-Nn Site 78 /site_type="modifiedn /note=n4-hydroxypro!ine (Pro)" Site 87 /site_type="bindingn /note="carbohydrate (Lys) (covalent)" Site 87 /site_type="modifiedn /note="5-hydroxylysine (Lys)" Site 96 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 99 /site_type="binding" /note="carbohydrate (Lys) (covalent)" Site 99/site_type="modified" /note="5-hydroxyiysine (Lys)" Site 108 /sitejype-'modified" /note="4-hydroxyproline (Pro)" Site 111 /sitejype-'modified" /note="4-hydroxyproline (Pro)" Site 129 /siteJype="modified" /note="4-hydroxypro(ine (Pro)" Site 132 /siteJype="modified" /note="4-hydroxyprofine (Pro)" Site 135 /sitejype="binding" /note="carbohydrate (Lys) (covalent)" Site 135 /site_type="modified" /note="5-hydroxylysine (Lys)" Site 141 /site_type="binding"/note="carbohydrate (Lys) (covalent)" Site 141 /site_type="modified" /note="5-hydroxylysine (Lys)" Site 147/sitejype-'modified" /note="4-hydroxyproIine (Pro)" Site 153 /site Jype="modified,f /note="4-hydroxyproiine (Pro)" Site 159 /site_type="binding" /note="carbohydrate (Lys) (covalent)" Site 159 /site_type=umodified" /note="5-hydroxylysine (Lys)" Site 162 /site_type="binding" /note="carbohydrate (Lys) (covalent)" Site 162 /site_type="modified" /note="5-hydroxylysine (Lys)n Site 171 /sitejype-'modified" /note="4-hydroxyprofine (Pro)" Site 195 /site_type="modified" /note="4-hydroxypro(ine (Pro)" Site 198 /site_type="binding" /note=ncarbohydrate (Lys) (covalent)" Site 198 /siteJype="modified" /note="5-hydroxylysine (Lys)" Site 210 /siteJype="binding" /note="carbohydrate (Lys) (covalent)" Site 210 /sitejype-'modified" /note="5-hydroxylysine (Lys)" Region 248..369 /region_name="domain" /note="C-type lectin homology #label LCH" Site 337 /site_type="binding" /note="carbohydrate (Asn) (covalent)" ORIGIN 1 mlllplsvll lltqpwrslg aemttfsqki lanactlvmc splesglpgh dgqdgrecph 61 gekgdpgspg pagragrpgw vgpigpkgdn gfvgepgpkg dtgprgppgm pgpagregps 121 gkqgsmgppg tpgpkgetgp kggvgapgiq gfpgpsglkg ekgapgetga pgragvtgps 181 gaigpqgpsg argppglkgd rgdpgetgak gesglaevna Ikqrvtildg hlrrfqnafs 241 qykkavlfpd gqavgekrfktagavksysd aeqlcreakg qlasprssae neavtqmvra 301 qeknaylsmn distegrfty ptgeilvysn wadgepnnsd egqpencvei fpdgkwndvp 361 cskqllvicef SEQ ID NO: 63 A57250 mannan-binding protein - chicken (fragment) gi|1362725|pir||A57250[1362725] FEATURES Location/Qualifiers source 1.30 /organism="Gallus gallus" ./db_xref="taxon:9031" Protein 1..30 /product="mannan-binding protein" /note="collectin" Site 28 /siteJype="modified" /note="4-hydroxyproline (Pro)" ORIGIN 1 lltcdkpeek myscpiiqcs apavnglpgd SEQ ID NO: 64 A53570 collectin-43 - bovine gi|1083017|pir||A53570[1083017] FEATURES Location/Qualifiers source 1..301 /organism=BBos taurus" /db_xref="taxon:9913" ' Protein 1..301 /product="collectin-43,7note="lectin CL-43" Region 177..299 /region_name="domain" /note="C-type lectin homology #label LCH" ORIGIN 1 eemdvysekt Itdpctlvvc appadslrgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdr gdpgekgarg etsvlevdtl rqrmrnlege vqrlqnivtq yrkavlfpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepnnrak degpenclei ysdgnwndie creerlvice 301 f SEQ ID NO: 65 AAF28384 lung surfactant protein A [Sus scrota] gi|6782434|gblAAF28384.1 |AF133668J [6782434] FEATURES Location/Qualifiers source 1.. 116 /organism="Sus scrofa" /db_xref="taxon:9823" Protein SEQ ID NO: 66 AAF22145 lung surfactant protein D precursor; SPD; SP-D; CP4 [Sus scrofa] gi|6760482|gb|AAF22145.2|AF132496_1 [6760482] sig _peptide 1 ..20 mat_peptide 21..378 /product="lung surfactant protein D" CDS 1 ..'378 /gene="SFTPD" /coded_by="AF132496.2:44.. 1180" ORIGIN 1 mlllplsvli lltqpprslg aemktysqra vanacalvmc spmenglpgr dgrdgregpr 61 gekgdpglpg avgragmpgl agpvgpkgdn gstgepgakg digpcgppgp pgipgpagke 121 gpsgqqgnig ppgtpgpkge tgpkgevgal gmqgstgarg paglkgerga pgergap-gsa 181 gaagpagatg pqgpsgargp pglkgdrgpp gerg'akgesg Ipgitalrqq vetlqgqvqr 241 Iqkafsqykk velfpngrgv gekifktggf ektfqdaqqv ctqaggqmas prseteneal 301 sqlvtaqnka aflsmtdikt egnftyptge plvyanwapg epnnnggssg aencveifpn 361 gkwndkacge Irlvicef SEQ ID NO: 67 P41317 MANNOSE-BINDING PROTEIN C PRECURSOR (MBP-C) (MANNAN-BINDING PROTEIN) (RA-REACTIVE FACTOR'P28A SUBUNIT) (RARF/P28A) gi|1346477|sp|P41317|MABC_MOUSE[1346477] FEATURES Location/Qualifiers source 1..244 /organism="Mus. museulus" /db_xref="taxon:10090" gene 1.. 244 /gene="MBL2" Protein 1 ..244 /gene=nMBL2" /product="MANNOSE-BINDING PROTEIN C PRE¬CURSOR" Region 1...18 /gene="MBL2" /region_name="SignaI" /note="BY SIMILARITY." Region 3 /gene="MBL2" /region_name="Conflicf /nbte="l -> L (IN REF. 1)." Region 15 /gene="MBL2" /region_name="Confiict" /note="V -> A (IN REF. 1).". Region 19..244 /gene="MBL2" /region_name="Mature chain" /note="MANNOSE-BINDING PROTEIN C." Bond bond(29) /gene="MBL2" /bond_type=',disulfide" /note="INTERCHAIN (BY SIMILARITY)." Bond bond(34) /gene=HMBL2" /bond_type=ndisulfide" /note="lNTERCHAlN (BY SIMILARITY)." Region 38..96 /gene="MBL2" /region_name="Domain" /note="GOLLAGEN-LIKE (G- X-Y)." Site 43 /gene="MBL2" /site_type="hydroxylation" /note="(POTENTIAL)." Site 58 /gene="MBL2" /site_type="hydroxylation" /note="(POTENTIAL)." Site 69 /gene="MBL2" /site_type=nhydroxylation" /note="(POTENTIAL).M Site 78 /gene="MBL2" /site_type="hydroxylation" /note="(POTENTlAL)." Site 81 /gene="MBL2" /site_type="hydroxylation" /note="(POTENTlAL)." Region 149..242 /gene="MBL2" /region_name="Dornainn /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(151,240) /gene="MBL2" /bond_type="disuffide"/note="BY SIMILARITY." Bond bond(218,232) /gene="MBL2" /bond_type="disulfiden /note="BY SIMILARITY." ORIGIN 1 msiftsflll cwtwyaet ltegvqnscp wtcsspgln gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa Irselralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat pmaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcw ilgngkwndv pcsdsflaic 241 efsd SEQ ID NO: 68 P39039 MANNOSE-BINDING PROTEIN A PRECURSOR (MBP-A) (MANNAN- BINDING PROTEIN) (RA-REACTIVE FACTOR POLYSACCHARIDE-BINDING COMPONENT P28B POLYPEPTIDE) (RARF P28B) gi|729972|sp|P39039|MABA_MOUSE[729972] FEATURES Location/Qualifiers source 1..239 /organism=1,Mus musculus" /db_xref="taxon: 10090" genet..239/gene="MBL1" Protein 1..239 /gene="MBL1" /product="MANNOSE-BINDING PROTEIN A PRE¬CURSOR" Region 1..17 /gene="MBL1" /region_name="Signal" /note="BY SIMILARITY." Region 18..239 /gene="MBL1" /region name="Mature chain" /note="MANNOSE-BINDING PROTEIN A." Region 37..89 /gene="MBL1" /region_name="Domainn /note="COLLAGEN-L!KE (G-X-Y)." Region 144..239 /gene="MBL1" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(146,235) /gene="MBL1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(213,227) /gene="MBL1" /bond_type="disulfideH /note="BY SIMILARITY." ORIGIN 1 mlllpllpvl Icvvsvsssg sqtcedtlkt csviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeirilkskl qltnklhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaiprnae enkaiqevat giaflgrtde 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQ ID NO: 69 P42916 COLLECTIN-43 (CL-43) gi|1168967|sp|P42916|CL43_BOVIN[1168967] FEATURES Location/Qualifiers source 1..301 /organism="Bos taurus" /db_xref="taxon:9913" Protein 1..301 /product="COLLECTIN-43" Region 29..142 /region_name="Domain" /note="COLLAGEN-LIKE (G-X-Y)." Region 202..301 /region_name="Domainu /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(204,299) /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(277,291) /bond_type="disulflde" /note="BY SIMILARITY." ORIGIN 1 eemdvysekt Itdpctlvvc appadsirgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdr gdpgekgarg etsvlevdtl rqrmrnlege vqrlqnivtq yrkavlfpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepgnrak degpendei ysdgnwndie creerlvlce 301 f -SEQ ID NO: 70 CAB56155 DMBT1/8kb.2 protein [Homo sapiens] gi|5912464|emb|CAB56155.1|[5912464] sig_peptide 1..26 mat_peptide 26..2412 /product="DMBT1/8kb.2 protein" CDS 1..2412 /gene="DMBT1" /coded_by="AJ243212.1:107..7345" /note="Sequence is an alternative splice form of the DMBT1 gene that is expressed in human adult trachea. Isoforms of DMBT1 are identical to the collectin binding protein gp-340. Full-length cDNA clone contains 1 bp deletions in codons 100 and 1751, that were corrected by comparison with the genomic exons" ORIGIN 1 mgistvilem cllwgqvlst ggwiprttdy aslipsevpl dttvaegspf pseltlestv 6 12 18 24 30 36 42 48 54 60 66 72 78 84 90 96 102 108 114 120 126 132 138 144 150 156 162 168 aegspisles tlettvaegs lipsestles tvaegsdsgl alrlvngdgr cqgrveilyr gswgavcdds wdtndanwc rqlgcgwams apgnawfgqg sgpialddvr csghe- sylws cphngwlshn cghgedagvi csaaqpqstl rpeswpvris ppvptegses slalrlvngg drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd vrcsghesyl wscphngwlt hncghsedag vicsapqsrp tpspdtwpts hastagpess lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanw crqlgcgwat sapgnarfgq gsgpivlddv rcsgyesylw scphngwlsh ncqhsedagv icsaahswstpspdtlptit Ipastvgses slalrlvngg drcqgrvevl yrgswgtvcd dswdtndanv vcrqlgcgwa mlapgnarfg qgsgpivldd vrcsgnesyl wscphngwls hncghsedag vicsgpessl alrlvnggdr cqgrveviyr gswgtvcdds wdtndanwc rqlgcgwams apgnarfgqg sgpivlddvr csghesylws cpnngwlshn cghhedagvi csaaqsrstp rpdtlstitl ppstvgsess Itlrlvngsd rcqgrvevly rgswgtvcdd swdtndanw crqlgcgwat sapgnarfgq gsgpivlddv rcsghesylw scphngwlsh ncghhedagv icsvsqsrpt pspdtwptsh astagpessl alrlvnggdr cqgrveviyr gswgtvcdds wdtsdanwc rqlgcgwats apgnarfgqg sgpivlddvr csgyesylws cphngwlshn cqhsedagvi csaahswstp spdtlptitl pastvgsess lalrlvnggd rcqgrvevly qgswgtvcdd swdtndanw crqlgcgwam sapgnarfgq gsgpivldda rcsghesylw scphngwlsh ncghsedagv icsasqsrpt pspdtwptsh astagsessl alrlvnggdr cqgrveviyr gswgtvcddy wdtndanvac rqlgcgwams apgnarfgqg sgpivlddvr csghesylws cphngwlshn cghhedagvi csasqsqptp spdtwptsha stagsessla Irlvnggdrc qgrvevlyrg swgtvcddyw dtndanwcr qlgcgwatsa pgnarfgqgs gpividdvrc sghesylwsc phngwlshnc ghhedagvic sasqsqptps pdtwptshas tagsesslal rlvnggdrcq grvevlyrgs wgtvcddywd tndanwcrq Igcgwatsap gnarfgqgsg pivlddvrcs ghesyiwscp hngwlshncg hhedagvics afqsqptpsp dtwptsrast agsestlalr Ivnggdrcrg rvevlyqgsw gtvcddywdt ndanwcrql gcgwamsapg naqfgqgsgp ivlddvrcsg hepylwscph ngwlshncgh hedagvicsa aqsqstprpd twlttnlpal tvgsesslal rlvnggdrcr grvevlyrgs wgtvcddswd tndanwcrq lgcgwamsap gnarfgqgsg pivlgdvrcs gnesylwscp hkgwlthncg hhedagvics 1741 atqinstttd wwhpttttta rpssncggfl fyasgtfssp sypayypnna kcvweievns 1801 gyrinlgfsn Ikleahhncs fdyveifdgs Insslllgki cndtrqifts synrmtihfr 1861 sdisfqntgf lawynsfpsd atlrivnlns syglcagrve iyhggtwgav cddswtiqea 1921 ewcrqlgcg ravsalgnay fgsgsgpitl ddvecsgtes tlwqcrnrgw fshncnh^d 1981 agvicsgnhl stpapflnit rpnnyscggf Isqpsgdfss pfypgnypnn akcvwdievq 2041 nnyrvtvifr dvqleggcny dyievfdgpy rsspliarvc dgargsftss snfmsirfis 2101 dhsitrrgfr aeyysspsnd stnllclpnh mqasvsrsyl qsigfsasdl vistwngyye 2161 crpqitpnlv iftipysgcg tfkqadndti dysnlltaav sggiikrrtd irihvscrrnl 2221 qntwvdtmyi andtihvann tiqveevqyg nfdvnisfyt sssflypvts rpyyvdlnqd 2281 lyvqaeilhs davltlfvdt cvaspysndf tsltydlirs gcvrddtygp ysspslriar 2341 frfrafhfln rfpsvylrck mvvcraydps srcyrgcvlr skrdvgsyqe kvdwlgpiq 2401 Iqtpprreeepr SEQ ID NO: 71 BAA81747 coilectin 34 [Homo sapiens] gi|5162875]dbj|BAA81747.1|[5162875] FEATURES Location/Qualifiers source 1.277 /organism="Homo sapiens" /db_xref="taxon:9606" Protein 1..277 /product-'collectin 34" CDS 1.277 /coded_by=nAB00263l1:6..839n ORIGIN 1 mngfasllrr nqfillvlfl Iqiqslgldi dsrptaevca thtispgpkg ddgekgdpge 61 egkhgkvgrm gpkgikgelg dmgdrgnigk tgpigkkgdk gekgllgipg ekgkagtvcd 121 cgryrkfvgq Idisiarlkt smkfvknvia gireteekfy yivqeeknyr eslthcrirg 181 gmlampkdea antliadyva ksgffrvfig vndleregqy mftdntplqn ysnwnegeps 241 dpyghedcve mlssgrwndt echltmyfvc efikkkk SEQ ID NO: 72 AAB94071 mannan-binding lectin; coilectin [Gallus gallus] gi|2736145|gb|AAB94071.1|[2736145] FEATURES Location/Qualifiers source 1.238 /organism="Gallus gallus" 7strain="White Leghorn" /db_xref="taxon:9031" /tissueJype="liver". Protein l.>238 /product="mannan-binding lectin" /name="c-type lectin" /n'ote=l'mannan-binding protein; MBP; mannose-binding protein; MBL; coilectin" CDS 1.238 /gene="cMBI" /coded J>y="AF022226.1:l.>714" ORIGIN 1 mmatsllttd kpeekmyscp iiqcsapavn glpgrdgrdg pkgekgdpgeglrglqgipg 61 kagpqglkge vgpqgekgqk gergivvtdd Ihrqitdlea kirvleddls rykkalslkd 121 vvnigkkmfv stgkkynfek gkslcakags vlasprneae ntalkdlidp ssqayigisd 181 aqtegrfmyl sggpltysnw kpgepnnhkn edcaviedsg kwndldcsns nifiicel SEQ ID NO: 73 AAB36019 mannan-binding protein, MBP=lectin {N-terminal} [chickens, serum, Peptide Partial, 30 aa] [Gallus gallus] giI1311692|gb|AAB36019.1|[1311692] FEATURES Location/Qualifiers source 1.30 /organism=nGallus gallus" /db_xref="taxon:9031" Protein 1.30 /partial /product="mannan-binding protein" /name="lectin" /note="MBP" ORIGIN 1 lltcdkpeek myscpiiqcs apavnglpgd SEQ ID NO: 74 .. AAB27504 conglutinin (N) {N-terminal} [cattle, Peptide Partial, 60 aa] [Bos taurus] gi|386660|gb|AAB27504.11[386660] . FEATURES Location/Qualifiers source 1.60 /organism=rrBos taurus" /dbjcref="taxon:9913" Protein 1.60 /partial /product="conglutinin (N)". ORIGIN 1 aemttfsqki lanactlvmc splesgipgh dgqdgrecph gekgdpgspg pagragrpgw SEQ ID NO: 75 CAA53511 collectin-43 [Bos taurus] gi|499385|emb|CAA53511.1 ([499385] FEATURES Location/Qualifiers source 1..301 /organism=MBos taurus" /db_xref=ntaxon:9913w /tissue_type="liver" /cloneJib="lambda gt 11" Protein 1..301 /product="colIectin-43" mat_peptide 1..301 /product="coIlectin-43" CDS 1..301 /coded jDy="X75912.1: ORIGIN 1 eemdvyxekt Itdpctlwc appadslrgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdr gdpgekgarg etsvlevdtl rqrmmlege vqriqnivtq yrkavifpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepgnrak degpenclei ysdgnwndie creerlvice 301 f SEQ ID NO: 76 AAA82010 mannose-binding protein C [Mus musculus] gi|773288|gb|AAA82010.1 ][773288] FEATURES Location/Qualifiers source 1..244/organism="Mus musculus" /strain="BALB/c" /db_xref="taxon: 10090" /clone="Lambda 14 and 52; Cos11A" /cloneJib="NIH/3T3 Swiss mouse embryo cell line and BALB/c pWE15 cosmid li¬brary" Protein 1..244 /product="mannose-binding protein C" Site 1..59 /site^type^signal-peptide" /note="signal-peptide and collagen-like region" mat_peptide 98 /product="mannose-binding protein C" /note="collagen-Iike domain" mat_peptide 121 /product-'mannose-binding protein C" /note="linking-peptide domain" mat_peptide ORIGIN 1 msiftsflll cwtwyaet Itegvqnscp wtcsspgln gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa Irseiralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat prnaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcw ilgngkwndv pcsdsflaic 241 efsd SEQ ID NO: 77 AAA82009 mannose-binding protein A [Mus musculus] gi|773280|gb|AAA82009.1|[773280] sig_peptide 1..18 mat_peptide 19..239 /product^'unnamed" mat_peptide 19..>52 /product="mannose-binding protein A" /note="collagen-like region" rnat_peptide 91 /product-'mannose-binding protein A" /note=ncollagen-like domain" mat_peptide 116 /produqt=Mmannose-binding protein A" /note^Iinking-peptide domain" CDS 1..239 /gene="Mbl1" /coded_by="join(U09007.1:275..428,U09D08.1:287..403, U09009.1:166..240,U09010.1:78..451)" ORIGIN 1 mlllpllpvl Icvvsvsssg sqtcedtlkt csyiacgrdg rdgpkgekge pgqgirglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeirilkskl qltnklhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaipmae enkaiqevat giafigitde 181 ategqfmyvfggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa Lung surfactant protein SEQ ID NO: 78 P35247 Pulmonary surfactant-associated protein D precursor (SP-D) (PSP-D) gi|464486|sp|P35247lPSPD_HUMAN[464486] FEATURES Location/Qualifiers source 1..375/organism="Homo sapiens" /db_xref="taxon:9606" gene 1 ..375 /gene="SFTPD" /note="SFTP4; PSPD" Protein 1..375/gene="SFTPD"/product="Pulmonary surfactant-associated protein D precursor" Region 1..20 /gene=BSFTPD" /region_name="Signal" /note="BY SIMILARITY." Region 21.375 /gene="SFTPD" /region_name="Mature chain" /note="PULMONARY SURFACTANT-ASSOCIATED PROTEIN D." Region 31 /gene="SFTPDn /region_name="Conflict" /note="M -> T (IN REF. 2)." Region 46..222 /gene="SFTPD" /region_name="Domain" /note=n COLLAGEN-LIKE." Region 59/gene="SFTPDn /region_name="Conflict" /note="P -> F (IN REF. 3)." Site 78 /gene="SFTPD" /site_type="hydroxyIation" /note="(BY SIMILARITY)." Site 87 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Site 90 /gene="SFTPD" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Site 96 /gene="SFTPD" /site_type="hydroxyiation" /note="(BY SIMILARITY)." Site 99 /gene="SFTPD" /site_type="hydroxy!ation" /note="(BY SIMILARITY)." Region 122 /gene="SFTPD" /region_name="Conflict" /note="A -> P (IN REF. 2)." Site 171 /gene="SFTPD" /site_type="hydroxylation,7note="(BY SIMILARITY)." Site 177 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Region 180 /gene-"SFTPD'* /region_name="Conflict" /note="T -> A (IN REF. 2)." Region 206 /gene="SFTPD" /region_name="Conflict" /note="D -> P (IN REF. 3)." Region 223..252 /gene="SFTPD" /region_name="Domain" /note="COILED COIL (POTENTIAL)." Region 227..253 /gene="SFTPD" /region_name="Helical region" Region 254..256 /gene="SFTPD" /region_name="Hydrogen bonded turn" Region 257..260 /gene="SFTPD" /region_nam'e="Beta-strand region" Region 261 ..262 /gene="SFTPD" /region_name="Hydrogen bonded turn" Region 263..272 /gene="SFTPD" /region_name="Beta-strand region" Region 274..283 /gene="SFTPD" /region jiame="Helical region" Region 279..375 /gene="SFTPD" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(281,373) /gene="SFTPD'7bond_type="disulfide" Region 284..2857gene="SFTPD" /region_name="Hydrogen bonded turn" Region 287..288 /gene="SFTPD" /region_name="Beta-strand region" Region 294..307 /gene="SFTPD" /region_name="HeIical region" Region 308 /gene="SFTPD" /region_name="Hydrogen bonded turn" Region 311..316 /gene="SFTPD" /regipn_name="Beta-strand region" Region 321..322 /gene="SFTPD" /region_name="Hydrogen bonded turn" Region 325 /gene="SFTPD" /region_name="Beta-strand region" Region 327..328/gene="SFTPD"/region_narhe="Hydrogen bonded turn" Region 331 /gene="SFTPDB /region_name="Beta-strand region" Region 337 /gene="SFTPD" /region_name="Beta-strand region" Region 339.-.340 /gene="SFTPD" /region jiame="Hydrogen bonded turn" Region 345..347 /gene="SFTPD" /region_name="Helical region" Bond bond(351,365) /gene="SFTPD,! /bondJype="disulfide" Region 351 ..354 /gene="SFTPD" /region_name="Beta-strand region" Region 356..357 /gene="SFTPD" /region_name="Hydrogen bonded turnH-Region 360..363 /gene="SFTPD" /region_name="Beta-strand region" Region 365..366 /gene="SFTPD" /regionjiame="Hydrugen bonded turn" Region 369..375 /gene="SFTPDM /region_name="Beta-strand region" Region 374 /gene=nSFTPD" /region jiame="Conflicr /note=nE -> EH (IN REF. 3)." ORIGIN 1 mllfllsalv Iltqplgyle aemktyshrt mpsactlvmc ssvesgipgr dgrdgregpr 61 gekgdpgipg aagqagmpgq agpvgpkgdn gsvgepgpkg dtgpsgppgp pgvpgpagre 121 galgkqgnig pqgkpgpkge agpkgevgap gmqgsagarg lagpkgergv pgergvpgnt 181 gaagsagamg pqgspgargp pglkgdkgip gdkgakgesg Ipdvaslrqq vealqgqvqh 241 Iqaafsqykk velfpngqsv gekifktagf vkpfteaqll ctqaggqlas prsaaenaal 301 qqlvvaknea aflsmtdskt egkftyptge slvysnwapg epnddggsed cveiftngkw 361 ndracgekrl wcef SEQ ID NO: 79 NPJ302395 microfibrillar-associated protein 4; microfibril-associated glycoprotein 4 [Homo sapiens] gi|23111005|ref|NP_002395.1 ][23111005] FEATURES Location/Qualifiers source 1..255 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="17" /map="17p11.2" Protein 1..255 /product="microfibrillar-associated protein 4" /note="microfibril- associated glycoprotein 4" Region 36..255 /region_name="smart00186, FBG, Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen betaand gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous" Region 38..254 /region_name="pfam00147, fibrinogen_C, Fibrinogen beta and gamma chains, C-terminal globular domain" CDS 1 ..255 /gene="MFAP4" /coded_by=nNM_002404.1:26..793n /db_xref="LocuslD;4239"/db_xref="MiM:600596,, ORIGIN 1 mkallalpll (Ilstppcap qvsgirgdal erfclqqpld cddiyaqgyq sdgvyliyps 61 gpsvpvpvfc dmtteggkwt vfqkrfngsv sffrgwndyk Igfgradgey wlglqnmhll 121 tlkqkyelrv dledfennta yakyadfsis pnavsaeedg ytlfvagfed ggagdslsyh 181 sgqkfstfdrdqdlfvqnca alssgafwfr schfahlngf ylggshlsya riginwaqwkg 241 fyyslkrtem kirra SEQ ID NO: 80 1KMRA Chain A, Solution Nmr Structure Of Surfactant Protein B (11-25) (Sp- B11- 25) gi|22219056|pdbl1 KMR|A[22219056] FEATURES Location/Qualifiers source 1..15 /organism="Homo sapiens" /db_xref="taxon:9606" SecStr 3.. 11 /sec_str_type="helix" /note="helix 1" ORIGIN 1 cralikriqa mipkg SEQ ID NO; 81 P50404 Pulmonary surfactant-associated protein D precursor (SP-D) (PSP-D) gi|1709879|sp|P50404|PSPD_MOUSE[1709879] FEATURES Location/Qualifiers source 1 ..374 /organism="Mus musculus" /db_xref="taxon: 10090" gene 1 ..374 /gene="SFTPD" /note="SFTP4" Protein 1..374 /gene="SFTPD" /product="Pulmonary surfactant-associated protein D precursor" Region 1..19 /gene="SFTPD" /region_name="Signaln /note="BY SIMILARITY." Region 20..374 /gene="SFTPD" /region_name="Mature chain" /note="PULMONARY SURFACTANT-ASSOCIATED PROTEIN D." Region 45..221 /gene="SFTPD" /regionjiame="Domain" /note="COLLAGEN-LIKE." Site 89 /gene="SFTPD" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Region 222..253 /gene="SFTPD" /region_name="Domain" /note="COILED COIL (POTENTIAL)." Region 278..374 /gene="SFTPD" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(280,372) /gene="SFTPD" /bond_type="disulfide" /note="BY SIMILARITY." . Bond bond(350,364) /gene="SFTPD" /bond_type="disulfide" /note="BY SIMILARITY." ORIGIN 1 mlpflsmlvl Ivqplgnlga emkslsqrsv pntctlvmcs ptenglpgrd grdgregprg 61 ekgdpglpgp mglsglqgpt gpvgpkgeng sagepgpkge rglsgppglp gipgpagkeg 121 psgkqgnigp qgkpgpkgea gpkgevgapg mqgstgakgs tgpkgergap gvqgapgnag ' 181 aagpagpagp qgapgsrgpp glkgdrgvpg drgikgesgl pdsaalrqqm ealkgklqrl 241 evafshyqka alfpdgrsvg dkifrtadse kpfedaqemc kqaggqlasp rsatenaaiq 301 qlitahnkaa flsmtdvgte gkftyptgep Ivysnwapge pnnnggaenc veiftngqwn 361 dkacgeqrlv icef SEQ ID NO: 82 P06908 Pulmonary surfactant-associated protein A precursor (SP-A) (PSP-A) (PSAP) gi|1172693|sp|PQ6908|PSPA_CANFA[1172693] FEATURES Location/Qualifiers source 1..248 /organism-'Canis familiaris" /db_xref="taxon:9615" gene 1 ..248 /gene="SFTPA1" /note="SFTPA; SFTP1" Protein 1..248 /gene="SFTPAr /product="Pulmonary surfactant-associated protein A precursor" Region 1..17 /gene="SFTPA1" /region_name="Signal" Region 18..248 /gene="SFTPA1" /region_name="Mature chain" /note="PULMONARY SURFACTANT-ASSOCIATED PROTEIN A." Site 20 /gene="SFTPA1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Region 28.. 100 /gene="SFTPA1" /region_name="Domain" /note=nCOLLAGEN-LIKE." • Region 153..248 /gene=nSFTPA1" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(155,246) /gene="SFTPA1" /bond_type="disulfide" /note="BY SIMILARITY." Site 207 /gene="SFTPA1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (PROBABLE)." . Bond bond(224,238) /gene="SFTPA1" /bond_type="disulfide" /note="BY SIMILARITY." ORIGIN 1 mwlrclalal tllmvsgien ntkdvcvgnp gipgtpgshg Ipgrdgrdgv kgdpgppgpl 61 gppggmpghp gpngmtgapg vagergekge pgergppglp asldeelqtt Ihdlrhqilq 121 tmgvlslhes llvvgrkvfs snaqsinfnd iqelcagagg qiaapmspee neavasivkk 181 yntyaylglv espdsgdfqy mdgapvnytn wypgeprgrg keqcvemytd gqwnnknclq 241 yrlaicef SEQ ID NO: 83 P12842 Pulmonary surfactant-associated protein A precursor (SP-A) (PSP-A) (PSAP)gi|131413|splP12842|PSPA_RABIT[131413] FEATURES Location/Qualifiers source 1..247 /organism="Oryctolagus cuniculusn /db_xref="taxon:9986" gene 1 ..247 /gene="SFTPA1" /note="SFTPA; SFTP1" Protein 1..247/gene="SFTPA1"/produdt="Pulmonary surfactant-associated protein A precursor" Region 1..15 /gene="SFTPA1" /region_name="Signal" /note="POTENTIAL." Region 12 /gene="SFTPA1" /region_name="Variant" /note="S -> P." Region 16..247 /gene="SFTPA1"/region_name="Mature chain" /note="PULMONARY SURFACTANT-ASSOCIATED PROTEIN A." Region 27..99 /gene="SFTPA1" /region_name="Domain" /note="COLLAGEN-LIKE." Region 57..60 /gene="SFTPA1" /region_name=nConflict" /note="GPMG -> APWA (IN REF. 2)." Region 152..247 /gene="SFTPA1" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(154,245) /gene="SFTPA1" /bond_type="disulfide" /note="BY SIMILARITY." Site 206 /gene="SFTPA1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (PROBABLE)." Bond bond(223,237) /gene="SFTPA1" /bond_type="disulfide" /note="BY SIMILARITY." ORIGIN 1 mlllslaltl isapasdtcd tkdvcigspg ipgtpgshgl pgrdgrdgvk gdpgppgpmg 61 ppggmpglpg rdgligapgv pgergdkgep gergppglpa yldeelqatl helrhhalqs 121 igvlslqgsm kavgekifst ngqsvnfdai revcaraggr iavprsleen eaiasivker 181 ntyaylglae gptagdfyyl dgdpvnytnw ypgeprgqgr ekcvemytdg kwndknclqy 241 rlvicef SEQ ID NO: 84 NP_033186 surfactant associated protein D [Mus musculus] gi|6677921|ref|NP_033186.1|[6677921] sig_peptide 1 ..19 mat_peptide 20..374 /product=nsurfactant associated protein D" Region 260..373 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref="CDD:smart00034" . Region 271.374 /region_name="Lectin C-type domain" /note="lectin_c" /db_xref="CDD:pfam00059" CDS 1 ..374 /gene="Sftpd" /coded_by="NM_009160.1:43.. 1167" /db_xref="Locus!D:20390" /db_xref="MGD:109515" ORIGIN 1 mlpflsmlv! Ivqplgnlga emkslsqrsv pntctlvmcs ptenglpgrd grdgregprg . 61 ekgdpglpgp mglsglqgpt gpvgpkgeng sagepgpkge rglsgppglp gipgpagkeg 121 psgkqgnigp qgkpgpkgea gpkgevgapg mqgstgakgs tgpkgergap gvqgapgnag 181 aagpagpagp qgapgsrgpp glkgdrgvpg drgikgesgl pdsaalrqqm ealkgkiqri 241 evafshyqka alfpdgrsvg dkifrtadse kpfedaqemc kqaggqlasp rsatenaaiq 301 qlitahnkaa flsmtdvgte gkftyptgep Ivysnwapge pnnnggaenc veiftngqwn 361 dkacgeqrly icef SEQ ID NO: 85 1B08C Chain C, Lung Surfactant Protein D (Sp-D) (Fragment) gi|6573321|pdb|1B08|C[6573321] FEATURES Location/Qualifiers source 1..158 /organisrn="Homo sapiens" /db_xref="taxon:9606" SecStr 13.. 36 /sec_str_type=nhelixn /note=nhelix 7" Region 38.. 158 /region_name="Domain 3" /note="NCBI Domains" SecStr 39. .44 /sec_str_type=nsheet" /note="strand 21" SecStr 45..51 /sec_str_type="sheet"/note="strand 22" SecStr 53..56 /sec str_type="sheet" /note="strand 23" SecStr 57..67 /seclstr_type="helix" /note="helix 8" Bond bond(64,156) /bond_type="disulfide" SecStr 77..90 /sec_str_type="helix" /note="helix 9" SecStr 93..96 /sec_str_type="sheet" /note="strand 24" Hetjoin(bond(100),bond(100),bond(100),bond(104),bond(104), . bond(104),bond(127),bond(132),bond(133)) /heterogen="( CA, 8)" Het join(bond(104),bond(133),bond(133),bond(133)) /heterogen="( CA, 9 )" SecStr 107..110 /sec_str_type="sheet" /note="strand 25" SecStr 112..115 /sec_str_type="sheet" /note="strand 26" Het join(bond(124),bond(126),bond(132),bond(144),bond(145), bond(145),bond(145),bond(145),bond(145),bond(145), bond(145),bond(145),bond(145),bond(145),bond(145), bond(145),bond(145),bond(145),bond(145),bond(145)> bond(145),bond(145),bond(145),bond(145),bond(145),bond(145))/heterogen=n( CA, 7)" SecStr 133.. 139 /sec_str_type="sheet" /note="strand 27" Bond bond(134,148) /bond_type=ndisulfide" SecStr 141 ..147 /sec_str_type="sheet" /note="strand 28" SecStr 150.. 158 /sec_str_type="sheet"/note="strand 29" ORIGIN 1 eaeagsvasi rqqvealqgq vqhiqaafsq ykkvelfpng qsvgekifkt agfvkpftea 61 qllctqaggq lasprsaaen aalqqlwak neaaflsmtd sktegkftyp tgeslvysnw 121 apgepnddgg sedcveiftn gkwndracge krlvvcef SEQ ID NO: 86 1B08B Chain B, Lung Surfactant Protein D (Sp-D) (Fragment) gi|6573320|pdb| 1 B08|B[6573320] FEATURES Location/Qualifiers source 1..158 /organism="Homo sapiens" /db_xref="taxon:9606" SecStr 11..34 /se'c_str_type="helix,, /note="heiix 4" Region 37.. 158 /region_name="Domain 2" /note="NCBI Domains" SecStr 39..44 /sec_str_type="sheet" /note="strand.11" SecStr 45.. 51 /sec_str_type="sheet"/note="strand 12" SecStr 53..56 /sec_str type="sheet" /note="strand 13". SecStr 57..67 /sec_str_type="helix" /note="helix 5" Bond bond(64,156) /bond_type="disulfide" SecStr 77.. 90 /sec_str_type="helix" /note="heiix 6" SecStr 93..96 /sec_str_type="sheet" /note="strand 14" SecStr 97.. 100 /sec_str_type="sheet" /note="strand 15" Hetjoin(bond(100),bond(100),bond(100),bond(104),bond(104), bond(104),bond(127),bond(132),bond(133))/heterogen="( CA, 5)" Het join(bond(104),bond(133),bond(133),bond(133)) /heterogen="( CA, 6 )" SecStr 107.. 110 /sec_str_type="sheet" /note="strand 16" Hetjoin(bond(124),bond(126),bond(132),bond(144),bond(145), bond(145)) /heterogen="( CA, 4)" SecStr 133.. 139 /sec_str_type="sheet"/note="strand 17" Bond bond(134,148) /bond_type="disulfide" SecStr 141.. 147 /sec_str_type="sheef /note="strand 18"-SecStr 150..153/sec_str_type="sheef/note="strand 19" SecStr 154.. 158 /sec_str_type="sheet" /note="strand 20" ORIGIN 1 eaeagsvasi rqqveaiqgq vqhlqaafsq ykkvelfpng qsvgekifkt agfvkpftea 61 qllctqaggq lasprsaaen aalqqlwak neaaflsmtd sktegkftyp tgeslvysnw 121 apgepnddgg sedcveiftn gkwndracge krlvvcef - SEQ ID NO: 87 1B08A Chain A, Lung Surfactant Protein D (Sp-D) (Fragment) gi|6573319|pdb|1B08|A[6573319] FEATURES Location/Qualifiers source 1..158/organism="Homo sapiens" /db_xref="taxon:9606" SecStr 10..36 /sec_str_type="helix" /note="helix 1" Region 38..158 /region_name="Domain 1" /note="NCBI Domains" SecStr 39..44 /sec_str_type=" sheet" /note="strand 1" SecStr 45..51/sec_str_type="sheet"/note="strand 2" SecStr 53..56 /sec_str_type="sheet" /note="strand 3" SecStr 57..67 /sec_str_type=" helix" /note="heiix 2" Bond bond(64,156) /bond_type="disulfide" SecStr 77..90 /sec_str_type="helix" /note="heiix 3" SecStr 93..96 /sec_str_type="sheet" /note="strand 4" SecStr 97.: 100 /sec_str_type="sheet" /note="strand 5" Hetjoin(bond(100),bond(100),borid(100),bond(104),bond(104), bond(104),bond(127),bond(132),bond(133)) /heterogen="( CA, 2 )" Het join(bond(104),bond(133),bond(133),bond(133)) /heterogen="( CA, 3)" SecStr 107..110 /sec_str_type="sheef /note="strand 6" Hetjoin(bond(124),bond(126),bond(132),bond(144),bond(145), bond(145)) /heterogen="( CA, 1 )" SecStr 133.. 139 /sec_str_type="sheet" /note="strand 7" Bond bond(134,148) /bondJype="disulfide" SecStr 141 ..147 /sec_str_type="sheetn /note="strand 8" • SecStr 150.. 153 /sec_str_type="sheet"/note="strand 9" SecStr 154.. 158 /sec_str_type="sheef /nbte=" strand 10" ORIGIN 1 eaeagsvasi rqqveaiqgq vqhlqaafsq ykkvelfpng qsvgekifkt agfvkpftea 61 qllctqaggq lasprsaaen aalqqlwak neaaflsmtd sktegkftyp tgeslvysnw 121 apgepnddgg sedcveiftn gkwndracge krlwcef SEQ ID NO: 88 NP_060049 deleted in malignant brain tumors 1 isoform c precursor [Homo sapiens] gi|8923740|ref|NP_060049.1 ([8923740] sig_peptide 1..25 mat_peptide 26..2403 /product="deleted in malignant brain tumors 1 isoform c" Region 102..202 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 105..202 /region_narne="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530" Region 234..334 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 237..334 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 363..463 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 366..463 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530B Region 484..584 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 487..'584 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530" Region 594..692 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 595..692 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD: pfam00530" Region 723..823 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 726..823 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 852..952 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 855..952 /region_name=BScavenger receptor cysteine-rich domain" /note="SRCR" /db_xref=,,CDD:pfam00530" Region 983..1083 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 986..1083 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR,7db_xref="CDD:pfam00530" Region 1112..1212 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SRu Region 1115.. 1212 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 1241.1341 /region_name="Scavenger receptor Cys-rich" /note="SR" ./db_xref="CDD:SR" Region 1244..1341 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530" Region 1370.. 1470 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 1373.. 1470 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530" Region 1499.. 1599 /region_name="Scavenger receptor Cys-rich" /note=nSR" /db_xref="CDD:SR" Region 1502.. 1599 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfgm00530" Region 1630.. 1730 /region_name="Scavenger receptor Cys-rich". /note="SR" /db xref="CDD:SR" Region 1633.. 1730 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR,7db_xref="CDD:pfam00530" Region 1756.. 1867/regionjiame="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:CUB" Region 1756..1864/region_name="CUB domain"/note="CUB" /db_xref="CDD:pfam00431" Region 1873..1976 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xreN"CDD:SR" Region 1885.. 1976 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530" Region 1998..2106 /region_name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:CUB" Region 1998..2104 /region_name="CUB domain" /note-'CUB" /db_xref="CDD:pfam00431" Region 2117..2371 /region_name="Zona pellucida-like domain" /note="zona_pellucida" /db_xref="CDD:pfam00100" Region 2117..2368 /region_name="Zona pellucida (ZP) domain" /note="ZP" /db_xref="CDD:ZP" . CDS 1..2403 /gene="DMBT1" /coded_by="NM_017579.1:107..7318" /note="isoform c is encoded by transcript variant 3" /db_xref="LocuslD:1755" /db_xref="MIM:601969n ORIGIN 1 mgistvilem cllwgqvist ggwiprttdy aslipsevpl dttvaegspf pseltlesta ■6 12 18- 24 30 36 42 48 54 60 66 72 78 84 90 96 102 108 114 120 126 132 138 144 150 156 162 168 174 180 186 aegspisles tlestvaegs lipsestles tvaegsdsgl alrlvngdgr cqgrveilyr gswgtvcdds wdtndanwc rqlgcgwams apgnawfgqg sgpialddvr csghesylws cphngwlshn cghgedagvi csaaqpqstl rpeswpvris ppvptegses sla|rivngg drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd vrcsghesyl wscphngwlt hncghsedag vicsaplsrp tpspdtwpts hastagpess lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanw crqlgcgwat sapgnarfgq gsgpivlddv rcsgyesylw scphngwlsh ncqhsedagv icsdtlptit Ipastvgses slalrlvngg drcqgrvevl yrgswgtvcd dswdtndanv vcrqlgcgwa mlapgnarfg qgsgpivldd vrcsgnesyl wscphngwls hncghsedag vicsgpessl alglvnggdr cqgrvevlyr gswgtvcdds wdtndanwc rqlgcgwats apgnarfgqg sgpivlddvr csghesylws cpnngwlshn cghhedagvi csaaqsrstp rpdtlstitl ppstvgsess Itlrlvngsd rcqgrvevly rgswgtvcdd swdtndanw crqlgcgwat sapgnarfgq gsgpivlddv rcsghesyiw scphngwlsh ncghhedagv icsvsqsrpt pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr gswgtvcdds wdtsdanwc rrlgcgwats apgnarfgqg sgpivlddvr csgyesylws cphngwlshn cqhsedagvi csaahswstp spdtlptitl pastvgsess lalrlvnggd rcqgrvevly qgswgtvcdd swdtndanw crqigcgwam sapgnarfgq gsgpivlddv rcsghesyiw scphngwlsh ncghsedagv icsasqsrpt pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr gswgtvcddy wdtndanwc rqlgcgwams apgnarfgqg sgpivlddvr csghesylws cphdgwlshn cghhedagvi csasqsqptp spdtwptsha stagsessla Irlvnggdrc qgrvevlyrg pwgtvcddyw dtndanwcr qlgcgwatsa pgnarfgqgs gpivlddvrc sghesylwsc phngwlshnc ghhedagvic sasqsqptps pdtwptshas tagsesslal rivnggdrcq grvevlyrgs wgtvcddywd tndanwcrq Igcgwatsap gsarfgqgsg pialddvrcs ghesylwscp hngwlshncg hhedagvics asqsqptpsp dtwptsrast agsestlalr Ivnggdrcrg rvevlyqgsw gtvcddywdt ndanwcrql gcgwamsapg naqfgqgsgp ivlddvrcsg hesyjwscph ngwlshncgh hedagvicsa aqsqstprpd twlttnlpal tvgsesslal rlvnggdrcr grvevlyrgs wgtvcddswd tndanwcrq Igcgwamsap gnarfgqgsg pivlddvrcs gnesylwscp hkgwlthncg hhedagvics atqinstttd wwhpttttta rpssncggfl fyasgtfssp sypayypnna kcvweievns gyrinlgfsn Ikleahhncs fdyveifdgs Insslllgki cndtrqifts synrmtihfr sdisfqntgf lawynsfpsd atlrlvnlns syglcagrve iyhggtwgtv cddswtiqea ewcrqlgcg 1921 ravsaignay fgsgsgpitl ddvecsgtes tlwqcrnrgwfshncnhred agvicsgnni 1981 stpapflnit rpntdyscgg flsqpsgdfs spfypgnypn nakcvwdiev qnnyrvtvif 2041 rdvqleggcn ydyievfdgp yrsspliarv cdgargsfts ssnfmsirfi sdhsitrrgf 2101 raeyysspsn dstnllcipn hmqasvsrsy Iqslgfsasd Ivistwngyy ecrpqitpnl 2161 viftipysgc gtfkqadndt idysnfltaa vsggiikrrt dlrihvscrm Iqntwvdtmy 2221 randtihvan ntiqveevqy gnfdvnisfy tsssflypvt srpyyvdlnq dlyvqaeilh 2281 sdavltlfvd tcvaspysnd ftsltydlir sgcvrddtyg pysspsiria rfrfrafhfl 2341 nrfpsvylrc kmvvcraydp ssrcyrgcvi rskrdvgsyq ekvdwlgpi qiqtpprree 2401 epr SEQ ID NO: 89 NP_015568 deleted in malignant brain tumors 1 isoform b precursor [Homo sapiens] gi|6633801]ref|NP_015568.1|[6633801] sig_peptide 1..25 mat_peptide 26..2413 /product="deleted in malignant brain tumors 1. isoform b" Region 102..202 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 105..202 /region_name="Scavenger receptor cysteine-rich domain" /note=BSRCR"/db_xref="CDD:pfam00530" Region 234..334 /region_name=,'Scavenger receptor Cys-rich" /note=,fSR" /db_xref="CDD:SR" Region 237..334 /region_name="Scavenger receptor cysteine-rich domain" /note=,,SRCRM/db_xref=HCDD:pfam00530" Region 363..463 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 366..463 /region name="Scavenger receptor cysteine-rich domain" /note="SRCRn /dbjcref=~CDD:pfam00530" Region 494..594 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 497..594 /region name="Scavenger receptor cysteine-rich domain" /note="SRCRM/db_xref="CDD:pfam00530" Region 602..702 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 605..702 /region name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref=7CDD:pfam00530" Region 733..833 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 736..833 /region name="Scavenger receptor cysteine-rich domain" /note^SRCR^db.xref^CDDipfamOOSSO" Region 862..962 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 865..962 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530n Region 993.. 1093 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 996.. 1093 /region name-'Scavenger receptor cysteine-rich domain" /note="SRCRM/db_xref^"CDD:pfam00530n Region 1122.. 1222 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref=nCDD:SR" Region 1125.. 1222 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfam00530H Region 1251.. 1351 /region_name="Scavenger receptor Cys-rich" /note=nSR" /db_xref=,,CDD:SR" Region 1254.. 1351 /regionjiame="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530H Region 1380.. 1480 /regionjname-'Scavenger receptor Cys-rich" /note=MSR" /db_xref="CDD:SR" Region 1383.. 1480 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 1509.. 1609 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref=BCDD:SRH Region 1512.. 1609 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/dbjcref="CDD:pfam00530" Region 1640.. 1740 /region_name="Scavenger receptor Cys-rich" /note="SR" /dbjcref=flCDD:SR" Region 1643.. 1740 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR"/db_xref="CDD:pfamOG530" Region 1766.. 1877 /region_name=nDomain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUBM /db_xref="CDD:CUB" Region 1766..1874 /region_name="CUB domain" /note="CUB" /dbjcref=HCDD:pfam00431" Region 1883..1986 /regionjiame-'Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SRM Region 1895.. 1986 /regionjiame="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 2008..2116 /regionjiame="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:CUB" Region 2008..2114 /region_name="CUB domain" /note="CUB" /db_xref="CDD:pfam00431" Region 2127..2381 /region_name="Zona pellucida-like domain" /note="zona_pelIucida,!/db_xref="CDD:pfam00100n Region 2127..2378 /region_name="Zona pellucida (ZP) domain" /note="ZP" /db_xref="CDD:ZP" CDS 1..24137gene="DMBT1" /coded J)y="NMJ)07329.1:107..7348H /db_xref^TocuslD:1755"/db_xref^"MIM:601969" ORIGIN 1 mgistvilem cilwgqvlst ggwiprttdy aslipsevpl dqtvaegspf psestlesta 61 aegspisles tlestvaegs lipsestles tvaegsdsgl alrlvngdgF cqgrveilyr 121 gswgtvcdds wdtndanvvc rqigcgwams apgnawfgqg sgpialddvr csghesylws 181 cphngwlshn cghgedagvi csaaqpqstl rpeswpvris ppvptegses slalrlvngg 241 drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd 301 vrcsghesyl wscphngwlt hncghsedag vicsapqsrp tpspdtwpts hastagpess 361 lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanw crqlgcgwat sapgnarfgq 421 gsgpivlddv rcsgyesyiw scphngwlsh ncqhsedagv icsaahswst pspdtiptit 481 Ipastvgses slalrlvngg drcqgrvevi yrgswgtvcd dswdtndanv vcrqlgcgwa 541 mlapgnarfg qgsgpivldd vrcsgnesyl wscphngwls hncghsedag vicsgpessl 601 alrlvnggdr cqgrvevtyr gswgtvcdds wdtndanvvc rqigcgwams apgnarfgqg 661 sgpivlddvr csghesylws cpnngwlshn cghhedagvi csaaqsrstp rpdtlstitl 721 ppstvgsess Itlrlvngsd rcqgrvevly rgswgtvcdd swdtndanw crqlgcgwam 781 sapgnarfgq gsgpivlddv rcsghesylw scphngwlsh ncghhedagv icsvsqsrpt 841 pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr gswgtvcdds wdtsdanvvc 901 rqlgcgwats apgnarfgqg sgpivlddvr csgyesylws cphngwlshn cqhsedagvi 961 csaahswstp spdtlptitl pastvgsess lalrlvnggd rcqgrvevly qgswgtvcdd 1021 swdtndanw crqpgcgwam sapgnarfgq gsgpivlddv rcsghesypw scphngwlsh 1081 ncghsedagv icsasqsrpt pspdtwpts'h astagsessl alrlvnggdr cqgrvevlyr 1141 gswgtvcddy wdtndanvvc rqigcgwams apgnarfgqg sgpivlddvr csghesylws 1201 cphngwlshn cghhedagvi csasqsqptp spdtwptsha stagsessla Irlvnggdrc 1261 qgrvevlyrg swgtvcddywdtndanwcrqlgcgwatsa pgnarfgqgs gpivlddvrc 1321 sghesylwsc phngwlshncghhedagvic sasqsqptps pdtwptshas tagsesslal 1381 rlvnggdrcq grvevlyrgs wgtvcddywd tndanwcrq Igcgwatsap gnarfgqgsg 1441 pivlddvrcs ghesylwscp hngwlshncg hhedagvics asqsqptpsp dtwptsrast 1501 agsestlalr Ivnggdrcrg rvevlyqgsw gtvcddywdt ndanwcrql gcgwamsapg .1561 naqfgqgsgp ivlddvrcsg hesylwscph ngwlshncgh hedagvicsa aqsqstprpd 1621 twtttnlpal tvgsessial rlvnggdrcr grvevlyrgs wgtvcddswd tndanwcrq 1681 Igcgwamsap gnarfgqgsg pivlddvrcs gnesylwscp hkgwlthncg hhedagvics 1741 atqinstttd wwhpttttta rpssncggfl fyasgtfssp sypayypnna kcvweievns 1801 gyrinlgfsn Ikleahhncs fdyveifdgs insslllgki cndtrqifts synrmtihfr 1861 sdisfqntgf lawynsfpsd atlrlvnlns syglcagrve iyhggtwgtv cddswtiqea 1921 ewcrqlgcg ravsalgnay fgsgsgpitl ddvecsgtes tlwqcrnrgw fshncnhred 1981 agvicsgnhl stpapflnit rpntdyscgg flsqpsgdfs spfypgnypn nakcvwdiev 2041 qnnyrvtvif rdvqleggcn ydyievfdgp yrsspliarv cdgargsfts ssnfmsirfi 2101 sdhsitrrgf raeyysspsn dstnllclpn hmqasvsrsy Iqslgfsasd Ivistwngyy 2161 ecrpqitpnl viftipysgc gtfkqadndt idysnfltaa vsggiikrrt dlrihvscrm 2221 Iqntwvdtmy iandtihvan ntiqveevqy gnfdvnisfy tsssflypvt srpyyvdlnq 2281 dlyvqaeilh sdavltlfvd tcvaspysnd ftsltydlir sgcvrddtyg pysspslria 2341 rfrfrafhfl nrfpsvylrc kmwcraydp ssrcyrgcvl rskrdvgsyq ekvdwlgpi 2401 qiqtpprree epr SEQ ID NO: 90 NP_004397 deleted in malignant brain tumors 1 isoform a precursor [Homo sapiens] gi|4758170|ref|NP_004397.1|[4758170] sig_peptide 1..25 mat_peptide 26.. 1785 /product="deIeted in malignant brain tumors 1 isoform a" Region 102..202 /region_name="Scavenger receptor Cys-rich" /note="SRn /dbjcref="CDD:SR" Region 105..202 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCRVdbjcref=HCDD:pfam00530" Region 234..334 /regionjiame="Scavenger receptor Cys-rich" /note="SR" /db_xref=BCDD:SR" Region 237..334 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCRM /db_xref=MCDD:pfam00530H Region 363..463 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref=nCDD:SR" Region 366..463 /region_name="Scavenger receptor cysteine-rich domain" /note=nSRCR"/dbjcref=HCDD:pfam00530" Region 494..594 /region_name'="Scavenger receptor Cys-rich" /note^'SR" /db_xref="CDD:SR" Region 497..594 /region_name="Scavenger receptor cysteine-rich domain" /note=,,SRCRn /db.xref=nCDD:pfam00530" Region 623.J23 /region_name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Regbn 626-723 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db-xref="CDD:pfam00530" Region 752..852 /region_name="Scavenger receptor Cys-rich" /note="SR" 7db xref="CDD:SRn Region 755..852 /region_name=nScavenger receptor cysteine-rich domain" /note="SRCR'7db_xref="CDD:pfam00530" Region 881.981. /region_name="Scavenger receptor Cys-rich" /note-'SR" /db_xref="CDD:SR" Region 884..981 /region_name="Scavenger receptor cysteine-rich domain" /note="SRCR" /db_xref="CDD:pfam00530" Region 1012..1112 /region__name="Scavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 1015..1112 /region_name="Scavenger receptor cysteine-rich domain" /note=nSRCR" /dbjcref="CDD:pfam00530" Region 1138..12497regionjiame="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUBn /db„xref=nCDD:CUB" Region 1138..1246/regionjiame="CUB domain,7note="CUBI, /db_xref="CDD:pfam00431" Region 1255.. 1358 /region_name=nScavenger receptor Cys-rich" /note="SR" /db_xref="CDD:SR" Region 1267..1358 /region_name="Scavenger receptor cysteine-rich domain" /note^SRCRVdbjcref^'CDDipfamOOSSO' Region 1380..1488/region__name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note=nCUB" /db_xref="CDD:CUB" Region 1380.. 1486 /region_name="CUB domain" /note=wCUB" /db_xref="CDD:pfam00431" Region 1499.. 1751 /region_name="Zona peliucida-Iike domain" /note="zona jpellucida" /db„xref="CDD:pfam00100" Region 1499..1750 /region_name="Zona pellucida (ZP) domain" /note="ZP" /db_xref="CDD:ZP" CDS 1..1785/gene="DMBT1"/coded_by="NM_004406.1:107..5464" /db.xref="LocuslD:1755"/db_xref="MIM:601969" ORIGIN 1 mgistvilem cllwgqvlst ggwiprttdy aslipsevpl dqtvaegspf psestlesta 61 aegspisles tlestvaegs lipsestles tvaegsdsgl alrivngdgr cqgrveilyr 121 gswgtvcdds wdtndanwc rqigcgwams apgnawfgqg sgpiaiddvr csghesylws 181 cphngwlshn cghgedagvi csaaqpqstl rpeswpvris ppvptegses slalrivngg 241 drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd 301 vrcsghesyl wscphngwlt hncghsedag vicsapqsrp tpspdtwpts hastagpess 361 lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanw crqlgcgwat sapgnarfgq 421 gsgpivlddv rcsgyesylw scphngwlsh ncqhsedagv icsaahswst pspdtiptit 481 Ipastvgses slalrivngg drcqgrvevl yqgswgtvcd dswdtndanv vcrqpgcgwa 541 msapgnarfg qgsgpivldd vrcsghesyp wscphngwls hncghsedag vicsasqsrp 601 tpspdtwpts hastagsess lalrlvnggd rcqgrvevly rgswgtvcdd ywdtndanw 661 crqlgcgwam sapgnarfgq gsgpivlddv rcsghesyiw scphngwlsh ncghhedagv 721 icsasqsqpt pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr gswgtvcddy 781 wdtndanwc rqlgcgwats apgnarfgqg sgpivlddvr csghesylws cphngwlshn 841 cghhedagvi csasqsqptp spdtwptsra stagsestla Irlvnggdrc rgrvevlyqg 901 swgtvcddyw dtndanvvcr qigcgwamsa pgnaqfgqgs gpivlddvrc sghesylwsc 961 phngwlshnc ghhedagvic saaqsqstpr pdtwlttnlp altvgsessl alrlvnggdr 1021 crgrvevlyr gswgtvcdds wdtndanwc rqigcgwams apgnarfgqg sgpivlddvr 1081 csgnesylws cphkgwlthn cghhedagvi csatqinstt tdwwhptttt tarpssncgg 1141 flfyasgtfespsypayypn nakcvweiev nsgyrinlgf snlkleahhn csfdyveifd 1201 gslnsslllg kicndtrqif tssynrmtih frsdisfqnt gflawynsfp sdatlrlvnl 1261 nssyglcagr veiyhggtwg tvcddswtiq eaewcrqlg cgravsalgn ayfgsgsgpi ' 1321 tlddvecsgt estlwqcrnr gwfshncnhr edagvicsgn hlstpapfin itrpntdysc 1381 ggflsqpsgd fsspfypgny pnnakcvwdi evqnnyrvtv ifrdvqlegg cnydyievfd 1441 gpyrssplia rvcdgargsf tsssnfmsirfisdhsitrrgfraeyyssp sndstnllcl 1501 pnhmqasvsr sylqslgfsa sdlvistwng yyecrpqitp nlviftipys gcgtfkqadn 1561 dtidysnflt aavsggiikr rtdlrihvsc rmiqntwvdt myiandtihv anntiqveev 1621 qygnfdvnis fytsssflyp vtsrpyyvdl nqdlyvqaei Ihsdavltlf vdtcvaspys 1681 ndftsltydl irsgcvrddt ygpysspslr iarfrfrafh flnrfpsvyl rckmvvcray 1741 dpssrcyrgc vlrskrdvgs yqekvdwlg piqlqtpprr eeepr SEQIDNO:91 LNBOC1 pulmonary surfactant protein C - bovine gi|7428752|pir||LNBOC1 [7428752] FEATURES Location/Qualifiers source 1..34 /organism="Bos taurus" /db_xref="taxon:9913" Protein 1..34 /product="pulmonary surfactant protein C" /note=Hpulmonary surfactant protein PSP-6" Site 4 /site^type-'binding" /note="palmitate (Cys) (covaient)" Site 5 /site_type="binding" /note="palmitate (Cys) (covaient)" ORIGIN 1 lipccpvnik rllivvvvvv llvvvivgal Imgl SEQ ID NO; 92 LNDGC1 pulmonary surfactant protein C-dog gi|7428750|pir||LNDGC1 [7428750] FEATURES Location/Qualifiers source 1..35 /organism-'Canis famiiiaris" /db_xref="taxon:9615" Protein 1 ..35 /product="pulmonary surfactant protein C" Site 5 /site_type="binding" /note="palmitate (Cys) (covaient)" ORIGIN 1 Igipcfpssl krlliivwi vlvwvivga llmgl // SEQ ID NO: 93 JN0450 conglutinin precursor - bovine gi|346501|pir||JN0450[346501] FEATURES Location/Qualifiers source 1..371 /organism="Bos taurus" /db_xref="taxon:9913" Protein 1.-.371 /product="conglutinin precursor"/note=nC3b-binding protein" Region 1..20/region_name="domain"/note=,,signal sequence" Region 21..371 /region_name="product,7note="conglutinin" Region 46..214 /region_name="region" /note="collagen-iike" Site 63 /site_type="binding" /note="carbohydrate (Lys) (covaient)" Site 63 /siteJype="modified" /note="5-hydroxylysine (Lys)n Region 75..371 /regionjiame="product"/note="conglutinin-N" Site 78 /siteJype="modified" /note="4-hydroxyproiine (Pro)" Site 87 /site_type=wbinding" /note="carbohydrate (Lys) (covaient)" Site 87 /siteJype=Hmodified" /note="5-hydroxylysine (Lys)"-Site 96 /siteJype=wmodified" /note=n4-hydroxyproline (Pro)" Site 99 /site_type="binding" /note="carbohydrate (Lys) (covaient)" . Site 99 /site_type="modified" /note="5-hydroxylysine (Lys)" Site 108 /site_type="modrfied" /note="4-hydroxyproline (Pro)" Site 111 /site_type="modifiedn /note="4-hydroxyproline (Pro)" Site 129 /siteJype="rnodified" /note="4-hydroxyproiine (Pro)" • Site 132 /siteJype^modifiecT /note=n4-hydroxyproline (Pro)" Site 135 /site_type="binding" /note="carbohydrate (Lys) (covaient)" Site 135 /siteJype="modified" /note="5-hydroxy|ysine (Lys)" • Site 141 /sitejype="binding" /note=Mcarbohydrate (Lys) (covaient)" Site 141 /site_type=nmodified" /note="5-hydroxyiysine (Lys)" . Site 147 /site_type="modified" /note="4-hydroxyproline (Pro)" -Site 153 /site_Jype="modified" /note="4-hydroxyproiine (Pro)" Site 159/site_type="binding"/note="carbohydrate (Lys) (covaient)" Site 159 /site_type="modified" /note="5-hydroxylysine (Lys)" Site 162/site_type="binding,7note="carbohydrate (Lys) (covaient)" Site 162 /siteJype="modified" /note="5-hydroxylysine (Lys)" Site 171 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 195 /siteJype="modified" /note="4-hydroxyproiine (Pro)" Site 198/site_type="binding,7note="carbohydrate (Lys) (covaient)" Site 198 /siteJype="modified" /note="5-hydroxy lysine (Lys)" Site 210 /site_type="bindingf7note="carbohydrate (Lys) (covaient)" Site 210 /site.Jype^modified" /note=n5-hydroxylysine (Lys)" Reaion 248.-369 /reglon_name="domainM /note="C-type lectin homology #label LCH" Site 337 /site_type="binding" /note="carbohydrate (Asn) (covaient)" ORIGIN 1 mlllplsvll Iltqpwrsig aemttfsqki lanactlvmc splesglpgh dgqdgrecph 61 gekgdpgspg pagragrpgw vgpigpkgdn gfvgepgpkg dtgprgppgm pgpagregps 121 gkqgsmgppg tpgpkgetgp kggvgapgiq gfpgpsglkg ekgapgetga pgragvtgps 181 gaigpqgpsg argppglkgd rgdpgetgak gesgiaevna Ikqrvtildg hlrrfqnafs 241 qykkavlfpd gqavgekifk tagavksysd aeqlcreakg qlasprssae neavtqmvra 301 qeknaylsmn distegrfty ptgeilvysn wadgepnnsd egqpencvei fpdgkwndvp 361 cskqllvicef SEQIDNO:94 A45225 pulmonary surfactant protein D precursor - human gi|346375|pir||A45225[346375] FEATURES Location/Qualifiers source 1..375 /organism="Homo sapiens" /db_xref="taxon:9606" Protein 1 ..375 /product="pulmonary surfactant protein D precursor" /note="SP-D" Region 1..20 /region_name=,Idomain" /note="signal sequence" Region 21 ..375 /regionjiame="product" /note="pulmonary surfactant protein D" Region 21..45 /region_name="domain" /note="non-colIagenous" Region 46..222 /region_name="domain" /note="collagenous" Site 90 /site_type="binding" /note="carbohydrate (Asn) (covaient)" Region 223..375 /region_name="domain" /note="non-collagenous" Region 254..373 /region_name="domain" /note="C-type lectin homology #Iabel LCH" Bond bond(281,373) /bond_type="disu(fide" Bond bond(351,365) /bond_type="disulfide" ORIGIN 1 mllfllsalv lltqplgyle aemktyshrt mpsactlvmc ssvesgipgrdgrdgregpr 61 gekgdpglpg aagqagmpgq agpvgpkgdn gsvgepgpkg dtgpsgppgp pgvpgpagre 121 galgkqgnig pqgkpgpkge agpkgevgap gmqgsagarg lagpkgergv pgergvpgnt 181 gaagsagamg pqgspgargp pglkgdkgip gdkgakgesg Ipdvaslrqq vealqgqvqh 241 Iqaafsqykk velfpngqsv gekifktagf vkpfteaqll ctqaggqlas prsaaenaal 301 qqlwaknea afismtdskt egkftyptge slvysnwapg epnddggsed cveiftngkw 361 ndracgekrl wcef SEQ ID NO: 95 LNHUC pulmonary surfactant protein C precursor, long splice form - human ai|71983|pir||LNHUC[71983J FEATURES Location/Qualifiers source 1-197 /organism="Homo sapiens" ydbjcref="taxon:9606" Protein 1..197 /product-'pulmonary surfactant protein C precursor, long splice form" /note="3.7 kDa surfactant polypeptide; pulmonary surfactant protein SP5; pulmonary surfactant proteolipid SP-C; pulmonary surfactant proteolipid SPL(pVal)" Region 1..197 /region_name="product" /note="pulmonary surfactant protein C precursor, short splice form" Region 1..145 /region_name=Mproduct" /note="puimonary surfactant protein C precursor, short splice form" Region 1..23 /region_name=wdomainM /note="propeptidew Region 24„58 /region jiame=nproducf /note="pulmonary surfactant protein C" Site 28 /site_type="binding" /note="palmitate (Cys) (covalent)" Site 29 /site_type="binding" /note="palmitate.(Cys) (covalent)" Region 152.. 197 /region_name="producf /note="pulmonary surfactant protein C precursor, short splice form" ORIGIN 1 mdvgskevlm esppdysaap rgrfgipccp vhlkrilivv wwlivvvi vgallmglhm 61 sqkhtemvle msigapeaqq rlalsehlvt tatfsigstg Iwydyqqll iaykpapgtc 121 cyimkiapes ipslealnrk vhnfqmecsl qakpavptsk Igqaegrdag sapsggdpaf 181 Igmavntlcg evplyyi SEQ ID NO: 96 LNDGPS pulmonary surfactant protein A precursor - dog gij71970|pirj|LNDGPS[71970] FEATURES Location/Qualifiers source 1..248 /organism="Canis familiaris" /db_xref="taxon:9615" Protein 1..248 /product="pulmonary surfactant protein A precursor" /note=npulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A" Region 1..17 /region_name=,,domain" /note="signal sequence" Region 18..248 /region_narne=Mproduct" /note="pulmonary surfactant protein A" Site 20 /site_type=nbinding" /note="carbohydrate (Asn) (covalent)" Region 28.. 102 /region_name=Mregion" /note="collagen-Iike'1 Site 30 /site_type="modifiedn /note="4-hydroxyproline (Pro)" Region 127..246 /region_name="domain" /note="C-type lectin homology #label LCH" Site 207 /site_type="binding" /note="carbohydrate (Asn) (covalent)" ORIGIN 1 mwlrclalal tllmvsgien ntkdvcvgnp gipgtpgshg Ipgrdgrdgv kgdpgppgpl 61 gppggmpghp gpngmtgapg vagergekge pgergppglp asldeelqtt Ihdlrhqilq 121 tmgvlslhes llwgrkvfs sgaqsinfnd iqelcagagg qiaapmspee neavasivkk 181 yntyaylglv espdsgdfqy mdgapvnytn wypgeprgrg keqcvemytd gqwnnknclq 241 yrlaicef SEQ ID NO: 97 LNHUPS pulmonary surfactant protein A precursor (genomic clone) - human gi|71967|pir|)LNHUPS[71967] FEATURES Location/Qualifiers source 1..248 /organism="Homo sapiens" /db_xref="taxon:9606" Protein 1 ..248 /product=wpulmonary surfactant protein A precursor (genomic clone)" /note="alveolar proteinosis protein; pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein (PSP-A)" Region 1 ..20 /region_name="domain" /note="signal sequence" Region 21..248 /regionjiame=l,producf /note="pulmonary surfactant protein A" Bond bond(26) /bond_type="disulfiden /note="interchainw Region 28..100 /region_name=ndomain" /note="collagenous" Site 30 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 33 /siteJype=nmodlfied,, /note=n4-hydroxyproline (Pro)" Site' 36 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 42 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 51 /siteJype=,,modified" /note="5-hydroxylysine (Lys)" Site 57 /sitejype-'modified" /note="4-hydroxyproline (Pro)" Site 63 /siteJype="modifiedM /note="4-hydroxyproiine (Pro)" Site 76 /site_type="modified" /note="4-hydroxyproline (Pro)" Site 79 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 82 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 88 /site_type="modified" /note="5-hydroxylysine (Lys)" Site 91 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 97 /site_type="modifiedH /note="4-hydroxyproline (Pro)" Region 127..246 /region_name=ndomain,7note="C-type lectin homology #label LCH" Bond bond(155,246) /bond_type=,,disulfide" Site 207 /site Jype="binding" /note="carbohydrate (Asn) (covalent)" Bond bond(224,238) /bond_type=ndisulfide" ORIGIN 1 mwlcplalnl ilmaasgavc evkdvcvgsp.gipgtpgshg Ipgrhgrdgl kgdigppgpm 61 gppgempcpp gndglpgapg ipgecgekge pgergppglp ahldeeiqat Ihdfrhqilq 121 trgalslqgs imtvgekvfs sngqsitfda iqeacaragg riavprnpee neaiasfvkk 181 yntyayvglt egpspgdfry sdgtpvnytn wyrgepagrg keqcvemytd gqwndrncly 241 srlticef SEQ ID NO: 98 A53570 collectin-43 - bovine gi|1083017|pir||A53570[1083017] FEATURES Location/Qualifiers source 1..301 /organism=,,Bos taurus" l6bj(ref^,liaxor\:9Q13" Protein 1..301 /produ'ct=ncol)ectin«43M/note=,,lectin CL-43" Region 177..299 /region^ame^'domain" /note="C-type lectin homology #label LCH" ORIGIN 1 eemdvysekt Itdpctlwc appadslrgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdrgdpgekgarg etsvlevdtl rqrmrnlege vqrlqnivtq yrkavlfpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepnnrak degpenclei ysdgnwndie creerivice 301 f SEQ ID NO: 99 S33603 surfactant protein D - bovine gi|423283|pir||S33603[423283 FEATURES Location/Qualifiers source 1..369 /organism="Bos taurus" /db_xref="taxon:9913" Protein 1..369 /product="surfactant protein D" Region 248..367 /region name="domainM /note="C-type lectin homology #label LCH" ORIGIN 1 mlllplsvll lltqpwrslg aemkiysqkt manactlvmc sppedglpgr dgrdgregpr 61 gekgdpgspg pagragmpgp.agpiglkgdn gsagepgpkg dtgppgppgm pgpagregps ■ 121 gkqgsmgppg tpgpkgdtgp kggvgapgiqgspgpaglkg ergapgdpga pgragapgpr 181 gaigpqgpsg argppglkgd rgtpgergak gesglaevna Irqrvgileg qlqrlqnafs 241 qykkamlfpn grsvgekifk tvgsektfqd aqqictqagg qlpsprsgae nealtqlata 301 qnkaaflsms dtrkegtfiy ptgeplvysn wapqepnndg gsencveifp ngkwndkvcg 361 eqrlvicef SEQIDNO:100 AAF28384 lung surfactant protein A [Sus scrofa] gi|6782434|gb|AAF28384.1 |AF133668 J [6782434] FEATURES Location/Qualifiers source 1..T16 /organism="Sus scrofa" /db_xref="taxon:9823" Protein SEQIDNO:101 AAF22145 lung surfactant protein D precursor; SPD; SP-D; CP4 [Sus scrofa] gi|6760482|gbiAAF22145.2|AF132496J[6760482] sig_peptide 1..20 mat_peptide 21 ..378 /product="lung surfactant protein D" CDS.1 ..378 /gene=,,SFTPD" /coded_by="AF132496.2:44.. 1180" ORIGIN 1 mlllpisvli Iitqpprslg aemktysqra vanacalvmc spmenglpgr dgrdgregpr 61 gekgdpglpg avgragmpgl agpvgpkgdn gstgepgakg digpcgppgp pgipgpagke 121 gpsgqqgnig ppgtpgpkge tgpkgevgal gmqgstgarg paglkgerga pgergapgsa 181 gaagpagatg pqgpsgargp pglkgdrgpp gergakgesg Ipgitalrqq vetlqgqvqr 241 Iqkafsqykk velfpngrgv gekifktggf ektfqdaqqv ctqaggqmas prseteneal 301 sqlvtaqnka aflsmtdikt egnftyptge plvyanwapg epnnnggssg aencverfpn 361 gkwndkacge Irlvicef SEQIDNOM02 P15783 PULMONARY SURFACTANT-ASSOCIATED PROTEIN C (SP-C) (PULMONARY SURFACTANT-ASSOCIATED PROTEOLIPID SPL(VAL)) gi|131422|sp|P15783|PSPC_BOVIN[131422]' FEATURES Location/Qualifiers source 1..34 /organism="Bos taurus" /db_xref="taxon:9913" gene 1..34 /gene=MSFTPC" /note="SFTP2" Protein 1 ..34 /gene="SFTPC" /product="PULMONARY SURFACTANT-ASSOCIATED PROTEIN C" Site 4 /gene="SFTPC" /site_type="lipid-binding" /note="PALMITATE (BY SIMILARITY)." Site 5 /gene="SFTPC" /site_type="lipid-binding" /note="PALMITATE (BY SIMILARITY).'" Region 21 /gene="SFTPC" /region_name="Conflicr /note="L -> V (IN REF. 2)." Region 26./gene="SFTPC" /region_name="Conflict" /note="l -> V (IN REF. 2)." Region 28..34 /gene="SFTPC" /region name="Conflict" /hote="GALLMGL -> IGAMLAM (IN REF. 2)." ORIGIN 1 lipccpvnik rlliwvvw llvwivgal Imgl SEQIDNOM03 P35246 PULMONARY SURFACTANT-ASSOCIATED PROTEIN D PRECURSOR (SP-D) (PSP-D) gj|464485|sp|P35246|PSPD_BOVIN[464485] FEATURES Location/Qualifiers source 1..369 /organism="Bos taurus" /db xref="taxon:9913" gene 1..369 /gene="SFTPD" /note="SFTP4" Protein 1..369 /gene="SFTPD" /product="PULMONARY SURFACTANT-ASSOCIATED PROTEIN D PRECURSOR" Region 1..20 /gene="SFTPD" /region_name="Signar /note="BY SIMILARITY." Region 21.369 /gene-'SFTPD" /region_name="Mature chain" /note=BPULMONARY SURFACTANT-ASSOCIATED PROTEIN D." Region 46..216 /gene="SFTPD" /region_name="Domain" /note="COLLAGEN-LIKE." Site 78 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Site 87 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Site 90 /gene="SFTPD" /site_type="glycosylation" /note="POTENTIAL." Site 96 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Site 99 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Site 165 /gene="SFTPD" /site_type="hydroxylation" /note=n(BY SIMILARITY)." Site 171 /gene="SFTPD" /site_type="hydroxylation" /note="(BY SIMILARITY)." Region 217..248 /gene="S'FTPD" /region_name="Domain" /note="COILED COIL (POTENTIAL)." Region 273..369 /gene="SFTPD." /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(275,367) /gene="SFTPD" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(345,359) /gene="SFTPD" /bond_type="disuifide" /note="BY SIMILARITY." ORIGIN 1 mlllplsvll lltqpwrslg aemk.iysqkt manactlvmc sppedglpgr dgrdgregpr 61 gekgdpgspg pagragmpgp agpiglkgdn gsagepgpkg dtgppgppgm pgpagregps 121 gkqgsmgppg tpgpkgdtgp kggvgapgiq gspgpaglkg ergapgepga pgragapgpa 181 gafgpqgpsg argppglkgd rgtpgergak gesglaevna Irqrvgileg qlqrlqnafs 241 qykkamlfpn grsvgekifktvgsektfqd aqqictqagg qlpsprsgaenealtqlata 301 qnkaaflsms dtrkegtfiy ptgeplvysn wapqepnndg gsencveifp ngkwndkvcg 361 eqrlvicef SEQIDNO: 104 P42916 COLLECTIN-43 (CL-43) gi|'1168967|sp|P42916|CL43_BOVIN[1168967] FEATURES Location/Qualifiers source 1..301 /organism="Bos taurus" /db_xref="taxon:9913" Protein 1..301 /product="COLLECTIN-43" Region 29..142 /region_name=*,Domain" /note="COLLAGEN4JKE (G-X-Y)." Region 202..301 /region_name="Domain" /note="OTYPE LECTIN (SHORT FORM)." Bond bond(204,299) /bondJype="disulfide" /note="BY SIMILARITY." Bond bond(277,291) /bond_type=ndisuifide" /note="BY SIMILARITY." ORIGIN 1 eemdvysekt Itdpctlvvc appadslrgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdr gdpgekgarg etsvlevdtl rqrmmlege vqrlqnivtq yrkavlfpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepgnrak degpenclei ysdgnwndie creerlvice 301 f SEQIDNO: 105 CAB56155 DMBT1/8kb.2 protein [Homo sapiens] ' gi|5912464|emb|CAB56155.11[5912464] sig_peptide 1..26 mat^peptide 26..2412 /product="DMBT1/8kb.2 protein" CDS 1..2412/gene="DMBTr7coded_by="AJ243212.1:107..7345n /note="Sequence is an alternative splice form of the DMBT1 gene that is expressed in human adult trachea. Isoforms of DMBT1 are identical to the collectin binding protein gp-340. Fuli-length cDNA clone contains 1 bp deletions in codons 100 and 1751, that were corrected by comparison with the genomic exons" ORIGIN 1 mgistvilem cllwgqvlst ggwiprttdy aslipsevpl dttvaegspf pseltlestv 61 aegspisles tlettvaegs lipsestles tvaegsdsgl alrlvngdgr cqgrveilyr 121 gswgavcdds wdtndanvvc rqlgcgwams apgnawfgqg sgpialddvr csghesylws 181 cphngwlshn cghgedagvi csaaqpqstl rpeswpvris ppvptegses slalrlvngg 241 drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd 301 vrcsghesyl wscphngwlt hncghsedag vicsapqsrp tpspdtwpts hastagpess 361 lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanw crqlgcgwat sapgnarfgq 421 gsgpividdv rcsgyesylw scphngwlsh ncqhsedagv icsaahswst pspdtlptit 481 lpastvgses slalrlvngg drcqgrvevl yrgswgtvcd dswdtndanv vcrqlgcgwa 541 mlapgnarfg qgsgpivldd vrcsgnesyl wscphngwls hncghsedag vicsgpessl 601 alrlvnggdr cqgrvevlyr gswgtvcdds wdtndanvvc rqlgcgwams apgnarfgqg 661 sgpivlddvr csghesylws cpnngwlshn cghhedagvi csaaqsrstp rpdtfstitl 721 ppstvgsess Itlrlvngsd rcqgrvevly rgswgtvcdd swdtndanw crqlgcgwat 781 sapgnarfgq gsgpividdv rcsghesylw scphngwlsh ncghhedagv icsvsqsrpt 841 pspdtwptsh astagpessl alrlvnggdr cqgrvevlyr gswgtvcdds wdtsdanwc 901 rqlgcgwats apgnarfgqg sgpivlddvr csgyesylws cphngwlshn cqhsedagvi 961 csaahswstp spdtlptitl pastvgsess lalrlvnggd rcqgrvevly qgswgtvcdd 1021 swdtndanw crqlgcgwam sapgnarfgq gsgpivldda rcsghesylw scphngwlsh 1081 ncghsedagv icsasqsrpt pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr 1141 gswgtvcddy wdtndanvac rqlgcgwams apgnarfgqg sgpivlddvr csghesylws 1201 cphngwishn cghhedagvi csasqsqptp spdtwptsha stagsessla Irivnggdrc 1261 qgrvevlyrg swgtvcddyw dtndanvvcr qigcgwatsa pgn'arfgqgs gpivlddvrc 1321 sghesylwsc phngwlshnc ghhedagvic sasqsqptps pdtwptshas tagsesslal 1381 rlvnggdrcq grvevlyrgs wgtvcddywd tndanvvcrq Igcgwatsap gnarfgqgsg 1441. pivlddvrcs ghesylwscp hngwlshncg hhedagvics afqsqptpsp dtwptsrast 1501 agsestlalr Ivnggdrcrg rvevlyqgsw gtvcddywdt ndanwcrql gcgwamsapg 1561 naqfgqgsgp ivlddvrcsg hepylwscph ngwishncgh hedagvicsa aqsqstprpd . 1621 twittnlpal tvgsesslal rivnggdrcr grvevlyrgs wgtvcddswd tndanvvcrq 1681 Igcgwamsap gnarfgqgsg pivigdvrcs gnesylwscp hkgwlthncg hhedagvics 1741 atqinstttd wwhpttttta rpssncggfl fyasgtfssp sypayypnna kcvweievns 1801 gyrinlgfsn Ikleahhncs fdyveifdgs Insslllgki cndtrqifts synrmtihfr 1861 sdisfqntgf lawynsfpsd atlrlvnlns syglcagrve iyhggtwgav cddswtiqea ,1921 ewcrqlgcg ravsalgnay fgsgsgpitl ddvecsgtes tlwqcrnrgw fshncnhred 1981 agvicsgnhl stpapfinit rpnnyscggf Isqpsgdfss pfypgnypnn akcvwdievq 2041 nnyrvtvifr dvqleggcny dyievfdgpy rsspliarvc dgargsftss snfmsirfis 2101 dhsitrrgfr aeyysspsnd stnllclpnh mqasvsrsyl qslgfsasdi vistwngyye 2161 crpqitpnlv iftipysgcg tfkqadndti dysnlltaav sggiikrrtd Irihvscrml 2221 qntwvdtmyi andtihvann tiqveevqyg nfdvnisfyt sssflypvts rpyyvdlnqd 2281 lyvqaeilhs davltlfvdt cvaspysndf tsltydlirs gcvrddtygp ysspslriar 2341 frfrafhfln rfpsvylrck mwcraydps srcyrgcvlr skrdvgsyqe kvdwlgpiq 2401 Iqtpprreee pr SEQIDNO:106 AAD49696 gp-340 variant protein [Homo sapiens] gi|5733598|gb|AAD49696.1|AF159456_1[5733598] ' FEATURES Location/Qualifiers source 1..2413 /organism="Homo sapiens" /db_xref="taxon:9606" /chramosome=n10w /map="10q25.3-26.1" Protein 1 ..2413 /product="gp-340 variant protein" /name=nscavenger receptor cysteine-rich protein SRCR" /note="putative receptor for SP-D" CDS1..2413/gene="DMBT1n/coded-by="AF159456.1:107..7348M ORIGIN 1 mgistvilem cllwgqvlst ggwiprttdy aslipsevpl dqtvaegspf psestlesta 61 aegspisles tlestvaegs lipsestles tvaegsdsgl alrlvngdgr cqgrveilyr 121 gswgtvcdds wdtndanwc rqlgcgwams apgnawfgqg sgpialddvr csghesylws 181 cphngwishn cghgedagvi csaaqpqstl rpeswpvris ppvptegses slalrlvngg 241 drcrgrvevl yrgswgtvcd dywdtndanv vcrqlgcgwa msapgnaqfg qgsgpivldd 301 vrcsghesyi wscphngwlt hncghsedag vicsapqsrp tpspdtwpts hastagpess 361 lalrlvnggd rcqgrvevly rgswgtvcdd swdtsdanvv crqlgcgwat sapgnarfgq 421 gsgpivlddv rcsgyesylw scphngwish ncqhsedagv icsaahswst pspdtlptit 481 Ipastvgses slalrlvngg drcqgrvev! yrgswgtvcd dswdtndanv vcrqlgcgwa 541 mlapgnarfg qgsgpivldd vrcsgnesyl wscphngwis hncghsedag vicsgpessl 601 alrlvnggdr cqgrvevlyr gswgtvcdds wdtndanwc rqlgcgwams apgnarfgqg 661 sgpivlddvr csghesylws cpnngwfshn cghhedagvi csaaqsrstp rpdtlstitl 721 ppstvgsess Itlrlvngsd rcqgrvevly rgswgtvcdd swdtndanw crqlgcgwam 781 sapgnarfgq gsgpivlddv rcsghesylw scphngwish ncghhedagv icsvsqsrpt 841 pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr gswgtvcdds wdtsdanwc 901 rqlgcgwats apgnarfgqg sgpivlddvr csgyesylws cphngwishn cqhsedagvi 961 csaahswstp spdtlptitl pastvgsess lalrlvnggd rcqgrvevly qgswgtvcdd 1021 swdtndanw crqpgcgwam sapgnarfgq gsgpivlddv rcsghesypw scphngwish' 1081 ncghsedagv. icsasqsrpt pspdtwptsh astagsessl alrlvnggdr cqgrvevlyr 1141 gswgtvcddy wdtndanwc rqlgcgwams apgnarfgqg sgpivlddvr csghesylws 1201 cphngwishn cghhedagvi csasqsqptp spdtwptsha stagsessla Irivnggdrc 1261 qgrvevlyrg swgtvcddyw dtndanwcr qlgcgwatsa pgnarfgqgs gpivlddvrc 1321 sghesylwsc phngwlshnc ghhedagvic sasqsqptps pdtwptshas tagsesslal 1381 rlvnggdrcq grvevlyrgs wgtvcddywd tndanvvcrq Igcgwatsap gnarfgqgsg 1441 pivlddvrcs ghesylwscp hngwlshncg hhedagvics asqsqptpsp dtwptsrast 1501 agsestlalr Ivnggdrcrg rvevlyqgsw gtvcddywdt ndanvvcrql gcgwamsapg 1561 naqfgqgsgp ivlddvrcsg hesylwscph ngwlshncgh hedagvicsa aqsqstprpd 1621 twlttnlpal tvgsesslal rlvnggdrcr grvevlyrgs wgtvcddswd tndanvvcrq 1681 Igcgwamsap gnarfgqgsg pivlddvrcs gnesylwscp hkgwlthhcg hhedagvics 1741 atqinstttd wwhpttttta rpssncggfl fyasgtfssp sypayypnna kcvweievns 1801 gyrinlgfsn lkleahhncs fdyveifdgs Insslllgki cndtrqifts synrmtihfr 1861 sdisfqntgf iawynsfpsd atlrlvnins syglcagrve iyhggtwgtv cddswtlqea 1921 evvcrqlgcg ravsalgnay fgsgsgpitl ddvecsgtes tlwqcrnrgw fshncnhred 1981 agvicsgnhl stpapfinit rpntdyscggfisqpsgdfs spfypgnypn nakcvwdiev 2041 qnnyrvtvif rdvqleggcn ydyievfdgp yrsspliarv cdgargsfts ssnfmsirfi 2101 sdhsitrrgf raeyysspsn dstnllclpn hmqasvsrsy Iqslgfsasd Ivistwngyy 2161 ecrpqitpnl viftipysgc gtfkqadndt idysnfltaa vsggiikrrt dlrihvscrm 2221 Iqntvwdtmy iandtihvan ntiqveevqy gnfdvnisfy tsssflypvt srpyyvdlnq 2281 dlyvqaeilh sdavltlfvd tcvaspysnd ftsltydlir sgcvrddtyg pysspslria 2341 rfrfrafhfl nrfpsvylrc kmwcraydp ssrcyrgcvl rskrdvgsyq ekvdvvlgpi 2401 qlqtpprree epr SEQIDNO:107 AAD31380 surfactant protein D precursor [Mus muscuius] gi|4877556|gb]AAD31380.1|AF047742J[4877556] sig_peptide 1..19 mat peptide 20..374 /product="surfactant protein D" CDS1..374/gene="Sftp4" /coded_by=^in(AF047741.1:5705..5900,AF047742.1:312..428, AF047742.1:669..785AF047742.1:1112..1228, AF047742.1:1977..2093,AF047742.1;3162..3245, AF047742.1:5010..5386)H ORIGIN 1 mlpflsmlvl Ivqplgnlga emkslsqrsv pntctlvmcs ptenglpgrd grdgregprg 61 ekgdpglpgp mglsglqgpt gpvgpkgeng sagepgpkge rglsgppglp gipgpagkeg 121 psgkqgnigp qgkpgpkgea gpkgevgapg mqgstgakgs tgpkgergap gvqgapgnag 181 aagpagpagp qgapgsrgpp glkgdrgvpgdrgikgesgi pdsaalrqqm ealkgklqrl 241 evafshyqka alfpdgrsvg dkifrtadse kpfedaqemc kqaggqlasp rsatenaaiq 301 qiitahnkaa flsmtdvgte gkftyptgep Ivysnwapge pnnnggaenc veiftngqwn 361 dkacgeqrlv icef SEQIDNO; 108 B61249 pulmonary'surfactant protein C - dog gi|539712|pir||B61249[539712] FEATURES Location/Qualifiers source 1..35 /organism="Canis familiaris" /db_xref=^taxon:9615,, Protein 1..35 /product="pulmonary surfactant protein C" . ORIGIN 1 Igipcfpssl krlliivvvi vlvvvvivga llmgl SEQIDNO: 109 S00609 pulmonary surfactant protein C - bovine gi|89749jpir|JS00609[89749] FEATURES Location/Qualifiers source 1 ..34 /organism="Bos taurus" /dbjcref="taxon:9913" Protein 1..34 /product="pulmonary surfactant protein C" /note="pulmonary surfactant protein PSP-6" Site 4 /site_type="binding" /note="palmitate (Cys) (covalent)" Site 5 /site_type="binding" /note="palmitate (Cys) (covalent)" ORIGIN 1 lipccpvnik rlliwvwv llwvivgal Imgl .SEQIDNO:110 A43628 pulmonary surfactant protein A - human (fragments) gi|280854|pir||A43628[280854] FEATURES Location/Qualifiers source 1.35 /organism="Homo sapiens" /db_xref=ntaxon:9606w Protein 1.35 /product="pulmonary surfactant protein A" ORIGIN 1 gqsitfdagk eqcvemytdg qwndrnciyl ticef SEQIDNO:111 AAB48076 Surfactant protein B (SP-B) [Oryctolagus cuniculus] gi|1850933|gb|AAB48076.11[1850933] FEATURES Location/Qualifiers source 1.370 /organism-'Oryctoiagus cuniculus" /db_xref=Mtaxon:9986,,/tissueJype="Iiver,, Protein 1.370 /product="Surfactant protein B (SP-B)" CDS 1.370/gene="SP-B" /coded_by="join(U40853.1:2194..2263, U40853.1:2591.2718, U40853.1:2941.3012,U40853.1:3257..3382, U40853.1:3590..3727,U40853.1:3925..4014, U40853.1:6043..6226,U40853.1:6421.6581 U40853.1:7266..7346,U40853.1:7829..7891)" /note="Surfactant protein B (SP-B) is a key component of lung surfactant, a surface active material secreted by type II epithelial cells of lung alveolus; SP-B maintains biophysical properties and physiological function of surfactant; Pulmonary surfactant associated protein" ORIGIN 1 makshlppwl Illllptlcg pgtavwatsp lacaqgpefw cqsleqalqc kalghclqev 61 wghvgaddlc qecqdivnil tkmtkeaifq dtirkflehe cdvlplkllv pqchhvidvy 121 fpltityfls qinakaicqh Iglcqpgspe ppldplpdkl viptllgalp akpgphtqdl 181 saqrfpiplp lcwlcrtllk riqamipkgv lamavaqvch vvplvvggic qclaerytvi 241 llevllghvl pqlvcglvlr cssvdsigqv pptlealpge wlpqdpecpl cmsvttqarn 301 iseqtrpqav yhaclssqld kqeceqfvel htpqllslls rgwdaraicq algacvatls 361 plqciqsphf . SEQIDNO:112 1901176A surfactant protein A gi|382753|prf||1901176A[382753] FEATURES Location/Quaiffiers source 1.247 /organism="Oryctolagus cuniculus" /db_xref="taxon:9986" ORIGIN 1 mlllslaltl isapasdtcd tkdvcigspg ipgtpgshgl pgrdgrdgvk gdpgppgpmg 61 ppggmpglpgrdgiigapgv pgergdkgep gergppglpa yldeeiqatl helrhhalqs 121 igvlslqgsm kavgekifst ngqsvnfdai revcaraggr iaivkevprs leeneaiasr 181 ntyaylglae gptagdfyyi dgdpvnytnw ypgeprgqgr ekcvemytdg kwndknclqy 241 rlvicef SEQIDNO:113 CAA53510 lung surfactant protein D [Bos taurus] gi|415939[emb|CAA53510.1|[415939] sig_peptide 1.20 mat_peptide 21 ..369 /product="lung surfactant protein D" CDS 1 ..369 /coded_by="X75911.1:102-1211" /db__xref="SWISS«PROT:P35246" . ORIGIN 1 mlllplsvll Htqpwrslg aemkiysqkt manactlvmc sppedglpgr dgrdgregpr 61 gekgdpgspg pagragmpgp agpiglkgdn gsagepgpkg dtgppgppgm pgpagregps 121 gkqgsmgppg tpgpkgdtgp kggvgapgiq gspgpaglkg ergapgepga pgragapgpa 181 gaigpqgpsg argppglkgd rgtpgergak gesglaevna Irqrvgileg qlqrlqnafs 241 qykkaralfpn grsvgekifk tvgsektfqd aqqictqagg qlpsprsgae nealtqlata 301 qnkaaflsms dtrkegtfiy ptgeplvysn wapqepnndg gsencveifp ngkwndkvcg 361 eqrlvicef SEQIDNO:114 CAA53511 collectin-43 [Bos taurus] gi|499385|emb|CAA53511.1|[499385] FEATURES Location/Qualifiers source 1.301 /organism="Bos taurus" /db_xref="taxon:9913" /tissue_type="liver" /clone_lib="lambda gt 11" Protein 1.301 /product="collectin-43" mat_peptide 1.301 /product="collectin-43" CDS 1.301 /coded_by=MX75912.1: ORIGIN 1 eemdvyxekt Itdpctlwc appadslrgh dgrdgkegpq gekgdpgppg mpgpagregp 61 sgrqgsmgpp gtpgpkgepg peggvgapgm pgspgpaglk gergapgpgg aigpqgpsga 121 mgppglkgdr gdpgekgarg etsvlevdtl rqrmrnlege vqrlqnivtq yrkavlfpdg 181 qavgekifkt agavksysda eqlcreakgq lasprssaen eavtqlvrak nkhaylsmnd 241 iskegkftyp tggsldysnw apgepgnrak degpenclei ysdgnwndie creerlvice 301 f SEQIDNO:115 CAA46152 lung surfactant protein D [Homo sapiens] gi|34767|emb|CAA46152.11[34767] sig_peptide 1 ..20 mat_peptide 21.375 /product="lung surfactant protein D" CDS 1 ..375 /gene="hsp-D" /coded_by="X65018.1:172..1299" /db_xref="SWISS- PROT:P35247" ORIGIN 1 mllfllsalv lltqplgyle aemktyshrttpsactlvmc ssvesglpgr dgrdgregpr 61 gekgdpglpg aagqagmpgq agpvgpkgdn gsvgepgpkg dtgpsgppgp pgvpgpagre 121 gplgkqgnig pqgkpgpkge agpkgevgap gmqgsagarg lagpkgergv pgergvpgna . 181 gaagsagamg pqgspgargp pglkgdkgip gdkgakgesg Ipdvaslrqq vealqgqvqh 241 Iqaafsqykk velfpngqsv gekifktagf vkpfteaqll ctqaggqlas prsaaenaal 301 qqiwaknea afismtdskt egkftyptge sivysnwapg epnddggsed cveiftngkw 361 ndracgekrl wcef SEQIDNO:116 AAA92788 lung surfactant protein C [Rattus norvegicus] gi|595282|gb|AAA92788.1|[595282] FEATURES Location/Qualifiers source 1.194 /organism-'Rattus norvegicus" /db_xref="taxon:-10116" /clone="sp-cn /tissue_type="liver" Protein 1.194 /product=nIung surfactant protein C" CDSL.194/gene="sp-c" /coded_by="join(U07796.1:1673.-1714, U07796.1:2841.2999, U07796.1:3252..3377, U07796.1:3598..3707/U07796.14053..4200)" ORIGIN 1 mdmgskevim esppdystgp rsqfripccp vhlkrllivv wvvlvwvi vgallmglhm 61 sqkhtemvle msiggapetq krlaisehtd tiatfsigst givlydyqri Itaykpapgt 121 ycyimkmape sipsiealar kfknfqakss tptsklgqee ghsagsdsds sgrdlaflgl 181 avstlcgvlp lyyi SEQ ID NO: 117 AAA31468 surfactant protein A [Oryctolagus cuniculus] gi|431446|gb|AAA31468.11[431446] FEATURES Location/Qualifiers source 1..247 /organism="Oryctolagus cuniculus" /strain-'NewZealand White" /db xref="taxon:9986" /tissue_type="liver" /dev_stage=nadult" Protein 1..247 /product="surfactant protein A" CDS 1 ..247 /coded_by="join(L19387.1:3864..4032,L19387.1:4241 ..4360, L19387.i:5010..5087,L19387.1:5533..5909)rt ORIGIN 1 mlllslaltl isapasdtcd tkdvcigspg ipgtpgshgl pgrdgrdgvk gdpgppapwa 61 ppggmpglpg rdgligapgv pgergdkgep gergppglpa yldeelqatl helrhhalqs 121 igvlslqgsm kavgekifst ngqsvnfdai revcaragg'r iavprsleen eaiasivker 181 ntyaylglae gptagdfyyl dgdpvnytnw ypgeprgqgr ekcvemytdg kwndknclqy 241 rlvicef Mannose binding lectin SEQ ID NO: 1 NP_034897 mannan-binding lectin serine protease 2 [Mus musculus] gi|6754642|ref|NPJ)34897.1|[6754642] sig_peptide 1..15 mat_peptide 16..185/product="mannan-binding lectin serine protease 2" Region 28..137 /region_name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein" /note="CUB" /db_xref="CDD:smart00042" Region 28..134 /region_name=nCUB domain" /note=MCUB" /db_xref=MCDD:pfam0043r Region 138..180/region_name="Calcium-binding EGF-Iike domain" /note="EGF_CAM /db_xref=BCDD:smart00179" variation 172 /a!lele=T /ailele=,rV" /db_xref="dbSNP:3167338" CDS 1 ..185 /gene="Masp2" /coded_by="NM_010767.1:32..589" /db_xref="LocuslD:17175M/db_xref="MGD:1330832" ORIGIN 1 mrlliflgll wslvatllgs kwpepvfgrl vspgfpekya dhqdrswtlt appgyrlrly 61 fthfdlelsy rceydfvkls sgtkvlatlc gqestdteqa pgndtfyslg pslkvtfhsd 121 ysnekpftgf eafyaaedyd ecrvslgdsv pcdhychnyl ggyycscrag yvlhqnkhtc 181 seqsl SEQ ID NO: 2 AAH10760 Similar to mannose binding lectin, serum (C) [Mus musculus] gi|14789670|gb)AAH10760.1|[14789670] source 1 ..244 /organism="Mus musculus" /strain="FVB/Nw /db_xref="taxon:10090" /clone=nMGC: 18500 IMAGE:4212216" Aissue type="Liver, normal. 5 month old male mouse." /cloneJib="NCLCGAPJJ9H /labJiost^DHlOB" /note='Vector: pCMV-SPORTS" Protein 1 ..244 /product="Similar to mannose binding lectin, serum (C)" CDS 1..244 /coded_by="BC010760.1:192..926" ORIGIN 1 msiftsflll cwtwyaet Itegvqnscp wtcsspgin gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa Irselralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat prnaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcw ilgngkwndv pcsdsflaic 241 efsd SEQ ID NO: 3 AAH21762 mannose binding lectin, liver (A) [Mus musculus] gi|18256010|gb|AAH21762.1|[18256010] source 1..239 /organism="Mus musculus" /strain="FVB/N" /db_xref="taxon: 10090" /clone="MGC:30242 IMAGE:5132514" /tissue_type="Liver, normal. 5 month old male mouse." /cloneJib^'NCLCGAPJjg*' /lab_host="DH10B"/note="Vecton pCMV-SPORT6" Protein-1..239 /product="mannose binding lectin, liver (A)" /db xref="Locus[D:17194" CD~S 1..239/coded_by="BC021762.1:75..794"/db_xref=MLocuslD:17194" ORIGIN 1 mlllpllpvl Icvvsvsssg sqtcedtlkt csviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeirilkskl qltnklhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaiprnae enkaiqevat giaflgitde 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQ ID NO: 4 Q9NPY3 Complement component C1 q receptor precursor (Complement component 1, q subcomponent, receptor 1) (C1qRp) (C1qR(p)) (C1q/MBL/SPA receptor) (CD93 antigen) (CDw93) gi|21759074|sp|Q9NPY3|CD93_HUMAN[21759074] source 1..652 /organism="Homo sapiens" /db_xref="taxon:9606 gene 1..652 /gene="C1QR1" /note="CD93" Protein 1..652 /gene="C1QR1" /product="Complement component C1q receptor precursor" Region 1..21 /gene="C1QR1"/region_name="Signal" Region 22..652 /gene="C1QR1" /region_name="Mature chain" /note="COMPLEMENT COMPONENT C1Q RECEPTOR. Region 22 /gene="C1QR1" /region_name="Conflict" /note="T-> V (IN AA SEQUENCE)." Region 24..580 /gene="C1QR1" /region name="Domain" /note="EXTRACELLULAF (POTENTIAL)." Region 32.. 174 /gene="C1QR1" /region_name="Domain" /note="C-TYPE LECTIN." Region 36 /gene="C1QR1" /region_name="Conflict" /note="C -> T (IN AA SEQUENCE)." Region 38..39 /gene="C1QR1M /region_name="Conflicr /note="TA -> Rl (IN AA SEQUENCE)." Region 155 /gene="C1QR1" /region_name="Conflict" /note=*'S -> N (IN REF. 1)." Region 186 /gene="C1QR1" /region_name="Conflict" /note="G -> A (IN AA SEQUENCE)." Region 260..301 /gene="C1QR1" /regionjiame^Domain" /note="EGF-LIKE 1." Bond bond(264,275) /gene="C1QR1" /bond_type="disulfide" /note="BY ' SIMILARITY." Bond bond(271,285) /gene="ClQR1" /bond_type="disulfide" /note="BY SIMILARITY." tond bond(287,300) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 302..344 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 2." 3ond bond(306,317) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(311,328) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 318 /gene="C1QR1" /region_name="Variant" /note="V -> A. fFTId=VAR_013573." Site 325 /gene="C1QR1" /site_type="glycosylation" /note="N-LlNKED (GLCNAC.) (POTENTIAL)." Bond bond(330,343) /gene="C1QR1n /bond_type="disulfide" /note="BY SIMILARITY." Region 345..384 /gene="C1QR1" /region name="Domain" /note="EGF-LIKE 3, CALCIUM-BINDING (POTENTIAL)." Borid bond(349,358) /gene="C1QR1H /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(354,367) /gene="C1QR1" /bond_type="disulfide"/note="BY SIMILARITY." Bond.bond(369,383) /gene="C1QR1" /bond_type=,,disulfide" /note="BY SIMILARITY." Region 385..426 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 4, CALCIUM-BINDING (POTENTIAL)." Bond bond(389,400) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(396,409) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(411,425) /gene="C1 QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 427..468 /gene="C1QR1n /region name=nDomain" /note="EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL)." Bond bond(431,443) /gene="C1QR1" /bond type="disulfide"/note="BY SIMILARITY." Bond bond(439,452) /gene="C1QR1" /bond type="disulfide" /note="BY SIMILARITY." Bond bond(454,467) /gene="C1QR1" /bondjype^'disulfide' /note="BY SIMILARITY." Region 492 /gene="C1QR1" /region_name=nConflict" /note="S -> A (IN AA SEQUENCE)." Region 496 /gene="C1QR1" /region name="Conflictn /note="R -> Q (IN AA SEQUENCE)." Region 504 /gene="C1QR1" /region_name="Conflict" /note="R -> G (IN AA SEQUENCE)." Region 541 /gene="C1QR1"/region_name=nConflict" /note="P -> S (IN REF. 1)." Region 581..601 /gene="C1QR1" /region_name-Transmembrane region" /note="POTENTIAL." Region 594..601 /gene="C1QR1"/region_name=,,Domain" /note="POLY-LEU." Region 602..652 /gene="C1QRr/region_name="Domain" /note="CYTOPLASMIC (POTENTIAL)." ORIGIN 1 matsmgllll llllltqpga gtgadteaw cvgtacytah sgklsaaeaq nhcnqnggnl 61 atvkskeeaq hvqrvlaqll rreaaltarm skfwiglqre'kgkcldpslp Ikgfswvggg 121 edtpysnwhk elrnsciskr cvsllldlsq pllpsrlpkw segpcgspgs pgsniegfvc 181 kfsfkgmcrp lalggpgqvt yttpfqttss sleavpfasa anvacgegdk detqshyflc' 241 kekapdvfdw gssgplcvsp kygcnfnngg chqdcfeggd gsflcgcrpg frllddlvtc 301 asrnpcsssp crggatcvlg phgknytcrc pqgyqidssq Idcvdvdecq dspcaqecvn 361 tpggfrcecw vgyepggpge gacqdvdeca Igrspcaqgc tntdgsfhcs ceegyvlage 421 dgtqcqdvde cvgpggplcd slcfntqgsf hcgclpgwvl apngvsctmg pvslgppsgp 481 pdeedkgeke gstvpraata sptrgpegtp katpttsrps Issdapitsa plkmlapsgs 541 pgvwrepsih hataasgpqe paggdssvat qnndgtdgqk lllfyilgtv vaiilllala 601 Igllvyrkrr akreekkekk pqnaadsysw vperaesram enqysptpgt dc SEQIDNO:5 089103 Complement component C1q receptor precursor (Complement component 1, q subcomponent, receptor 1) (ClqRp) (C1qR(p)) (C1q/MBL/SPA receptor) (CD93 antigen) (Cell surface antigen AA4) (Lymphocyte antigen 68) gi|21541998|sp|O89103|CD93_MOUSE[21541998 source 1..644 /organism="Mus musculus" /db_xref="taxon: 10090" gene 1..644/gene="C1QR1n/note="CD93; C1QRP; LY68; AA4" Protein 1..644 /gene="C1QR1" /product="Complement component C1q receptor precursor" Region 1..22 /gene="C1QR1" /region_name="Signal" /note="POTENTIAL." Region 23..644 /gene="C1QR1" /region_name="Mature chain" /note="COMPLEMENT COMPONENT C1Q RECEPTOR." Region 23..572 /gene="C1QR1" /region_name="Domain" /note="EXTRACELLULAR (POTENTIAL)." Region 31.173 /gene="C1QR1" /region_name=nDomainn /note="C-TYPE LECTIN." Site 102 /gene=MC1QR1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Region 257..298 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 1." Bond bond(261,272) /gene="C1QR1" /bond_type="disulfideM /note="BY SIMILARITY." Bond bond(268,282) /gene="C1QR1n /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(284,297) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 299..341 /gene=nC1QR1"/regionjname="Domain"7note=nEGF-LIKE 2." Bond bond(303,314) /gene="C1QR1"/bond_type=,,disulfide"./note="BY SIMILARITY." Bond bond(308,325) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Site 322 /gene="C1QR1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Bond bond(327,340) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 342..381 /gene="C1QR1B /region_name="Domain" /note="EGF-LIKE 3, CALCIUM-BINDING (POTENTIAL)." Bond bond(346,355) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(351,364) /gene="C1 QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(366,380) /gene=nC1QR1" /bond_type="disulfide" /note="BY SIMILARITY." . Region 382..423 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 4, CALCIUM-BINDING (POTENTIAL)." Bond bond(386,397) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(393,406) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(408,422) /gene=nC1QR1"/bond_type="disulfide" /note="BY SIMILARITY." Region 424..465 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 5, CALCIUM-BINDING (POTENTIAL)." ' Bond bond(428,440) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(436,449) /gene="C1 QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(451,464) /gene="C1QR1" /bond_type=" disulfide" /note="BY SIMILARITY." Region 573..593 /gene="C1QR1" /region_name="Transmembrane region" /note="POTENTIAL." Region 594..644 /gene="C1QR1" /region_name="Domain" /note="CYTOPLASMIC (POTENTIAL)." ORIGIN 1 maistglfll lgllgqpwag.aaadsqavvcegtacytahwgklsaaeaqh rcnenggnla 61 tvkseeearh vqqaltqllk tkapleakmg kfwiglqrek gnctyhdipm rgfswvggge 121 dtaysnwyka sksscifkrc vslildlslt phpshlpkwh espcgtpeap gnsiegflck 181 fnfkgmcrpl alggpgrvty ttpfqattss leavpfasva nvacgdeaks ethyflcnek 241 tpgifhwgss gplcvspkfg csfnnggcqq dcfeggdgsf rcgcrpgfrl Iddlvtcasr 301 npcssnpctg ggmchsvpls enytcrcpsg yqldssqvhc vdidecqdsp caqdcvntlg 361 sfhcecwvgy qpsgpkeeac edvdecaaan spcaqgcint dgsfycscke gyivsgedst 421 qcedidecsd argnpcdslc fntdgsfrcg cppgwelapn gvfcsrgtvf selparppqk 481 ednddrkest mpptempssp sgskdvsnra qttglfvqsd iptasvplei eipsevsdvw 541 felgtylptt sghskpthed svsahsdtdg qnlllfyilg twaislllv lalgiliyhk 601 rrakkeeike kkpqnaadsy swvperaesq apenqysptp gtdc SEQ ID NO: 6 P09871 Complement C1s component precursor (C1 esterase) gi| 115205|sp|P09871 |C1 S_HUMAN[115205] source 1. .688 /organism="Homo sapiens" /db_xref="taxon:9606" gene 1.688 /gene="C1S" Protein 1.688 /gene="C1S" /product="Complement C1s component precursor" /EC_number="3.4.21.42" Region 1.15 /gene="C1S" /r'egion_name="Signal" Region 16..437 /gene="C1S" /region_name="Mature chain" /note="COMPLEMENT ' C1S HEAVY CHAIN." Region 16..130 /gene="C1S"/region_name="Domain" /note="CUB 1." Bond bond(65,83) /gene="C1S" /bond_type="disulfide" Region 131.172 /gene="C1S" /region_name="Domain" /note="EGF-LIKE, CALCIUM-BINDING (POTENTIAL)." Bond bond(135,147) /gene="C1S"/bondjype-'disulfide" Bond bond(143,156) /gene="C1S" /bond_type="disulfide" Site 149/gene="C1Sn /site_type="hydroxylation" /note="(PROBABLE)." Bond bond(158,171) /gene="C1S"/bond_type="disulfide" Site 174 /gerie="C1S" /site_type="glycosylation" /note="N-LINKED (GLCNAC...)." Region 175..290 /gene="C1S" /region_name="Domain" /note="CUB 2." Bond bond(175,202)/gene="C1S"/bond_type="disulfide" Bond bpnd(234,251) /gene="C1S" /bond_type="disulfide" Region 293..355 /gene="C1S" /region_name="Domain" /note="SUSHI 1." Bond bond(294,341) /gene="C1S" /bond_type="disulfide" Region 294 /gene="C1S" /region_name="Conflict" /note="C -> K (IN REF. 6)." Bond bond(321,354) /gene="C1S" /bondjype^'disulfide" Region 358..422 /gene=rtC1S,,7region_name=,,Domain" /note=BSUSHI 2."-Bond bond(359,403) /gene="C1S" /bond_type="disulfide" Bond bond(386,421) /gene="C1SM /bondJype="disu!fide" Site 406 /gene="C1S" /siteJype="glycosylationn /note="N-LINKED (GLCNAC...)." Bond bond(425,549) /gene="C1S" /bondJype="disulfide" /note="INTERCHAIN." Region 438..688 /gene="C1SH /region_name="Mature chain" /note="COMPLEMENT . C1S LIGHT CHAIN." Region 438..688 /gene="C1 S" /region ^name^'Domain" /note="SERINE PROTEASE." Site 475 /gene="C1S" /sitejype="active" /note="CHARGE RELAY SYSTEM." Region 513 /gene="C1S" /region_name=nConfIicf /note="G -> GG (IN REF. 5)." Site 529 /gene="C1S" /site_type="active" /note="CHARGE RELAY SYSTEM." Region 573 /gene="C1S" /region_name=nConflicf /note="T--> A (IN REF. 7)." Bond bond(595,618) /gene="C1S" /bond_type=ndisulfide" Bond bond(628,659) /gene="C1 Sn /bondJypep'disulfide" Site 632 /gene="C1 S" /sitejype="active" /note=HCHARGE RELAY SYSTEM." Region 645..646 /gene="C1S" /region_name="Conflict" /note="TK -> GR (IN REF. 7)." ' ORIGIN 1 mwcivlfsll awvyaeptmy geilspnypq aypseveksw dievpegygi hlyfthldie 61 Isencaydsv qiisgdteeg ricgqrssnn phspiveefq vpynklqvif ksdfsneerf 121 tgfaayyvat dinectdfvd vpcshfcnnf iggyfcscpp eyflhddmkn cgvncsgdvf 181 taligeiasp nypkpypens rceyqirlek gfqwvtlrr edfdveaads agncldslvf 241 vagdrqfgpy cghgfpgpln ietksnaldi ifqtdltgqk kgwklryhgd pmpcpkedtp 301 nsvwepakak yvfrdwqit cldgfevveg rvgatsfyst cqsngkwsns klkcqpvdcg 361 ipesiengkv edpestlfgs virytceepy yymengggge yhcagngswv nevlgpelpk 421 cvpvcgvpre pfeekqriig gsdadiknfp wqvffdnpwa ggalineywv Itaahwegn 481 reptmyvgst svqtsrlaks kmltpehvfi hpgwkllevp egrtnfdndi alvrlkdpvk 541 mgptvspicl pgtssdynim dgdlglisgwgrtekrdrav rlkaarlpva plrkckevkv 601 ekptadaeay vftpnrnicag gekgmdsckg dsggafavqd pndktkfyaa glvswgpqcg 661 tyglytrvkn yvdwimktmq enstpred SEQ ID NO: 7 NP_036204 complement component 1, q subcomponent, receptor 1; complement component C1q receptor [Homo sapiens] gi|6912282|ref|NP_036204.11[6912282] source 1..652 /organism-"Homo sapiens" /db_xref="taxon:9606" /chromosome="20" /map="20p11.21M * Protein 1..652 /product="complement component 1, q subcomponent, receptor 1" /note="complement component C1q receptor" Region 32..130 /region_name=nsmart00034, CLECT, C-type lectin .(CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules" Region 47.. 128 /region-name="pfam00059) lectin_c, Lectin C-type domain. This family includes both long and short form C-type" Region 385..426 /region_name=,,smart00179, EGF_CA, Calcium-binding EGF-like domain" CDS 1..652 /gene="ClQR1" /coded_by="NM_012072.2:149..2107" /note="Clq/MBL/SPA receptor" /db_xref="LocusiD:22918" /db_xref="MIM: 120577" ORIGIN 1 matsmgllll llllltqpga gtgadteaw cvgtacytah sgklsaaeaq nhcnqnggnl 61 atvkskeeaq hvqrvlaqll rreaaltarm skfwiglqre kgkcldpslp Ikgfswvggg 121 edtpysnwhk elrnsciskr cvsllldlsq Dllonrlpkw seqpcgspgs pgsniegfvc 181 kfsfkgmcrp lalggpgqvt yttpfqttss sleavpfasa anvacgegdk detqshyflc 241 kekapdvfdw gssgplcvsp kygcnfnngg chqdcfeggd gsflcgcrpg frllddlvtc '301 asrnpcsssp crggatcvig phgknytcrc pqgyqldssq Idcvdvdecq dspcaqecvn 361 tpggfrcecw vgyepggpge gacqdvdeca Igrspcaqgc tntdgsfhcs ceegyviage 421 dgiqcqdvde cvgpggplcd sicfntqgsf hcgclpgwvl apngvsctmg pvslgppsgp 481 pdeedkgeke gstvpraata sptrgpegtp katpttsrps Issdapitsa plkmlapsgs 541 sgvwrepsih hataasgpqepaggdssvatqnndgtdgqk lllfyilgtvvaillllala 601 Igllvyrkrr akreekkekk pqnaadsysw vperaesram enqysptpgt dc SEQ ID NO: 8 NP_000233 soluble mannose-binding lectin precursor; mannose-binding lectin; mannose binding protein; Mannose-binding lectin 2, soluble (opsonic defect) [Homo sapiens] gi|4557739|ref|NPJ)00233.1|[4557739] sig_peptide 1..20 mat_peptide 21..248 /product="soluble mannose-binding lectin" variation 54 /ailele="D" /allele="G" /db_xref="dbSNP; 1800450" variation 57 /alleIe=flE" /allele="G" /db_xref="dbSNP:1800451" Region 134..245 /region_name="smart00034I CLECT, C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules" Region 144..246 /region_name="pfarn00059, lectin_c, Lectin C-type domain. This family includes both long and short form C-type" CDS 1 ..248 /gene="MBL2B /coded J>y="NMJ)00242.1:66..812" /db_xref=,,LocuslD;4153n/db„xref=,,MIM:154545,, ORIGIN 1 mslfpslpll Ilsmvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 9 P11226 Mannose-binding protein C precursor (MBP-C) (MBP1) (Mannan-binding protein) (Mannose-binding lectin) gi|126676|sp|P11226|MABC_HUMAN[126676] source 1 ..248 /organism-'Homo sapiens" /db__xref=ntaxon:9606" gene 1..248 /gene="MBL2H /note^'MBL" Protein 1..248 /gene=nMBL2" /product="Mannose-binding protein C precursor" ' Region 1..20 /gene="MBL2" /region_name="Signar Region 21 ..248 /gene="MBL2" /region_name="Mature chain" /note="MANNOSE- BINDING PROTEIN C." Region 21 ..41 /gene="MBL2" /region_name="Domainw /note=nCYS-RICH." Region 24 /gene="MBL2" /region_name="Variant" /note="T -> A (IN CHINESE). /FTld=VAR__013294." Region 42..99 /gene="MBL2M /region_name=,IDomainM /note="COLLAGEN-LIKE.H Site 47 /gene="MBL2" /siteJype="hydroxylation" Region 52 /gene=nMBL2n /region_name="Variant"7note="R -> C (IN 0.05% OF EUROPEAN AND AFRICAN POPULATIONS). /FTId=VAR_008543." Region 54 /gene=nMBL2M /region_name="Variant" /note=MG -> D (IN CAUCASIAN AND CHINESE POPULATIONS). /FTId=VAR_004182." Region 57 /aene="MBL2M /region_name="Variant" /note="G -> E (IN WEST AFRICAN POPULATION). /FTId=VARJ)04183." Site 73 /gene=nMBL2" /siteJype="hydroxyiation" Site 797gene="MBL2" /siteJype="hydroxyiation" Site 82 /gene=nMBL2" /sitejype^'hydroxylation" Site 88 /gene="MBL2" /siteJype=Mhydroxylation" Region 109 /gene="MBL2" /region_name="Hydrogen bonded turn" Region 110..129/gene-'MBLZ/region^name^'Helicar region" Region 130 /gene="MBL2" /region_name=,,Hydrogen bonded turn" Region 132.. 134 /gene="MBL2n /region_name="Beta-strand region" Region 135..136 /gene="MBL2" /region_name="Hydrogen bonded turn" Region 137..147 /gene=nMBL2" /region_name="Beta~strand region" Region 148.. 157 /gene="MBL2" /region_name=nHe!ical region" Region 153..246 /gene="MBL2" /region_name="Domain" /note="C-TYPE LECTIN (SHORT FORM)." Bond bond(155,244) /gene="MBL2" /bondJype="disulfide" Region 158.. 159/gene="MBL2"/region jiame="Hydrogen bonded turn" Region 161.162 /gene="MBL2" /region_name="Beta-strand region" Region 168..177/gene="MBL2"/region_name="Helical region" Region 182.. 187 /gene="MBL2" /region_name="Beta-strand region" Region 192..193 /gene="MBL2" /region_name="Hydrogen banded turn" Region 196,.197 /gene="MBL2" /region_name="Beta-strand region" Region 198.. 199 /gene="MBL2" /region_name="Hydrogen bonded turn" Region 202 /gene="MBL2" /region_name="Beta-strand region" Region 208 /gene="MBL2" /region_name="Beta-strand region" Region 210..211 /gene="MBL2" /region_name="Hydrogen bonded turn" Region 216..218 /gene="MBL2" /region jiame="Helical region" Bond bond(222,236) /gene="MBL2" /bond Jype=ndisulfide" Region 222„225 /gene="MBL2M /region_name="Beta-strand region" Region 227..2287gene="MBL2" /region_name="Hydrogen bonded turn" Region 231..234 /gene="MBL2" /region_name="Beta-strand region" Region 236..237 /gene="MBL2" /region_narne="Hydrogen bonded turn" Region 239..248 /gene="MBL2" /region_name="Beta-strand region" ORIGIN 1 mslfpslpll iismvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQIDNO:10 Q9ET61 Complement component C1q receptor precursor (Complement component 1, q subcomponent, receptor 1) (ClqRp) (C1qR(p)) (C1q/MBL/SPA receptor) (CD93 antigen) (Cell surface antigen AA4) gi|21541989|sp|Q9ET61[CD93J*AT[21541989] source 1...643 /organism="Rattus norvegicus" /db_jcref="taxon:10116" gene 1 ..643 /gene="C1QR1" /note="CD93; C1QRP2" Protein 1..643 /gene="C1QR1" /product=nComp!ement component C1q receptor precursor" Region 1..23 /gene="C1QR1" /region__name="Signal" /note^'POTENTlAL" Region 24..643 /gene="C1QR1M /regionjname="Mature chain" . /note="COMPLEMENT COMPONENT C1Q RECEPTOR." Region 24..571 /gene="C1QR1" /region_name="Domain" /note=nEXTRACELLULAR (POTENTIAL).'" Region 31..173 /gene="C1GR1" /region_name="Domain" /note="C-TYPE LECTIN." Region 257..298 /gene="C1 QR1" /region_name="Domainn /note="EGF-LIKE 1." Bond bond(261,272) /gene="C1QR1" /bond type="disulfide" /note="BY SIMILARITY." Bond bond(268,282) /gene=nC1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(284,297) /gene=nC1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 299..341 /gene=nC1QR1" /region_name="Domain" /note="EGF-LIKE 2." Bond bond(303,314) /gene="C1QR1n /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(308,325) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Site 322 /gene="C1QR1" /site_type="glycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Bond bond(327,340) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 342..381 /gene="C1QR1" /regionjiame^'Domain" /note="EGF-LIKE 3, CALCIUM-BINDING (POTENTIAL)." Bond bond(346,355) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(351,364) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(366,380) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Region 382..423 /gene="C1QR1" /region_name="Domain" /note="EGF-LIKE 4, CALCIUM-BINDING (POTENTIAL)." Bond bond(386,397) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(393,406) /gene="C1QR1" /bond_type="disulfide" /note="BY .SIMILARITY." Bond bond(408,422) /gene="C1QR1" /bond_type="disull^de,, /note="BY SIMILARITY." Region 417 /gene="C1QR1" /region_name="Conflict" /note="E -> K (IN REF. 2)." Region 424..462 /gene="C1QR1" /region_name="Domain" /note="EGF-L!KE 5, CALCIUM-BINDING (POTENTIAL)." Bond bond(428,437) /gene="C1QR1n /bond_type="disulfide" /note='-'BY SIMILARITY." Bond bond(433,446) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Bond bond(448,461) /gene="C1QR1" /bond_type="disulfide" /note="BY SIMILARITY." Site 498 /gene="C1QR1" /site_type="giycosylation" /note="N-LINKED (GLCNAC.) (POTENTIAL)." Region 572..592 /gene="C1QR1" /region_name=nTransmembrane region" /note="POTENTlAL" Region 593.-643 /gene="C1QR1" /region_name="Domain" /note="CYTOPLASMlC (POTENTIAL)." • ORIGIN 1 nnvtstgllll Igllgqlwag aaadseawc egtacytahw gklsaaeaqh rcnenggnla 61 tvkseeearh vqealaqllk tkapsetkig kfwiglqrek gkctyhdlpm kgfswvggge 121 dttysnwyka skssciskrc vslildlslk phpshlpkwh espcgtpdap gnsiegflck 181 fnfkgmcspl alggpgqlty ttpfqattss Ikavpfasva nwcgdeaes ktnyylcket 241 tagvfhwgss gplcvspkfg csfnnggcqq dcfeggdgsf rcgcrpgfrl Iddlvtcasr 4 301 npcssnpctg ggmchsvpls enytchcprg yqldssqvhc vdidecedsp cdqecintpg 361 gfhcecwvgy qssgskeeac edvdectaay spcaqgctnt dgsfycscke gyimsgedst 421 qcedideclg npcdtlcint dgsfrcgcpa gfelapngvs ctrgsmfsel.parppqkedk 481 gdgkestvpl tempgslngs kdvsnraqtt dlsiqsdsst asvpleievs seasdvwldl 541 gtylpttsgh sqpthedsvp ahsdsdtdgq klllfyilgt vvaislllal alglliylkr 601 kakkeeikek kaqnaadsys wiperaesra penqysptpg tdc SEQIDNO:11 NPJD06601 mannan-binding lectin serine protease 2, isoform 1 precursor; MBL-associated plasma protein of 19 kD; small MBL-associated protein [Homo sapiens] gi|21264363|ref|NP_006601.2|[21264363] ■ sig_peptide 1..15 mat_peptide 16..444 /product="mannan-binding. lectin serine protease 2, isoform 1t chain A" Region 28..136/region_name=="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref=,,CDD:smart00042" Region 28..134 /region jiame="CUB domain" /note="CUB" /db_xref="CDD:pfam00431" Region 138.. 180 /region jiame="CaIcium-binding EGF-Iike domain" /note="EGF_CA" /db_xref="CDD:smart00179" variation 155 /allele="H" /allele="RH /dbjcref="dbSNP:2273343" Region 184..295/region_name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db„xref="CDD:smart00042" Region 184..293 /region_name="CUB domain" /note="CUB" /db_xref="CDD:pfam00431" Region 300..361 /region_name="Domain abundant in complement control proteins" /note="CCP7db_xref=HCDD:smart00032w Region 300..361 /region_name=,lSushi domain (SCR repeat)" /note="sushi" /db_xref="CDD:pfam00084n Region 366..430 /region_name=nDomain abundant in complement control proteins" /note="CCP" /db_xref=,,CDD:smart00032n Region 366..430 /region_name="Sushi domain (SCR repeat)" /note="sushr /db_xref="CDD:pfam00084" variation 377 /allele=MA" /allele="Vn /db_xref="dbSNP:2273346" Region 444..679 /region_name=Trypsin-iike serine protease" /note="Tryp_SPc" /db_xref="CDD:smart00020n mat_peptide 445..686 /product="mannan-binding lectin serine protease 2, isoform 1, chain B" Region 445..679 /region_name='TrypsinB /note="trypsin" /db__xref="CDD:pfam00089" CDS 1..686/gene="MASP2"/coded_by=nNM_006610.2:22..2082" /db_xref=nLocusID:10747"/db_xref="MIM:605102" ORIGIN 1 mrlltllgll cgsvatplgp kwpepvfgrl aspgfpgeya ndqerrwtlt appgyrlrly 61 fthfdlelsh Iceydfvkis sgakvlatlc gqestdtera pgkdtfyslg sslditfrsd 121 ysnekpftgf eafyaaedid ecqvapgeap tcdhhchnhl ggfycscrag yvlhrnkrtc 181 salcsgqvft qrsgeisspe yprpypklss ctysisleeg fsvildfves fdvethpetl 241 cpydfikiqt dreehgpfcg ktlphrietk sntvtitfvt desgdhtgwk ihytstaqpc 301 pypmappngh vspvqakyil kdsfsifcet gyellqghlp Iksftavcqk dgswdrpmpa 361 csivdcgppd dlpsgrveyi tgpgvttyka viqysceetf ytmkvndgky vceadgfwts 421 skgekslpvc epvcglsarttggriyggqk akpgdfpwqv lilggttaag allydnwvlt 481 aahavyeqkh dasaldirmg tlkrlsphyt qawseavfih egythdagfd ndialiklnn 541 kwinsnitp iclprkeaes fmrtddigta sgwgltqrgf larnlmyvdi pivdhqkcta 601 ayekppyprg svtanmlcag lesggkdscr gdsggalvfl dseterwfvg givswgsmnc 661 geagqygvyt kvinyipwie niisdf SEQIDN0:12 NP_631947 mannan-binding lectin serine protease 2, isoform 2 precursor; MBL-associated plasma protein of 19 kD; small MBL-associated protein [Homo sapiens] gi|21264361|ref|NP_631947.1|[21264361] sig_peptide 1.15 matjDeptide 16..185 /product=Hmannan-binding lectin serine protease 2, isoform 2" Region 28..136 /regionjiame-'Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:smart00042". Region 28..134 /region_name="CUB domain" /note="CUB" /db_xref="CDD:pfam0043r Region 138..180 /region_name=nCalcium-binding EGF-like domain" /note^EGFJ^AVdb^xref^DDismarKXmg" variation 155 /alIele=nHH /allele^R" /dbjcref="dbSNP:2273343" CDS 1 ..185 /gene^MASPa" /coded J)y="NMJ39208.1:22..579" /db_xref="LocuslD:10747"/db_xref=,,MIM:605102" ORIGIN .1 mrlltllgll cgsvatplgp kwpepvfgrl aspgfpgeya ndqerrwtlt appgyrlrly 61 fthfdlelsh Iceydfvkls sgakvlatlc gqestdtera pgkdtfyslg sslditfrsd. 121 ysnekpftgf eafyaaedid ecqvapgeap tcdhhchnhi ggfycscrag yvlhmkrtc 181 seqsl SEQIDNO:13 NPJ324302 mannan-binding lectin serine protease 1, isoform 2, precursor; protease, serine, 5 (mannose-binding protein-associated); manan-binding lectin serine protease-1; Ra-reactive factor serine protease p100 [Homo sapiens] gi|21264359|ref|NP_624302.1|[21264359] sig_peptide 1.19 mat_j>eptide 20..445 /product="mannan-binding lectin serine protease 1, isoform 2, chain A" variation 21 /a!lele=T /allele="T" /db_xref="dbSNP: 1062049" Region 23..138 /region_name="Domain first found in G1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref=,,CDD:smart00042', Region 23..135 /region_name="CUB domain" /note="CUB" /db_xref="CDD:pfam00431M Region 139.. 181 /region jiame-'Calcium-binding EGF-like domain" /note=nEGF_CA" /db_xref="CDD:smart00179" Region 185..294 /region_name="CUB domain" /note="CUB" /db__xref="CDD:pfam00431" Region 190..296 /region_name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:smart00042" variation 235 /allele=nQ" /allele=nE" /db_xref="dbSNP:3203210" variation 258 /allele^" /allele^A" /db_xref="dbSNP:866085" Region 301.362 /region_name=,,Domain abundant in complement control proteins" /note=,,CCP,,/db_xref=,,CDD:smart00032n Region 301.362 /region_name="Sushi domain (SCR repeat)" /note-'sushi" /db_xref="CDD:pfam00084" Region 367..432 /region_name="Domain abundant in complement control proteins" /hote="CCP" /db_xref=nCDD:smart00032" 'Region 367..4327region_name="Sushi domain (SCR repeat)" /note="sushi!f /db^xref^'CDDipfamOOOS^' mat_peptide 446.J28 /product="mannan-binding lectin serine protease 1, isoform 2, chain B" Region 449. J11 /region_name="Trypsin-Iike serine protease" /note="Tryp_SPc" /db_xref=nCDD:smart00020" Region 450..711 /region_name=Trypsin" /note=,,trypsinu/db_xref=,,CDD:pfam00089,, variation 616 /aIlele="A" /aIIele="V" /db_xref="dbSNP:2461280" Region 661..703 /region jname="lmmunoglobulin A1 protease" /note="IGA1" /db_xref="CDD:pfam02395" CDS 1..728/gene="MASP1M /coded by="NM_139125.1:51..2237" /db„xref="LocuslD:5648"/db_xref=nMIM:600521" ORIGIN 1 mrwlllyyal cfslskasah tvelnnmfgq iqspgypdsy psdsevtwni tvpdgfrikl 61 yfmhfnless ylceydyvkv etedqvlatf cgrettdteq tpgqewlsp gsfmsitfrs 121 dfsneerftg fdahymavdv deckeredee Iscdhychny iggyyescrf gyilhtdnrt 181 crvecsdnlf tqrtgvitsp dfpnpypkss eclytielee gfmvnl.qfed rfdiedhpev 241 pcpydyikik vgpkvlgpfc gekapepist qshsvlilfh sdnsgenrgw rlsyraagne 301 cpelqppvhg kiepsqakyf fkdqvlvscd tgykvlkdnv emdtfqiecl kdgtwsnkip 361 tckivdcrap gelehglitf strnnlttyk seikyscqep yykmlnnntg iytcsaqgvw 421 mnkvlgrslp tclpecgqps rslpslvkri iggrnaepgl fpwqalivve dtsrvpndkw 481 fgsgallsas wiltaahvlr sqrrdttvip vskehvtvyl gihdvrdksg avnssaarw 541 Ihpdfniqny nhdialvqlq epvplgphvm pvclprlepe gpaphmlglv agwgisnpnv 601 tvdeiissgt rtlsdviqyv klpvvphaec ktsyesrsgn ysvtenmfca gyyeggkdtc 661 Igdsggafvi fddlsqrww qglvswggpe ecgskqvygv ytkvsnyvdw vweqmglpqs 721 vvepqver SEQIDNO:14 NP_001870 mannan-binding lectin serine protease 1, isoform 1, precursor, protease, serine, 5 (mannose-binding protein-associated); manan-binding lectin serine protease-1; Ra-reactive factor serine protease p100 [Homo sapiens] gi|21264357|ref|NP_001870.3|[21264357] sig_peptide 1..19 mat_peptide 20..448 /product="mannan-binding lectin serine protease 1, isoform 1, chain A" variation 21 /a!lele=T /allele="r /db_xref="dbSNP: 1062049" Region 23..138 /regionjiame="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note="CUB" /db_xref="CDD:smart00042" Region 23.:135/region_name="CUBdomain"/note-'CUB" /db_xref="CDD:pfam00431" Region 139..181 /region_name="Calcium-binding EGF-like domain" /note=,,EGF_CA"/db_xref=^CDD:sma^t00179,, Region 185..294 /region_name="CUB domain" /note-'CUB" /db_xref="CDD:pfam00431" Region 190..296 /region_name="Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein." /note=,,CUB" /db_xref="CDD:smart00042" variation 235 /allele=nQ" /allele="E" /db_xref="dbSNP:3203210" variation 258 /allele="P" /allele="A" /db_xref="dbSNP:866085" Region 301..362 /region_name="Domain abundant in complement control proteins" /note="CCP" /db_xref=,,CDD:smart00032n Region 301..362 /region_name="Sushi domain (SCR repeat)" /note="sushi" /db_xrQf="Cpp:pfam00084" Region 367..432 /region_name=,!Domain abundant incomplement control proteins" /note=MCCP"/db_xref="CDD:smart00032" Region 367..432 /region_name="Sushi domain (SCR repeat)" /note="sushi" /db_xref="CDD:pfam00084,, Region 448..691 /regionjiame-Trypsin-Iike serine protease" /note=Tryp_SPc" /db_xref="CDD:smart00020" mat_peptide 449..699 /product="mannan-binding lectin serine protease 1, isoform 1t chain B" Region 449..691 /region_na'me=Trypsinn /note=,,trypsinM /db_xref="CDD:pfam00089". Region 644..675/region name="lmmunoglobuIin A1 protease"/note="IGA1" /db_xref="CDD:pfam02395" CDS1..699/gene="MASP1n/coded_by="NM_001879.3:5l..2150n /db-xref="Locus!D:5648,7db_xref="MIM;600521" ORIGIN 1 mrwlllyyal cfslskasah tvelnnmfgq iqspgypdsy psdsevtwni tvpdgfrikl 61. yfmhfnless ylceydyvkv etedqvlatf cgrettdteq tpgqevvlsp gsfmsitfrs 121 dfsneerftg fdahymavdv deckeredee Iscdhychny iggyycscrf gyilhtdnrt 181 crvecsdnlf tqrtgvitsp dfpnpypkss eclytielee gfmvnlqfed ifdiedhpev 241 pcpydyikik vgpkvlgpfc gekapepist qshsvlilfh sdnsgenrgw rlsyraagne 301 cpelqppvhg kiepsqakyf fkdqvlvscd tgykvlkdnv emdtfqiecl kdgtwsnkip 361 tckivdcrap gelehglitf strnnlttyk seikyscqep yykmlnnntg iytcsaqgvw 421 mnkvigrslp tclpvcgipk fsrklmarif ngrpaqkgtt pwiamlshln gqpfcggsll 481 gsswivtaah cihqsldped ptlrdsdlls psdfkiilgk hwrlrsdene qhlgvkhttl 541 hpqydpntfe ndvalvelle spvinafvmp iclpegpqqe gamvivsgwg kqflqrfpet 601 Imeieipivd hstcqkayap Ikkkvtrdmi cagekeggkd acagdsggpm vtlnrergqw 661 ylygtvswgd dcgkkdrygv ysyihhnkdw iqrvtgvrn SEQIDNO: 15 XP_1 22683 similar to mannose binding lectin, liver (A) [Mus musculus] gi|20872845|ref|XPJ22683.1|[20872845]. source 1..239 /organism="Mus musculus" /strain="C57BL/6J" /dbjcref="taxon: 10090" /chromosome="14" Protein 1 ..239 /product="similar to mannose binding lectin, liver (A)" Region 126..236 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note="CLECT" /db_xref=MCDD:smart00034" Region 135..237 /regionjiame="Lectin C-type domain" /note="lectin_cw /db_xref="CDD:pfam00059" CDS 1..239 /gene=nMbl1" /codedJ>y="XMJ 22683.1:10.729' /db„xref=,,LocuslD:17194l7db_xref=,,MGD:96923,, ORIGIN 1 mlllpllpvl Icwsvsssg sqtcedtlkt csviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr xxxxxxxxxx xxxxxxxxxx xxxxxxhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaipmae enkaiqevat giaflgitde 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQIDNO:16 AAM21196 C-type mannose-binding lectin [Oncorhynchus mykiss] gi]20385163|gb|AAM21196.1|AF363271J[20385163] source 1 ..185 /organism="Oncorhynchus mykiss" /db_xref="taxon:8022" Protein 1.. 185 /product="C-type mannose-binding lectin" CDS 1 ..185 /gene="MBL" /coded J)y="AF363271.1:25..582n ORIGIN 1 meklaillll sasialgdan Itqllglepl Iktkveqttp eaqveavqeg ikegscpsdw 61 ytygshcfkf vsiqqsfvds eqnclalggn lasvhslley qfmqaltkda nghlhstwlg 121 gfdaikegtw mwsdgsrfdy tnwdtdepnn agegedclhm naasaklwfd vpcewkfasl -181 csrrm SEQ ID NO: 17 AAD45377 mannose-binding lectin [Sus scrofa] gi|5566370|gb|AAD45377.1|AF164576J[5566370] source 1.240 /organism="Sus scrofa" /db_xref="taxon:9823" /tissueJype="liverH Protein 1..240/product="mannose-binding lectin" CDS 1 ..240 /coded_by="AF164576.1:1 ..723" ORIGIN 1 mslfpslhli llivmtasht etencediqn tclviscdsp ginglpgkdg Idgakgekge 61 pgqgliglqg Ipgmvgpqgs pgipglpglk gqkgdsgidp gnslanlrse Idnikkwlif 121 aqgkqvgkkl yltngkkmsf ngvkalcaqf qasvatptns renqaiqeia gteaflgitd 181 eytegqfvdl tgkrvryqnwndgepnnads aehcveilkd gkwndifcss qlsavcefpa SEQ ID NO: 1'3 NP_034905 mannose binding lectin, liver (A) [Mus musculus] gi|6754654|ref|NP_034905.1 '[6754654] source 1..239 /organism="Mus musculus" /db_xref="taxon: 10090" /chromosome="14" /map="14 15.0 cM" Protein 1..239 /product="mannose binding lectin, liver (A)" misc_feature 19..239 /partial /note="mature protein based on homology to rat MPB- A" Region 126..236 /region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)11 /note="CLECr /db_xref="CDD:smart00034" Region 135..237 /region_name="Lectin C-type domain" /note="lectin_c" /dbjcref^'CDD^famOOOSg" CDS 1..239 /gene="Mbi1" /coded J)y="NM_010775.1:121..840" /db_xref="LocusiD:17194" /db_xref="MGD: 96923" ORIGIN 1 mlllpllpvl Icwsvsssg sqtcedtlkt csviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeirilkskl qltnklhafs 121 mgkksgkkff vtnhekmpfs kvkslctelq gtvaipmae enkaiqevat giaflgitde . 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQ ID NO: 19 NP_034906 mannose binding lectin, serum (C) [Mus musculus] gi|6754656|ref|NP_034906.1|[6754656] source 1..244 /organism="Mus musculus" /strain="BALB/c" /sub_species="domesticus" /db_xref="taxon: 1*0090" /chromosome-'19" /map="19 25.0 cM" /clone="a10" /tissue_type="Iiver" /cloneJib="lambda gt10" Protein 1..244 /product="mannose binding lectin, serum (C)n sig_peptide 1..18- Region 120..241 /regionj"iame="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note=uCLECT" /db_xref="CDD:smart00034" Region 140..242 /region_name="Lectin C-type domain" /note="iectin_c" /db_xref="CDD:pfam00059" ' CDS1..244/gene-"Mbl2,7coded_by="NMM010776.1:177..911" /note="polysaccharide-binding component of RaRF; sequence similarity to mannose-binding proteins" /db_xref=BLocuslD:17195" /dbjcref="MGD:96924" ORIGIN 1 msfftsflll cvvtvvyaet Itegvqnscp wtcsspgln gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa Irselralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat prnaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcvv ilgngkwndv pcsdsflaic 241 efsd SEQIDNO:20 AAL14428 dendritic cell-specific ICAM-3 grabbing nonintegrin [Macaca nemestrina] gi|16118455|gbjAAL14428.1|AF343727_1[16118455] source 1..381 /organism=,1Macaca nemestrina,7db_xref="taxo^:9545,' /cell_type="peripheral blood-derived dendritic cells" Protein 1.381 /product="dendritic cell-specific ICAM-3 grabbing nonintegrin" /name="membrane-associated mannose binding lectin" CDS 1..381 /coded_by=,,AF343727.1:1..1146,,/note=I,DC-SIGN,, ORIGIN 1 msdskeprlq qldlleeeql ggvgfrqtrg ykslagclgh gplvlqllsf tllagllvqv 61 skvpsslsqg qskqdaiyqn Itqlkvavse Isekskqqei yqeltrlkaa vgelpekskq 121 qeiyeeltrl raavgelpek sklqeiyqel trlkaavgel pekskqqeiy qelsrlkaav 181 gdlpekskqq eiyqkltqlk aavdglpdrs kqqeiyqeli qlkaaverlc hpcpwewtff 241 qgncyfmsns qrnwhdsita cqevgaqlw iksaeeqnfl qlqssrsnrf twmglsdlnh 301 egtwqwvdgs pllpsfkqyw nkgepnnvge edcaefsgng wnddkcnlak fwickksaas 361 csgdeerlls papttpnppp a SEQIDNO:21 AAF63470 mannose binding-like lectin precursor [Carassius auratusj gi|7542474|gb| AAF63470.1 |AF227739J [7542474] source 1..246 /organism="Carassius auratus" /db_xref="taxon:7957" /tissue_type="liver" Protein sig_peptide Region 14..25/region_name=="N-terminal segment" Region 26.-93 /region_name="collagen-like structure" Region 60..63 /region_name="break in collagen structure" Region 94.. 124 /region_name="neck region" Region 125..246 /regionjiame-'carbohydrate recognition domain" /note="CRD" CDS 1..246 /gene="MBL" /coded_by=f,AF227739.1: structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 llllqfalql Idgaepqnln cpayggvpgt pghnglpgrd grdgkdgaig pkgekgesgv 61 svqgppgkag ppgtagekge rgpsgpqgsp gsesvleslk seiqqlkaki atfekvssvc 121 hfrkvgqkyy itdgwgnfd qglkscmefg gtmvsprtsa enqallklw ssglgskkpy 181 igvtdrkteg qfvdtegkql tftnwgpgqp ddykglqdcg viedtglwdd ggcgdirpim 241 ceidik SEQ ID NO: 22 AAF63469 mannose binding-like lectin precursor [Danio rerio] gi|7542472|gb|AAF63469.1 |AF227738J [7542472] sig_peptide 1..23 mat_peptide 24..251 /product="mannose binding-like lectin" Region 24..36 /region_name="N-terminal segment" Region 37..101 /regionjiame="collagen-like structure" Region 71..74 /region_name="break in collagen structure" Region 102.. 132 /region_name="neck region" Region 133..251 /region_name="carbohydrate recognition domain" /note="CRD" CDS 1..251 /gene="mbl" /coded J>y="AF227738.1:68.. 823" /note="co!iectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 mallklflga llllqlvlql magaadpqsl ncpayagvpg tpghnglpgr dgrvgrdgan 61 gpkgekgepg vnvqgppgka gppgpagakg ergpsglpgq dcmsdslkse Iqklsdkial 121 iekwnfktf kkvgqkyyvt ddveetfdkg mqycssngga Ivlprtleen allkvfvssa 181 fkrlfiritd rekegefvdt drkkltftnw gpnqpdnykg aqdcgaiads glwddvscds 241 lypiiceiei k SEQ ID NO: 23 AAF63468 mannose binding-like lectin precursor [Cyprinus carpio] gi|7542470|gb JAAF63468.1 |AF227737_1 [7542470] sig_peptide 1..23 mat_peptide 24..256 /product="mannose binding-like lectin" Region 24..35 /regionjiame="N-terminal segment" Region 36.. 103 /region_name="colIagen-like structure" Region 70..737region_name="break in collagen structure" Region 104..134 /region_name="neck region" Region 135..256 /region_name="carbohydrate recognition domain" /note="CRD" CDS 1..256 /gene="MBL" /coded_by="AF227737.1:67..837" /note="co!lectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose" ORIGIN 1 malfklflgt llllqfalql Idgaepqnln cpayggvpgt pghnglpgrd grdgkdgaig 61 pkgekgesgv svqgppgkag ppgpagekge rgptgsqgsp gsesvleslk sejqqikaki 121 atfekvasvg hfrqvgqkyy itdgwgtfd qglkfckdfg gtmvfprtsa enqallkiw 181 ssglsskkpy igvtdreteg rfvntegkql tftnwgpgqp ddykglqdcg viedsglwdd 241 gscgdirpim ceidnk SEQ ID NO: 24 AAF21018 mannose-binding lectin 2 [Sus scrofa] gi|6644342|gb|AAF21018.1|AF208528J[6644342] source 1..31 /organism="Sus scrofa" /db_xref="taxon:9823" /chromosome="14" /map="between S0007 and Sw210H Protein 31 /product="mannose-binding lectin 2" /name="MBL2" CDS1..31/gene="MBL2" /coded-by=njoin(AF208528.1:771)" ORIGIN 1 tkgekgepgp gfrgsqgppg kmgppgnige t SEQ ID NO: 25 AAK30298 mannose-binding lectin precursor protein [Gallus gallus] gi|13561409|gb|AAK30298.1|[13561409] sig_peptide 1..21 mat_peptide 22..254 /product="mannose-binding lectin protein" . Region 22..46/region_name="N-terminal segment" Region 47..102 /region_name=,,collagen-Iike" Region 66 /region_name="break in collagen-like structure" Region 103.. 139 /regionjiame="neck region" Region 140..254 /region_name=ncarbohydrate recognition domain; CRD" CDS 1.254 /coded jDy="AF231714.1:242.. 1006" ORIGIN 1 mtllqpfsal llclslmmat sllttdkpee kmyscpiiqc. sapavnglpg rdgrdgpkge 61 kgdpgegirg Iqgipgkagp qglkgevgpq gekgqkgerg ivvtddlhrq itdleakirv 121 leddlsrykk aislkdwnv gkkmfvstgk kynfekgksl cakagsvlas pmeaental 181 kdlidpssqa yigisdaqte grfmylsggp Itysnwkpge pnnhknedca viedsgkwnd 241 Idcsnsnifi icel SEQ ID NO: 26 LNMSMC mannose-binding lectin C precursor- mouse gi|7428747]pir|]LNMSMC[7428747] FEATURES Location/Qualifiers source 1..244/organism="Mus musculus" /db_xref="taxon: 10090" Protein 1..244/product="mannose-binding lectin C precursor"/note="Ra-reactive factor P28a" Region 1..18 /region_name="domain" /note="signal sequence" Region 19..244/region_name="product"/note=,,mannose-binding lectin C" Bond bond(29)7bondJype="disulfide" /note="interchain" Bond bond(34) /bond_type=ndisulfide" /note="interchain" Region 38..94 /region_name="region"/note="collagen-like" Site 69 /siteJype=nmodified" /note="4-hydroxyproline (Pro)" Region 124. .240 /regionjiame^'domain11 /note="C-type lectin homology #label LCH" ORIGIN 1 msiftsflll cvvtwyaet Itegvqnscp wtcsspgln gfpgkdgrdg akgekgepgq 61 glrglqgppg kvgptgppgn pglkgavgpk gdrgdraefd tseidseiaa lrselralrn 121 wvlfslsekv gkkyfvssvk kmsldrvkal csefqgsvat prnaeensai qkvakdiayl 181 gitdvrvegs fedltgnrvr ytnwndgepn ntgdgedcw ilgngkwndv pcsdsflaic 241 efsd SEQIDNO:27 LNMSMA mannose-binding lectin A precursor - mouse gi|625320|pir||LNMSMA[625320] FEATURES Location/Qualifiers source 1..239 /organism="Mus musculus" /db_xref="taxon:10090n Protein 1..239 /product=Mmannose-binding lectin A precursor" /note="Ra-reactive factor P28b; serum mannan-binding protein" Region 1..17 /region_name="domain,! /note="signal sequence" 'Region 18..238 /region_name="product" /note="mannose-binding lectin A" Region 36..88 /region_name-"region" /note="collagen-like" Region 119..235 /region_name=,'domain" /note="C-type lectin homology #label LCH" ORIGIN 1 mlllpllpvl Icwsvsssg sqtcedtlkt psviacgrdg rdgpkgekge pgqglrglqg 61 ppgklgppgs vgspgspgpk gqkgdhgdnr aieeklanme aeirilkskl qltnklhafs 121 mgkksgkklf vtnhekmpfs kvkslctelq gtvaiprnae enkaiqevat giaflgitde 181 ategqfmyvt ggrltysnwk kdepnnhgsg edcviildng Iwndiscqas fkavcefpa SEQ ID NO: 28 LNRTMA mannose-binding lectin A precursor - rat gi|71975|pir||LNRTMA[71975] FEATURES Location/Qualifiers source 1..238 /organism=nRattus norvegicus" /db xref="taxon:10116" Protein 1 ..238 /product="marinose-binding lectin A precursor" /note="serum mannan-binding protein" Region 1..17 /region_name="domain" /note="signaI sequence" Region IS.^SS/region^name^'producr/ndte^'mannose-binding lectin A" Region 36..88 /region_name="region" /note="co!Iagen-like" Site 61 /siteJype="modified" /note="4-hydroxyproline (Pro)" Site 67 /site_type="modified" /note="4-hydroxyproline (Pro)" Site 73 /site_type="modified" /note="4-hydroxyproline (Pro)" Site 79 /siteJype=!lmodified" /note="lysine derivative (Lys) (probably 5- hydroxylysine)" Site 82 /site Jype="modified" /note="lysine derivative (Lys) (probably 5- hydroxylysine)" Region 85..87 /region_name=,'region,7note="ceII attachment (R-G-D) motif1 Region 118..234 /region_name=wdomain" /note="C-type lectin homology #label LCH" ORIGIN 1 mlllpllvll cvvsvsssgs qtceetlktc sviacgrdgr dgpkgekgep gqglrglqgp 61 pgklgppgsv gapgsqgpkg qkgdrgdsra ievklanmea eintlkskie Itnklhafsm 121 gkksgkkffv tnhermpfsk vkalcselrg tvaiprnaee nkaiqevakt saflgitdev 181 tegqfmyvtg grltysnwkk depndhgsge dcvtivdngl wndiscqash tavcefpa SEQ ID NO: 29 LNRTMC mannose-binding lectin C precursor- rat gi|71974|pir||LNRTMC[71974] FEATURES Location/Qualifiers source 1..244/organism=HRattus norvegicus" /db_xref="taxon:10116" Protein 1..244 /product=nmannose-binding lectin C precursor" Region 1.. 18 /region j^ame="domain" /note="signal sequence" Region 19..244/region_name="productn/note-'mannose-binding lectin C" Bond bond(29) /bondjype^'disulfide" /note="interchain" Bond bond(34) /bond_type="disulfideM /note="interchain" Region 38..94 /region_name="region" /note=ncollagen-like" Site 69 /siteJype=nmodified" /npte="4-hydroxyproline (Pro)" Region 124. .240 /region_name="domain" /note="C-type lectin homology #label LCH" ORIGIN 1 mslftsflll cvltavyaet Itegaqsscp viacsspgln gfpgkdghdg akgekgepgq 61 glrglqgppg kvgpagppgn pgskgatgpk gdrgesvefd ttnidleiaa Irselramrk 121 wvllsmseriv gkkyfmssvr rmplnrakal cselqgtvat prnaeenrai qnvakdvafl 181 gitdqrtenvfedltgnrvrytnwnegepn nvgsgencw lltngkwndv pcsdsflwc 241 efsd SEQ ID NO: 30 LNHUMC mannose-binding lectin precursor - human gi|71973|pir|[LNHUMC[71973] FEATURES Location/Qualifiers source 1..248 /organism-'Homo sapiens" /db_xref="taxon:9606" Protein 1..248 /product="mannose-binding lectin precursor" /note="mannan-binding protein" Region 1..20./region_name="domain" /note="signal sequence" Region 21..248/region_name="product"/note="mannose-binding lectin" Region 42..99 /region_name="region" /note="collagen-liken Site 47/site_type="modifiedn./note="4-hydroxypro!ine (Pro) (partial)" Site 73 /siteJype="modifiedw /note="4-hydroxyproline (Pro) (partial)" Site 79 /site__type="modified" /note="4-hydroxyproline (Pro) (partial)" Site 82 /siteJype="modified" /note="4-hydroxyproline (Pro) (partial)" . Site 88 /siteJype=" modified" /note="4-hydroxyproline (Pro) (partial)" Region 128..244 /regionjiame^'domain1' /note="C-type lectin homology #label LCH" ORIGIN 1 mslfpslpll llsmvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgkigppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQIDNO:31 BAA86864 complement C1s [Homo sapiens] gi|6407558|dbj|BAA86864.1 |[6407558J FEATURES Location/Qualifiers source 1..329 /organism="Homo sapiens" /db_xref=ntaxon:9606° /tissueJype=r,peripheral leukocytes" /cloneJib="FIXH" Protein 1..329 /product=McomplementC1s" CDS 1..329 /coded jDy="join(AB009076.1:1142..1146, AB009076.1:1703..1910,AB009076.1:2118..2295, AB009076.1:3495..3620,AB009076.1:4328..4527, AB009076.1:5047..5200,AB009076.1:5748..>5863)" /note='This gene consists of total 12 exons, the last 4 exons of which were reported by Toshi,M. et al.(J.Mol.Biol. 208:709-714, 1989) ORIGIN 1 mwcivlfsll awvyaeptmy geilspnypq aypseveksw dievpegygi hlyfthldie 61 lsencaydsv qiisgdteeg rlcgqrssnn phspiveefq vpynklqvif ksdfsneerf 121 tgfaayyvat dinectdfvd vpcshfcnnf iggyfcscpp eyfihddmkn cgvncsgdvf 181 taligeiasp nypkpypens rceyqirlek gfqvwtlrr edfdveaads agncldslvf 241 vagdrqfgpy cghgfpgpln ietksnaldi rfqtdltgqk kgwkiryhgd pmpcpkedtp 301 nsvwepakak yvfrdwqit cldgfewe SEQ ID NO: 32 CAB56124 mannose-binding lectin [Homo sapiens] gi|5911809|emb|CAB56124.11[5911809] FEATURES Location/Qualifiers source 1..248 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="10" /map="10q11,2-q21" /note="MBL haplotype HYPD" Protein 1..248/product="mannose-binding lectin" sig_peptide 1..20 CDS 1..248 /gene="MBLtt /coded_by="Y16582.1:892..1638" ORIGIN 1 mslfpslpll llsmvaasys etvtcedaqk tcpaviacss pgingfpgkd gcdgtkgekg 61 epgqglrglq gppgkigppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 33 CAB56123 mannose-binding lectin [Homo sapiens] ' gi|5911807|emb[CAB56123.11[5911807] FEATURES Location/Qualifiers source 1..248 /organism="Homo sapiens" /db_xref=Htaxon:9606" /chromosome^lO" /map="10q11.2-q211' /note="MBL haplotype HYP A" Protein 1..248 /product="mannose-binding lectin" sig_peptide 1..20 CDS 1..248 /gene="MBL" /codedJ>y="Y16581.1:892.. 1638" ORIGIN 1 mslfpslpll lismvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 34 CAB56122 mannose-binding lectin [Homo sapiens] gi|5911798|emb|CAB56122.1|[5911798] FEATURES Location/Qualifiers source 1..248 /organism="Homo sapiens" /db xref="taxon:9606" /chromosome=M10" /map="10q11.2-q21H /note="MBL haplotype LXPA" Protein 1..248 /product="mannose-binding lectin" sig_peptide 1.20 CDS 1.248/gene="MBL,,/coded_by=,IY16580.1:892..1638,l ORIGIN 1 mslfpslpll lismvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ IDNO: 35 CAB56121 mannose-binding lectin [Homo sapiens] gi|5911796|emb|CAB5612U|[5911796] FEATURES Location/Qualifiers source 1.248 /organism=!,Homo sapiens" /db^xref^taxon^eoe'Vchromosome^lO'Vmap^lOqll^^r'/note^MBL haplotype LYPB" Protein 1.248 /product="mannose-binding lectin" sig_peptide 1.20 CDS 1.248 /gene="MBL" /coded_by="Yl6579.1:892..1638" ORIGIN 1 mslfpslpll lismvaasys etvtcedaqk tcpaviacss pgingfpgkd grddtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 36 CAB56045 mannose-binding lectin [Homo sapiens] gi|5911794|emb|CAB56045.11[5911794] /organism="Homo sapiens"/db_xref="taxon:9606" /chromosome^! 0" /map=,,10q1l2-q21"7note="MBL haplotype LYQC" Protein 1.248 /product="mannose-binding lectin" sig_peptide 1..20* CDS 1.248 /gene="MBL" /coded_by="Y16578.1:886.. 1632" ORIGIN 1 mslfpslpll lismvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkeekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 37 CAB56120 mannose-binding lectin [Homo sapiens] gi|5911792|emb|CAB56120.11[5911792} FEATURES Location/Qualifiers source 1..248 /organism="Homo sapiens" /db_xref=!'taxon:9606" /chromosome=n10" /map=n10q11.2-q2l" /note=MMBL haplotype LYPA" Protein 1..248 /product="mannose-binding lectin" sigjeptide 1..20 CDS 1..248 /gene="MBL" /coded_by="Y16577.1:892.. 1638" ORIGIN 1 mslfpslpll llsmvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 38 CAB56044 mannose-binding lectin [Homo sapiens] gi|5911790|emb|CAB56044.11[5911790] FEATURES Location/Qualifiers source 1.248 /organism="Homo sapiens" /db_xref=,,taxon:9606Vchromosome=u10,7map="10q11.2-q21,7note="MBL haplotype LYQA" Protein 1.248/product="mannose-binding lectin" sig_peptide 1.20 CDS 1.248 /gene="MBL" /coded_by="Y16576.1:886..1632" ORIGIN 1 mslfpslpll llsmvaasys etvtcedaqk tcpaviacss pgingfpgkd grdgtkgekg 61 epgqglrglq gppgklgppg npgpsgspgp kgqkgdpgks pdgdsslaas erkalqtema 121 rikkwltfsl gkqvgnkffl tngeimtfek vkalcvkfqa svatprnaae ngaiqnlike 181 eaflgitdek tegqfvdltg nrltytnwne gepnnagsde dcvlllkngq wndvpcstsh 241 lavcefpi SEQ ID NO: 39 AAB53110 C1qR(p) [Homo sapiens] gi|2052498|gbjAAB53110.1|[2052498] FEATURES Location/Qualifiers source l;652 /organism="Homo sapiens" /db_xref=Mtaxon:9606M /cellJine="U937 histiocytic cell line" Protein 1.652 /product="C1qR(p)" /function="mediates enhanced phagocytosis by human monocytes and macrophages in response to complement C1q, mannose binding lectin (MBL) and pulmonary surfactant protein A (SPA)" CDS 1 ..652 /coded_by="U94333.1:149..2107" /note="Clq/MBL/SPA receptor" ORIGIN 1 matsmgllli llllltqpga gtgadteaw cvgtacytah sgklsaaeaq nhcnqnggnl 61 atvkskeeaq hvqrvlaqll rreaaltarm skfwiglqre kgkcldpslp Ikgfswvggg 121 edtpysnwhk elrnsciskr cvsllldisq pllpnrlpkw segpcgspgs pgsniegfvc 181 kfsfkgmcrp lalggpgqvt yttpfqttss sleavpfasa arivacgegdk detqshyflc 241 kekapdvfdwgssgplcvsp kygcnfnngg chqdcfeggd gsflcgcrpg frllddlvtc 301 asrnpcsssp crggatcvlg phgknytcrc pqgyqidssq Idcvdvdecq dspcaqecvn 361 tpggfrcecw vgyepggpge gacqdvdeca Igrspcaqgc tntdgsfhcs ceegyvlage 421 dgtqcqdvde cvgpggplcd slcfntqgsf hcgclpgwvl apngvsctmg pvslgppsgp 481 pdeedkgeke gstvpraata sptrgpegtp katpttsrps Issdapftsa plkmlapsgs 541 sgvwrepsih hataasgpqe paggdssvat qnndgtdgqk lllfyilgtv vaillllala 601 Iglivyrkrr akreekkekk pqnaadsysw vperaesram enqysptpgt dc SEQ ID NO: 4n NP_571645 mannose binding-like lectin [Danio rerio] gi|18858997|ref|NP_571645.1|[18858997] sigjDeptide 1..23 • mat_peptide 24..251. /product="mannose binding-like lectin" • Region 24..36 /regionjname="N-terminal segment" Region 33..70 /fegion_name="Collagen triple helix repeat (20 copies)" /note="Collagen" /db_xref="CDD:pfam01391" Region 33..70 /region jTame=nCollagen triple helix repeat (20 copies)" /note="ColIagen,7db_xref=,,CDD:pfam01391" Region 37.. 101 /region_name="collagen-like structure" Region 37..70 /region_name="Coliagen triple helix repeat (20 copies)" /note="ColIagen" /db_xref=nCDD:pfam01391" Region 71 ..74 /regionjiame="break in collagen structure" Region 102.. 132 /regionjname="neck region" Region 133..251 /region_name="carbohydrate recognition domain" /note="CRD" Region 134..247/region_name="C-type lectin (CTL) or carbohydrate-recognition domain (CRD)" /note=nCLECT" /db_xref="CDD:smart00034" Region 146..247 /region_name="Lectin C-type domain" /note="Iectin_c" /dbjcref="CDD:pfam00059" CDS 1..251 /gene="mbr /coded_by="NMJ31570.1;68..823,, /note="collectin with structural homology to mannose-binding lectin but with a predicted carbohydrate specificity for galactose;mannose binding-like lectin" /db_xref=nLocuslD:58091" • ORIGIN 1 mallklflga llllqlvlql magaadpqsl ricpayagvpg tpghnglpgr dgrvgrdgan 61 gpkgekgepg vnvqgppgka gppgpagakg ergpsgipgq dcmsdslkse Iqklsdkial 121 iekwnfktf kkvgqkyyvt ddveetfdkg mqycssngga Ivlprtleen allkvfvssa 181 fkrlfiritd rekegefvdt drkkltftnw gpnqpd'nykg aqdcgaiads glwddvscds 241 lypiiceiei k SEQ ID NO: 41 BAA90338 mannose-binding lectin-associated serine protease (MASP) related protein [Cyprinus carpio] gi|6807499jdbj|BAA90338.1|[6807499] FEATURES Location/Qualifiers source 1..118/organism="Cyprinus carpio" /db_xref="taxon:7962n Protein 1..118 /product=nmannose-binding lectin-associated serine protease (MASP) related protein" CDS1..118/gene="MRPbn /coded_by="join(AB030447.1 : The second polypeptide preferably comprises at least 10, such as at least 12, for example at least 15, such as at least 20, for example at least 25, such as at least 30, for example at least 35, such as at least 40, for example at least 50 consecutive amino acid residues of the collectin or of a variant or a homologue to said protein. Such a variant or homologue is preferably at least 70%, such as 80%, for example 90%, such as 95% identical to the collectin. In a preferred'embodiment the second polypeptide sequence comprises the CRD domain of MBL or the neck region of MBL or the collagen-like domain of MBL. More preferably the second polypeptide comprises the neck region and the CRD domain of MBL. In a most preferred embodiment the second polypeptide sequence com¬prises the collagen-like domain, the neck region and the CRD domain of MBL. MBL is as defined above. quence shown quence shown quence shown quence shown quence shown quence shown quence shown quence shown Preferably the second polypeptide sequence comprises at least amnio acids 170-200 of the MBL sequence shown in Figure 2, such as at least amino acids 160-200 of the MBL sequence shown in Figure 2, such as at least amino acids 150-200 of the MBL sequence shown in Figure 2, such as at least amino acids 140-200 of the MBL sequence shown in Figure 2, such as at least amino acids 130-200 of the MBL sequence shown in Figure 2, such as at least amino acids 120-200 of the MBL se- n Figure 2, such as at least amino acids 110-200 of the MBL se-n Figure -2, such as at least amino acids 100-200 of the MBL se-n Figure 2, such as at least amino acids 90-200 of the MBL se-n Figure 2, such as at least amino acids 80-200 of the MBL se-n Figure 2, such as at least amino acids 70-200 of the MBL se-n Figure 2, such as at least amino acids 60-200 of the MBL se-n Figure 2, such as at least amino acids 80-228 of the MBL se-n Figure 2. Preferably the second polypeptide sequence comprises amino acids 80-228 of SEQ ID. NO 2. In a preferred embodiment the second polypeptide sequence is capable of associ¬ating with at least one MASP protein, such as a MASP protein selected from the group consisting of MASP-1, MASP-2 and MASP-3 or functional homologues or variants hereof. In particular the second polypeptide is capable of associating with said at least one MASP protein when being part of the fusion protein. Thereby the second polypeptide sequence is capable of providing the fusion protein with com¬plement system activating activity. In a preferred embodiment the second polypep¬tide sequence comprises an amino acid sequence selected from: 56-228 of SEQ ID. NO 2, 55-228 of SEQ ID. NO 2, 54-228 of SEQ ID. NO 2, and 50-228 of SEQ ID. NO 2. In a preferred embodiment the second polypeptide sequence has an amino acid sequence selected from: 56-228 of SEQ ID. NO 2, 55-228 of SEQ ID. NO 2, 54-228 of SEQ ID. NO 2, and 50-228 of SEQ ID. NO 2. In another embodiment the second polypeptide comprises the cysteine-rich region of the collectin, such as the N-terminal region of the collectin. Fusion protein The fusion protein comprises the first and the second polypeptide connected to each other, optionally through a (inker region. In a preferred embodiment the first poly¬peptide sequence is positioned N-terminally in the fusion protein and the second polypeptide sequence is positioned C-terminally. Specific examples of the components of the fusion protein are: - A fusion protein comprising the cysteine-rich region and the collagen-like domain of L-ficolin and the CRD domain of MBL - A fusion protein comprising the cysteine-rich region of L-ficoiin and the collagen¬like domain, the neck region and the CRD domain of MBL. - A fusion protein comprising the cysteine-rich region and the collagen-like domain of H-ficolin and the CRD domain of MBL. - A fusion protein comprising the cysteine-rich region of H-ficolin and the collagen¬like domain, the neck region and the CRD domain of MBL. --A fusion protein comprising the cysteine-rich region and the collagen-like domain of M-ficolin and the CRD domain of MBL - A fusion protein comprising the cysteine-rich region of M-fico!in and the collagen- like domain, the neck region and the.CRD domain of MBL. - A fusion protein comprising the cysteine-rich region of MBL, and the CRD domain of ficoiin. - A fusion protein comprising the cysteine-rich region of MBL and the collagen-like domain, the neck region and the CRD domain of ficoiin. - A fusion protein comprising the cysteine-rich region and the collagen-like domain of L-ficolin and the CRD domain of Pulmonary surfactant-associated protein D. - A fusion protein comprising the cysteine-rich region of L-ficolin and the collagen¬like domain, the neck region and the CRD domain of Pulmonary surfactant-associated protein D. - A fusion protein comprising the cysteine-rich region and the collagen-like domain of a ficoiin and the CRD domain of a coIIectin-43. - A fusion protein comprising the cysteine-rich region of a ficoiin and the collagen¬like domain, the neck region and the CRD domain of a collectin-43. A fusion protein comprising the amino acid sequence as defined by the sequence shown in Figure 3, or a functional homologue thereof, preferably a fusion protein consisting of the amino acid sequence as shown in Figure 3. In another embodiment the fusion protein has amino acid sequence 1-50 of the amino acid shown in Figure 1 and amino acid sequence 54-228 of the amino acid sequence shown in Figure 2. As discussed above the.fusioh protein is preferably capable of forming subunit com¬plexes as well as oligomers of subunit complexes. Preferably the fusion protein forms substantially only trimeric, tetrameric, pentameric and hexameric subunit oli¬gomers, such as trimeric, tetrameric, and pentameric subunit oligomers, such as trimeric or tetrameric subunit oligomers, more preferably substantially only tet¬rameric subunit oligomers, in order to obtain a more homogenous composition of fusion proteins. Homoloques In the present context the terms homologue or variant or functional- homologues are used as synonymes, wherein a homologue of a protein exhibits one or more substi-tuions, deletions, and/or additions of one or more amino acid residues. Fragments are a subgroup of homologues being truncations of the protein. A homologue of the protein may comprise one or more conservative amino acid substitutions, such as at least 2 conservative amino acid substitutions, for example at least 3 conservative amino acid substitutions, such as at least 5 conservative amino acid substitutions, for example at least 10 conservative amino acid substitu¬tions, such as at least 20 conservative amino acid substitutions, for example at least 50 conservative amino acid substitutions such as at least 75 conservative amino acid substitutions, for example at least 100 conservative amino acid substitutions. Conservative amino acid substitutions within the meaning of the present invention is substitution of one amino acid within a predetermined group of amino acids for an¬other amino acid within the same predetermined group, exhibiting similar or sub¬stantially similar characteristics. Such predetermined groups are for example: polar side chains (Asp, Glu, Lys, Arg, His, Asn, Gin, Ser, Thr, Tyr, and Cys,) non-polar side chains (Gly, Ala, Val, Leu, lie, Phe, Trp, Pro, and Met) aliphatic side chains (Gly, Ala Val, Leu, lie) cyclic side chains (Phe, Tyr, Trp, His, Pro) aromatic side chains (Phe, Tyr, Trp) acidic side chains (Asp, Glu) basic side chains (Lys, Arg, His) amide side chains (Asn, Gin) hydroxy side chains (Ser, Thr) sulphor-containing side chains (Cys, Met), and amino acids being monoamino-dicarboxylic acids or monoamino-monocarboxylic-monoamidocarboxylic acids (Asp, Glu, Asn, Gin). Conservative substitutions may be introduced in any position of a preferred protein. It may however also be desirable to introduce non-conservative substitutions. A non-conservative substitution should lead to the formation of a homologue of a protein capable of exerting a function similar to the function of said protein. Such substitu¬tion could for example i) differ substantially in hydrophobicity, for example a hydro¬phobic residue (Val, lie, Leu, Phe or Met) substituted for a hydrophilic residue such as Arg, Lys, Trp or Asn, or a hydrophilic residue such as Thr, Ser, His, Gin, Asn, Lys, Asp, Glu or Trp substituted for a hydrophobic residue; and/or ii) differ substan¬tially in its effect on polypeptide backbone orientation such as substitution of or for Pro or Gly by another residue; and/or iii) differ substantially in electric charge, for example substitution of a negatively charged residue such as Glu or Asp for a posi¬tively charged residue such as Lys, His or Arg {and vice versa); and/or iv) differ sub¬stantially in steric bulk, for example substitution of a bulky residue such as His, Trp, Phe or Tyr for one having a minor side chain, e.g. Ala, Giy or Ser (and vice versa). In a further embodiment the present invention relates to homologues of a preferred protein, wherein such homologues comprise substituted amino acids having hydro¬philic or hydropathic indices that are within +/-2.S, for example within +/- 2.3, such as within +/- 2.1, for example within +/- 2.0, such as within +/-1.8, for example within +/-1.6, such as within +/-1.5, for example within +/-1.4, such as within +/-1.3 for example within +/-1.2, such as within+/-1.1, for example within +/-1.0, such as within +/- 0.9, for example within +/- 0.8, such as within +/- 0.7, for example within +/- 0.6, such as within +/- 0.5, for example within +/- 0.4, such as within +/-•0.3, for example within +/- 0.25, such as within +/- 0.2 of the value of the amino acid it has substituted. The importance of the hydrophilic and hydropathic amino acid indices in conferring interactive biologic function on a protein is well understood in the art (Kyte & Doolit-tle, 1982 and Hopp, U.S. Pat. No. 4,554,101, each incorporated herein by refer¬ence). The amino acid hydropathic index values as used herein are: isoleucine (+4.5); va¬line (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+1.9); alanine (+1.8); glycine (-0.4 ); threonine (-0.7 ); serine (-0.8 ); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (-3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (-4.5) (Kyte & Doolittle, 1982). The amino acid hydrophilicity values are: arginine (+3.0); lysine (+3.0); aspartate (+3.0.+-.1); glutamate (+3.0.+-.1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (-0.4); proline (-0.5.+-.1); alanine (-0.5); histidine (-0.5); cys¬teine (-1.0); methionine (-1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4) (U.S. 4,554,101). Substitution of amino acids can therefore in one embodiment be made based upon their hydrophobicity and hydrophilicity values and the relative similarity of the amino acid side-chain substituents, including charge, size, and the like. Exemplary amino acid substitutions which take various of the foregoing characteristics into considera¬tion are well known to those of skill in the art and include: arginine and lysine; glu¬tamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine. Furthermore, a homologue may comprise addition or deletion of an amino acid, for example an addition or deletion of from 2 to 100 amino acids, such as from 2 to 50 amino acids, for example from 2 to 20 amino acids, such as from 2 to 10 amino ac¬ids, for example from 2 to 5 amino acids, such as from 2 to 3 amino acids. However, additions of more than 100 amino acids, such as additions from 100 to 500 amino acids, are also comprised within the present invention. Proteins sharing at least some homology with a preferred protein are to be consid¬ered as falling within the scope of the present invention when they are at least about 40 percent homologous, or preferably, identical, with the preferred protein, such as at least about 50 percent homologous, or preferably identical, for example at least about 60 percent homologous, or preferably identical, such as at least about 70 per¬cent homologous, or preferably identical, for example at least about 75 percent ho¬mologous, or preferably identical, such as at least about 80 percent homologous, or preferably identical, for example at least about 85 percent homologous, or preferably identical, such as at least about 90 percent homologous, or preferably identical, for example at least 92 percent homologous, or preferably identical, such as at least 94 percent homologous, or preferably identical, for example at least 95 percent ho¬mologous, or preferably identical, such as at least 96 percent homologous, or pref¬erably identical, for example at least 97 percent homologous, s or preferably identi¬cal, uch as at least 98 percent homologous, or preferably identical, for example at least 99 percent homologous, or preferably identical, with the preferred protein. Preferred proteins are complement activating proteins comprising collectins and lectins and homologues hereof. Homoloques of collectins A homologue of a collectin including MBL within the scope of the present invention should be understood as any protein capable of exerting a function similar to the function of a collectin and comprising one or more of the variations described above. In particular such function is the ability to activate complement upon binding to one or more carbohydrates. The terms functional homologues oicollectin used herein relate to functional equivalents or a fragment of collectin comprising a predetermined amino acid se¬quence, and such homologues are defined as: a) A homologue comprising an amino acid sequence capable of recognising and binding to glucans, lipophosphoglycans and glycoinositol phospholipids that contain sugar with 3- and 4-hydroxyl groups in the pyranose ring (i.e. Man, Glc, Fuc or GlcNAc) either alone or when being subunit complexed as described above and/or b) A homologue comprising an amino acid sequence capable of forming an asso¬ciation with a component of the Lectin/MBL pathway such as binding to the MASP-1, MASP-2, MASP-3 and/or sMAP either alone or when being subunit complexed as described above, wherein said binding result in activation of the Lectin/MBL pathway and/or c) A homologue comprising an amino acid sequence capable of by the collagen¬like domain forming an oligomeric structure of two or more subunits, where a subunit comprises three identical polypeptides of a cysteine-rich region, a colla¬gen-like domain, a neck region and a carbohydrate recognition domain. Homoloques of lectins A homologue of a lectin including ficolins within the scope of the present invention should be understood as any protein capable of exerting a function similar to the ' function of a lectin and comprising one or more of the variations previously de¬scribed. In particular such function is the ability to activate complement upon binding to one or more carbohydrates. The terms functional homologues of lectin used herein relate to functional equiva¬lents of a fragment of lectin comprising a predetermined amino acid sequence, and such homologues are defined as: a) A homologue comprising an amino acid sequence capable of recognising and binding to N-acetyi-glucosamine (GlcNAc), or N-acetyl-galactosamine (GalNAc), or elastin either alone or when being subunit complexed as described above and/or b) A homologue comprising an amino acid sequence capable of forming an asso¬ciation with a component of the Lectin/MBL pathway such as binding to the MASP-1, MASP-2, MASP-3 and/or sMAP either alone or when being subunit complexed as described.above, wherein said binding result in activation of the Lectin/MBL pathway and/or c) A homologue comprising an amino acid sequence capable of by the collagen-like domain forming an .oiigomeric structure of two or more subunits, where a subunit comprises three identical polypeptides of a cysteine-rich region, a colla-gen-iike domain, a-neck region and a fibrinogen-like domain. The activation of the lectin/MBL pathway, i.e. the activity of the fusion protein to acti¬vate the complement system may be assessed by assessing the C4 cleaving effect of the fusion protein or subunit complexes or oligomers of complexes thereof by the following method comprising the steps of - applying a sample comprising a predetermined amount of fusion protein as well as a predetermined amount of MASP-1, MASP-2 or MASP-3, - applying at least one complement factor to the sample, - detecting the amount of cleaved complement factors, - correlating the amount of cleaved complement factors to the.amount of fusion protein, and - determining the activity of the fusion protein. The complement factor preferably.used in the present method is a complement fac¬tor cleavable by the MBL/MASP-2 complex, such as C4. However, the complement factor may also be selected from C3 and C5. The cleaved complement factor may be detected by a variety of means, such as by of antibodies directed to the cleaved complement factor. The assay is carried out at conditions which minimize or eliminate interference from the classical complement activation pathway and the alternative complement activa¬tion pathway. Preferably a homologue of a collectin and/or a lectin exhibits two of the functions defined above, more preferably three of the functions defined above. Preparation of fusion protein The fusion protein may be prepared by any suitable method known to the person skilled in the art. Below are described several of the methods for preparing the fu¬sion protein, however the invention is not limited to those methods. Synthetic preparation When appropriate, in particular in relation to the size of the fusion protein, the fusion protein may be produced synthetically. The methods for synthetic production of pep¬tides are well known in art. Detailed descriptions as well as practical advice for pro¬ducing synthetic peptides may be found in Synthetic Peptides: A User's Guide (Ad¬vances in Molecular Biology), Grant G. A, ed„ Oxford University Press, 2002, or in: Pharmaceutical Formulation: Development of Peptides and Proteins, Frokjaer and Hovgaard eds., Taylor and Francis, 1999. Recombinant preparation The fusion proteins of the invention are preferably produced by use of recombinant DNA technologies. The.DNA sequence encoding each part of the fusion protein may be prepared by fragmentation of the DNA sequences encoding the full-length pro¬tein, (genomic DNA or cDNA) which the fusion protein part is derived from, using DNAase I according to a standard protocol (Sambrook et al.f Molecular cloning: A Laboratory manual. 2 rd ed„ CSHL Press, Cold Spring Harbor, NY, 1989). The ob¬tained DNA sequences encoding the individual parts of the fusion protein may then be fused together. The DNA sequence may also be prepared by polymerase chain reaction using spe¬cific primers, for instance as described in US 4,683,202 or Saiki et al., 1988, Sci¬ence 239:487-491. Thfe DNA sequence encoding a fusion protein of the invention may be prepared synthetically by established standard methods, e.g. the phosphoamidine method described by Beaucage and Caruthers, 1981, Tetrahedron Lett. 22:1859-1869, or the method described by Matthes et al., 1984, EMBO J. 3:801-805. According to the phosphoamidine method, oligonucleotides are synthesized, e.g. in an automatic DNA synthesizer, purified, annealed, ligated and cloned in suitable vectors. The DNA sequence is then inserted into a recombinant expression vector, which may be any vector, which may conveniently be subjected to recombinant DNA pro¬cedures. The choice of vector will often depend on the host cell into which it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vec¬tor that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated. In the vector, the DNA sequence encoding a fusion protein should be operably con¬nected to a suitable promoter sequence. The promoter may be any DNA sequence, which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell. Examples of suitable promoters for directing the transcription of the coding DNA sequence in mammalian cells are the SV 40 promoter (Subramani et al., 1981, Mol. Cell Biol. 1:854-864), the MT-1 (metallothionein gene) promoter (Palmiter et al., 1983, Science 222: 809-814) or the adenovirus 2 major late promoter. A suitable promoter for use in insect cells is the pofyhedrin promoter (Vasuvedan et al., 1992, FEBS Lett. 311:7-11), Suitable promoters for use in yeast host cells include promot¬ers from yeast glycolytic genes (Hitzeman et al., 1980, J. Biol. Chem. 255:12073-12080; Alber and Kawasaki, 1982, J. Mol. AppL Gen. 1: 419-434) or alcohol dehy¬drogenase genes (Young et al., 1982, in Genetic Engineering of Microorganisms for Chemicals, Hollaender et al, eds., Plenum Press, New York), or the TPI1 (US 4,599,311) or ADH2-4c (Russell et al., 1983, Nature 304:652-654) promoters. Suit¬able promoters for use in filamentous fungus host cells are, for instance, the ADH3 promoter (McKnight et al.', 1985, EMBO J. 4:2093-2099) or the tpiA promoter. The coding DNA sequence may also be operably connected to a suitable terminator, such as the human growth hormone terminator (Palmiter et aL, op. cit.) or (for fungal hosts) the TPI1 (Alber and Kawasaki, op. cit.) or ADH3 (McKnight et aL, op. cit.) promoters. The vector may further comprise elements such as polyadenylation sig¬nals (e.g. from SV 40 or the adenovirus 5 Elb region), transcriptional enhancer se¬quences (e.g. the SV 40 enhancer) and translational enhancer sequences (e.g. the ones encoding adenovirus VA RNAs). The recombinant expression vector may further comprise a DNA sequence enabling the vector to replicate in the host cell-in question. An example of such a sequence (when the host cell is a mammalian cell) is the SV 40 origin of replication. The vector may also comprise a selectable marker, e.g. a gene the product of which comple¬ments a defect in the host cell, such as the gene coding for dihydrofolate reductase (DHFR) or one which confers resistance to a drug, e.g. neomycin, hydromycin or methotrexate. The procedures used to ligate the DNA sequences coding the fusion proteins, the promoter and the terminator, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et aL, op.bit). ' The synthesis of the recombinant fusion protein may be by use of in vitro or in vivo cultures. The host cell culture is preferably an eucaryotic host cell culture. By trans-% formation of an eukaryotic cell culture is in this context meant introduction of recom¬binant DNA into the cells. The expression construct used in the process is charac¬terised by having the encoding region selected from mammalian genes including human genes and genes with big resemblance herewith such as the genes from the chimpanzee. The expression construct used is furthermore featured by the promoter region being selected from genes of virus or eukaryotes, including mammalian cells and cells from insects. The process for producing recombinant MBL according to the invention is charac¬terised in that the host cell culture is preferably eukaryotic, and for example a mam¬malian cell culture. A preferred host cell culture is a culture of human kidney cells and in an even more preferred form the host cell culture is a culture of human em- brybna! kidney cells (HEK cells), such as HEK 293 cell lines for production of re¬combinant human MBL. By "HEK 293 cell lines" is meant any cell line derived from human embryonal kidney tissue such as, but not limited to, the cell lines deposited at the American Type Culture Collection with the numbers CRL-1573 and CRL-10852. Other ceils may be chick embryo fibroblast; hamster ovary cells, baby hamster kid¬ney cells, human cervical carcinoma cells, human melanoma cells, human kidney cells, human umbilical vascular endothelium cells, human brain endothelium cells, human oral cavity tumor cells, monkey kidney cells, mouse fibroblast, mouse kidney cells, mouse connective tissue cells, mouse oligodendritic cells, mouse macro¬phage, mouse fibroblast, mouse neuroblastoma cells, mouse pre-B cell, mouse B lymphoma cells, mouse plasmacytoma cells, mouse teratocacinoma cells, rat astro¬cytoma cells, rat mammary epithelium cells, COS, CHO, BHK, VERO, HeLa, MDCK, WI38, and NIH 3T3 cells. Alternatively, fungal cells (including yeast cells) may be used as host cells. Exam¬ples of suitable yeast cells include cells of Saccharomyces spp. or Schizosaccharo-myces spp., in particular strains of Saccharomyces cerevisiae. Examples of other fungal cells are cells of filamentous fungi, e.g. Aspergillus spp. or Neurospora spp., in particular strains of Aspergillus oryzae or Aspergillus nigen The use of Aspergillus spp. for the expression of proteins is described in, e.g., EP 238 023. In addition, a host cell strain may be chosen which modulates the expression of the inserted sequences, or modifies and processes the gene product in the specific fashion desired. Such modifications (for example, glycosylation) and processing (for example, cleavage) of protein products may be important for the function of the protein. Different host cells have characteristic and specific mechanisms for the post-translational processing and modification of proteins and gene products., Ap¬propriate cell lines or host systems can be chosen to ensure the correct modification and processing of the foreign protein expressed. To this end, eukaryotic host cells which possess the cellular machinery for proper processing of the primary transcript, glycosylation, and phosphorylation of the gene product may be used. The mam¬malian cell types listed above are among those that could serve as suitable host cells. Methods of transfecting mammalian cells and expressing DNA sequences intro¬duced in the cells are described in e.g. Kaufman and Sharp, J. Mol. Biol. 159,1982, pp.'601-621; Southern and Berg, 1982, J. Mol. Appl. Genet 1:327-341; Loyter et al., 1982, Proc. Natl. Acad. Sci. USA 79: 422-426; Wigler et al., 1978, Cell 14:725; Cor-saro and Pearson, 1981, in Somatic Cell Genetics 7, p. 603; Graham and van der Eb, 1973, Virol. 52:456; and Neumann et al., 1982, EMBO J, 1:841-845. Other eucaryotic production systems are also envisaged by the present invention, such as the production of the fusion protein in a transgenic plant or animal. In another aspect the present invention provides a method for producing a fusion protein by - preparing a gene expression construct as defined above encoding a fusion protein, - transforming a host cell culture with the construct, - cultivating the host cell culture, thereby obtaining expression and secretion of the polypeptide into the culture medium, followed by obtaining a culture medium comprising recombinant fusion protein, and purifying the fusion protein. The medium used to culture the cells may be any conventional medium suitable for growing mammalian cells, such as a serum-containing or serum-free medium con¬taining appropriate supplements, or a suitable medium for growing insect, yeast or fungal cells. Suitable media are available from commercial suppliers or may be pre¬pared according to published recipes (e.g. in catalogues of the American Type Cul¬ture Collection). Example of culture medium are RPMI-1640 or DMEM supple¬mented with, e.g., insulin, transferrin, selenium, and foetal bovine serum The fusion proteins recombinantly produced by the cells may then be recovered from the culture medium by conventional procedures including separating the host cells from the medium by centrifugation or filtration, precipitating the'proteinaceous components of the supernatant or filtrate by means of a salt, e.g. ammonium sul¬phate, purification by a variety of chromatographic procedures, e.g. HPLC, ion ex¬change chromatography, affinity chromatography, or the like. In a preferred embodiment the fusion protein is purified by use of carbohydrate af¬finity chromatography as described above. In a preferred embodiment of the inven¬tion the affinity chromatography is performed by means of matrices of mannose, hexose or N-acetyl-glucoseamin derivatized matrices, which are suitable for affinity chromatography. In particular, an affinity chromatography is used, in which the ma¬trices have been derivatizised with mannose. Purified recombinant fusion protein is in this context to be understood as recombi¬nant fusion protein purified from cell culture supernatants or body fluids or tissue from transgenic animals purified by use of for example carbohydrate affinity cho-matography. After application of the culture media the column is washed, preferably by using non-denaturing buffers, having a composition, pH and ionic strength resulting in elimination of proteins, without eluting the fusion protein. Such a buffer may be TBS. Elution of fusion protein is performed with a selective desorbing agent, capable of efficient elution of fusion protein, such as TBS containing a desorbing agent, such as EDTA (5 mM for example) or mannose (50 mM for example), and fusion proteins are collected. Pharmaceutical composition and treatment The fusion protein obtained by the present invention may be used for the prepara¬tion of a pharmaceutical composition for the prevention and/or treatment of various diseases or conditions. In the present context the term pharmaceutical composition is used synonymously with the wording medicament. In addition to the fusion protein, the pharmaceutical.composition may comprise a pharmaceutical^ acceptable carrier substance and/or vehicles. In particular, a stabilising agent may be added to stabilise the fusion proteins. The stabilising agent may be a sugar alcohol, saccharide, protein and/or amino-acids. An example of a stabilising agent may be albumin or maltose. Other conventional additives may be added to the pharmaceutical composition de¬pending on administration form for example. In one embodiment the pharmaceutical composition is in a form suitable for injec¬tions. Conventional carrier substances,.such as isotonic saline, may be used. In another embodiment the pharmaceutical, composition is in a form suitable for pulmonal administration, such as in the form of a powder for inhalation or creme or fluid for topical application. A treatment in this context may comprise cure and/or prophylaxis of e.g. the immune system and reproductive system by humans and by animals having said functional units acting in this respect like those in humans. By conditions to be treated are not necessarily meant conditions presently known to be in a need of treatment, but comprise generally any condition in connection with current and/or expected need or in connection with an improvement of a normal condition. In particular, the treatment is a treatment of a condition of deficiency of lectins, such as MBL deficiency. In another aspect of the present invention the manufacture is provided of a medica¬ment consisting of said pharmaceutical compositions of fusion protein intended for treatment of conditions comprising cure and/or prophylaxis of conditions of diseases and disorders of e.g. the immune system and reproductive system by humans and by animals having said functional units acting like those in humans. Said diseases, disorders and/or conditions in need of treatment with the compounds of the invention comprise eg treatment of conditions of deficiency of MBL, treatment of cancer and of infections in connection with immunosuppressive chemotherapy including in particular those infections which are seen in connection with conditions during cancer treatment or in connection with implantation and/or transplantation of organs. The invention also comprises treatment of conditions in connection with recurrent miscarriage. Thus, in particular the pharmaceutical composition may be used for the treatment and/or prevention of clinical conditions selected from infections, MBL deficiency, cancer, .disorders associated with chemotherapy, such as infections, diseases asso¬ciated with human immunodeficiency virus (HIV), diseases related with congenital or acquired immunodeficiency. More particularly, chronic inflammatory demyelinating polyneuropathy (CIDP, Multifocal motoric neuropathy, Multiple scelrosis, Myasthenia Gravis, Eaton-LamberTs syndrome, Opticus Neuritis, Epilepsy; Primary antiphosho-iipid syndrome; Rheumatoid arthritis, Systemic Lupus erythematosus, Systemic scleroderma, Vasculitis, Wegner's granulomatosis, Sjogren's syndrome, Juvenile rheumatiod arthritis; Autoimmune neutropenia, Autoimmune haemolytic anaemia, Neutropenia; Crohn's disease, Colitis ulcerous, Coeliac disease; Asthma, Septic shock syndrome, Chronic fatigue syndrome, Psoriasis, Toxic shock syndrome, Dia¬betes, Sinuitis, Dilated cardiomyopathy, Endocarditis, Atherosclerosis, Primary hypo/agammaglobulinaemia including common variable immunodeficiency, Wiskot-Aldrich syndrome and serve combined immunodefiency (SCID), Secondary hypo/agammaglobulinaemia in patients with chronic lymphatic leukaemia (CLL) and multiple myeloma, Acute and chronic idiopathic thrombocytopenic purpura (ITP), Allogenic bone marrow transplantation (BTM), Kawasaki's disease, and Guillan-Barre's syndrome. The route of administration may be any suitable route, such as intravenously, intra-musculary, subcutanously or intradermally. Also, pulmonal or topical administration is envisaged by the present invention. In particular the fusion protein may be administered to prevent and/or treat infections in patients having clinical symptoms associated with congenital or acquired MBL deficiency or being at risk of developing such symptoms. A wide variety of condi¬tions may lead to increased susceptibility to infections in MBL-deficient individuals, such as chemotherapy or other therapeutic cell toxic treatments, cancer, AIDS, ge¬netic disposition, chronic infections, and neutropenia. The pharmaceutical composition may thus be administered for a period before the onset of administration of chemotherapy or the like and during at least a part of the chemotherapy. The fusion protein may be administered as a general "booster" before chemother¬apy, or it may be administered to those only being at risk of developing MBL defi¬ciency. The group of patients being at risk may be determined be measuring the MBL level before treatment and only subjecting those to treatment whose MBL level is below a predetermined level. The fusion protein is administered in suitable dosage regimes, in particularly it is usually administered at suitable intervals, eg. once or twice a week during chemo¬therapy. Normally from 1-100 mg is administered per dosage, such as from 2-10 mg, mostly from 5-10 mg per dosage. Mostly about 0.1 mg/kg body weight is administered. Furthermore, an aspect of the present invention is the use of a recombinant compo¬sition according to-the present invention in a kit-of-parts further comprising another medicament. In particular the other medicament may be an anti-microbial medica¬ment, such as antibiotics. Concerning miscarriage, it has been reported that the frequency of low plasma lev¬els of MBL is increased in patients with otherwise not explained recurrent miscar¬riages, which is the background for lowering of the susceptibility to miscarriage by a reconstitution of the MBL'level by administration of recombinant MBL in these cases. As to the nature of compounds of the invention, it appears, that in its broad aspect, the present invention relates to compounds which are able to act as opsonins, that is, able to enhance uptake by macrophages either through direct interaction be¬tween the compound and'the macrophage or through mediating complement depo¬sition on the target surface. Examples Example 1 Plasmidcloning of FCNMBL-M, -r2, -r3,-r4,-r5,-r6 and-r7. 1.1 Summary A series of plasmids were constructed for the expression in mammalian cells of protein fusions between recombinant human mannose-binding lectin" 2 gene (rhMBL) and human ficolin 2 (FCN2). The vector is derived from a high-copy-number ColEl-based plasmid and is designed to allow protein expression in mam¬malian systems. The fusion protein expressions are driven by the human cyto¬megalovirus (CMV) immediate early promoter to promote constitutive expression. Selection is made possible in bacteria by the ampiciliin-resistance gene under con¬trol of the prokaryotic p-lactamase promoter. The neomycin-resistance gene is driven by the SV40 early promoter, which provides stable selection with G418 in mammalian cells. 1.2 Constructs and experimental work In order to express fusion proteins between Ficolin2 and MBL we have designed and constructed a series of plasmids. The new recombinant plasmids are based on the previously cloned pcDNA2001-cintMBLcDNA. This plasmid contains a synthetic intron together with the cDNAfor human MBL. The following fusions were designed (underlined font indicates FCN2 part - italics indicate MBL part of the fusion protein.) FCN2MBLrt (SEQ ID NO:118V. FCN2 (signalseq+ collagen+'tiinge" to ficolin dom aa131) MBL (from aa129 carbo-hyd.bind dom.) MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCP-GLPGAPGDKGEAGTNGKRGERG PPGPPGKAGPPGPNGAPGEPQPCLTGPRTCKDLLDRGHFLSGWHTIYLPDCR-PLTFSLGKQVGNKFFLTNGEIMT FEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGN-RLTYTNWNEGEPNNAGSDEDC VLLLKHGQWNDVPCSTSHLAVCEFPI FCN2MBLr2 (SEQ ID NO: 119): FCN2 (signalseq+ collagen+"hinge"+part of ficolin-dom. containing pred. coil-coil to aa207) MBL (from aa129 carbohyd.bind dom.) MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCP-GLPGAPGDKGEAGTNGKRGERG PPGPPGKAGPPGPNGAPGEPQPCLTGPRTCKDLLDRGHFLSGWHTIYLPDCR-PLTVLCDMDTDGGGWTVFQRRVD ■GSVDFYRDWATYKQGFGSRLGEFWLGNDNIHALTAQGTSELRVDLVDFEDNY-Q FAKL TFSL GKQ VGNKFFL TNGE IMTFEKVKALCVKFQASVA TPRNAAENGAIQNLIKEEAFL GITDEKTEGQFVDL T-GNRLTYTNWNEGEPNNAGSD EDCVLLLKNGQWNDVPCS TSHLAVCEFPI FCN2MBLr3 (SEQ ID NO: 120): FCN2 (signalseq+ collagen to aa92) MBL (from aa101 coil-coil + carbohyd.bind dom.) MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCP-GLPGAPGDKGEAGTNGKRGERG PPGPPGKAGPPGPNGAPPDGDSSLAASERKALQTEMARIKKWLTFSLG-KQVGNKFFLTNGEIMTFEKVKALCVKF QASVATPRNAAENGAIQNUKEEAFLGITDEKTEGQFVDLTGNRLTYTN-WNEGEPNNAGSDEDCVLLLKNGQWND VPCSTSHLAVCEFPI FCN2MBLr4 (SEQ ID NO: 121): FCN2 (signalseq+ part of collagen to cons.K at aa_93) MBL (from cons.K at aa77 rest of collagen+coil-coil + carbohyd.bind dom.) MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCP-GLPGAPGDKGEAGTNGKRGERG PPGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMA-RIKKWLTFSLGKQVGNKFFLTNG EIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLT-GNRLTYTNWNEGEPNNAGS DEDCVLLLKNGQWNDVPCSTSHLAVCEFPI FCN2MBLr5 fSEQ ID NO: 122): FCN2 (signalseq+ part of collagen to cons.G at aa69) MBL (from cons.G at aa.64 rest of collagen(containing "kick")+coil-coil + carbohyd.bind dom.) MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCP-GLPGAPGDKGEAGTNGQGLflGL QGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMA-■ RIKKWLTFSLGKQVGNKFFLTNGE IMTFEKVKALCVKFQASVA TPRNAAENGAIQNUKEEAFLGITDEKTEGQFVDL T-GNRLTYTNWNEGEPNNAGSD EDCVLLLKNGQWNDVPCSTSHLAVCEFPI FCN2MBLr6 (SEQ ID NO: 123): MBL (replaced MBLcollagen(aa.41 to aa 99 )+coil-coil + carbohyd.bind dom.) FCN2 (inserted collagen aa.54 to aa.92) MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGCPGLPG/KPGDK-GEAGTNGKRGERGPPGPPGKAG PPGPNG/KPSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLT-NGEIMTFEKVKALCVKFQASVA TPR NAAENGAIQNLIKEEAFLGITDEKTEGQFVDL TGNRL TYTNWNEGEPNNA GSDED-CVLLLKNGQWNDVPCSTSHL AVCEFPI FCN2MBU7 (SEQ ID NO: 124): MBL (signal seq. to aa.25)FCN2 (collagen to aa93) MBL (from aa100 coil-coil + car¬bohyd.bind dom.) MS/.FPSLPLLLLSMW\/i\SySALQAADTCPEVKMVGLEGSDKLTILRGCPGLPGAP-GDKGEAGTNGKRGERGPPGP PGKAGPPGPHGAPSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKF-FLTNGEIMTFEKVKALCVKFQAS VA TPRNAAENGA1QNLIKEEAFLGITDEKTEGQFVDL TGNRL TYTNWNEGEPN-NAGSDEDCVLLLKNGQWNDVPC STSHLAVCEFPI Parental plasmids used for all constructions : • pcDNA2003-cintMBLcDNA • Invitrogen Genestorm cione RG000632 (Cat. No. H-K1000 Invitrogen). Constructions were done by recombination using the BD In-Fusion™ PCR Cloning Kit form BD (Cat. No. 631774). The BD in-Fusion Kit allows the cloning of PCR , products based only on 2 x 15 bp homology between vector and end of the PCR product. Ligase, or phosphatase are unnecessary when cloning with this kit. The ln-Fusion enzyme captures the DNA fragment ends and fuses the insert to the vector. Primers used for the PCR reactions are shown in table 1. PCR reactions and linearization of vector for recombination PCR reactions were done on plasmid "Genestorm RG000632" batch N135-15C di¬gested with Bstz17l (N135-20B). Primers pairs were used as described below. Kit for PCR reactions : PfuUltra™ Hotstart PCR Master Mix Stratagene #600630. The PCR reaction tubes were run on the BioRAD i-cycler using the temperature profile shown in table 2. For the recombination reactions the vector pcDNA2001-cintMBLcDNA was line¬arized by restriction enzyme digestion with the enzymes listed below. FCN2MBLr1: PCR using primers : Pr1-xho-MBLFCN + Pr4-Xmn-FCNMBL-rev (product 463 bp) Digest of pcDNA2001-cintMBLcDNA: Xhol + Xmnl (partial) FCN2MBLr2: PCR USING PRIMERS : Pr1-xho-MBLFCN + Pr5-Xmn-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA: Xhol + Xmnl (partial) FCN2MBLr3: PCR USING PRIMERS : Pr1-xho-MBLFCN + Pr6-b-Bsp-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA: Xhol + BspEl FCN2MBLr4: PCR USING PRIMERS : PrUxho-MBLFCN + Pr2-apa-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA: Xhol + Apal FCN2MBLr5: PCR USING PRIMERS : Pr1-xho-MBLFCN + Pr3-apa-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA : Xhol + Apal FCN2MBLr6. PCR USING PRIMERS : Pr8-BstAP-MBLFCN + Pr6-b-Bsp-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA: partial BstAPl + BspEI FCN2MBU7: PCR USING PRIMERS : Pr7-Alw-MBLFCN + Pr6-b-Bsp-FCNMBL-rev Digest of pcDNA2001-cintMBLcDNA :partial AlwNI + BspEI In-Fusion PCR recombination reactions In-Fusion PCR recombination reactions were set up using approx. 50-100 ng of Quiagen Minelute purified PCR products together with 50-100 ng of Quiagen Minelute purified linearized pcDNA2001-cintMBLcDNA . 1/10 of the recombination reactions were transformed into MAX efficiency DH5a Competent Cells (Invitrogen Cat. No. 18258-012). 1/10 and 9/10 from each trans¬formation were spread on separate LB plates containing 200 ug/ml ampicillin. Plates were incubated at 37°C overnight Screening for positive clones : At least 6 colonies from each experimental plate were picked for miniprep plasmid DNA isolation. To determine the presence of insert, DNA was analyzed by restriction digest analysis with the enzyme Pst\. Three indi¬vidual positive clones from each reaction were chosen for further work. Restriction Analysts In order to verify the selected individual recombinant plasmids after the primary screen we performed an intensive restriction enzyme digestion analysis on the plasmid DNA isolated. Plasmid DNA of the recombinants were digested with the enzyme shown in table 3. The expected fragments are also listed in the table. All recombinant clones tested exhibited the expected pattern. Digestion with EcoRI was not as predicted. An addi- tional fragment was observed both in digestion of the recombinant as well of the parental plasmid. The discrepancy can be explained by an additional EcoR1 site on the parental plasmid. Results Recombinant plasmids obtained are shown schematically in figures 4-8 for con¬structs r1, -r2, -r3,-r4, and -r5. Example 2 Experiments with transient expression of recombinant fusion proteins of hu¬man MBL and human FCN2 2.1 Summary We report the expression of recombinant human fusion proteins FCNMBUi, FCNMBLr4, FCNMBLr5 and MBL in HEK293 and Per.C6 cells. We found that the cell lines in the transient transfection experiment were able to produce at least the fusion proteins FCNMBLr4 and FCNMBLr5 assembled in active oligomeres with a structure primarly similar to MBL oligomer forms 3 and 4. The fusion proteins FCNMBLr4 and FCNMBLr5 behaved like MBL upon binding to a carbohydrate sur¬face and upon activating the complement cascade. 2.2 introduction The aim of the studies was to elucidate the possibility of creating a hybrid protein consisting of the collagen part of human ficoiin 2 and the human mannose binding lectin (MBL). Furthermore we wished to clarify if such molecules would still posses the ability to bind to complex carbohydrate structures and still are able to activate complement. Two eukaryotic cell lines of human origin HEK293 and Per.C6 were used as host cell lines for transient transfections with the respective expression plasmids. Tran¬scription was driven by.the*CMV-lE promoter enhancer. 2-3 Experimental Material and Methods Plasmids used for the transfection experiments pME607-FCNMBL-r1, -r2, -r3rr4;-r5,-r6 and-r7 (described in example 1) Origin of Cells used PerC6 cells were obtained from Crucell. HEK 293 Freestyle cells were obtained from InVitrogen . Culture media PerC6 ceils were cultured at 37°C in 10% (vol/vol) C02 maintained as monolayers in serum free medium. HEK 293 Freestyle were cultured at 37°C in 8% (vol/vol) C02 maintained as sus¬pension in an InVitrogen Freestyle medium. Transfections and harvest of media Per.C6 cells in serum containing medium were transfected with the DNA using the transfection reagent Lipofectamine. One day after transfection the medium was re¬placed with serum free medium. HEK293 cells in serum free Freestyle medium were transfected with the DNA using the transfection reagent 293fect. The medium was collected after approximately 4 days of incubation after transfection. Quantification of MBL Recombinant MBL assay (TRIFMA) using Mannan coated plates or mAb-131-01 coated plates. For quantification of MBL, time-resolved immunofiuorometry was car¬ried out. SDS-PAGE and Western blot analysis SDS-PAGE with subsequent electrophoretic transfer of proteins to polyvinylidene diflouride membranes and detection of MBL using monoclonal anti-MBL antibody was carried out C4 assay The assay is designed to measure MBL and rMBL abilities to initiate the MBL Lectin-pathway of the complement system. MBL associated serine protease (MASP 2) associated with MBL cleaves the complement factor C4 releasing C4a and C4b. The C4b deposition on the Manrian coated ELISA plates is detected with biotin la¬belled antibodies against C4b and Europium labelled Streptavidin. 2.4 RESULTS In the experiments described herein we were able to express FCN2MBLr4, FCN2MBLr5 and MBL transiently in both HEK293 and Per.C6 cells under serum free conditions. Oligomeric form of the fusion proteins The oligomeric forms of the fusion protein were examined by non-reducing denatur¬ing SDS PAGE followed by a western blot. The detecting antibody recognizes the CDR part of MBL (and maybe part of the coil-coil region). The results are shown in figure 10. It is evident from the figure that the most prominent form of the fusion proteins FCN2MBLr4 and FCN2MBLr5 is approximately 250 kDa corresponding to a 3- or 4-mere of subunits consisting of 3 single protein chains (24 kDa). The ap¬pearance of the oligomeric form was independent of the host cells used. MBL was produced in a wide range of oligomeric forms. Binding properties The fusion proteins were tested for functionality of the MBL carbohydrate binding domain by binding to a man nan surface and detection with an antibody that recog¬nizes the CDR part of MBL (and maybe part of the coil-coil region). The results are shown in table 4. It can be concluded that FCN2MBLr4 and FCN2MBLr5 were ex¬pressed just as well as MBL in the host cells and that the fusion proteins bind to a mannan surface. MASP-2 binding and C4 cleavge The fusion proteins were further tested for the capacity to bind MASP-2 and for acti¬vating the serine protease of MASP-2. This was done by measuring cleavage of the MASP-2 substrate complement factor C4 upon binding of the fusion protein to a mannan surface. Results are shown in table 5. It can be concluded from these re¬sults that the fusion proteins FCN2MBLr4 and FCN2MBLr5 preserved the ability to bind and activate MASP-2. Discussion The results described herein clearly demonstrate that it is possible to construct fu¬sion proteins of FCN 2 and MBL with the following properties; 1. The oligomeric structure of the fusion proteins is more simple than that of the MBL protein. 2. The fusion proteins keep the essential property of MBL activation of the comple¬ment cascade upon binding to a dense carbohydrate structure. Table 1. Primers used for the PCR reactions Sequence typed in bold shows the 15 bp homology needed for the recombina¬tion into the vector. WE CLAIM: 1. A fusion protein comprising i) A first polypeptide sequence derived from a lectin-complement pathway activating protein or a functional homologue at least 70% identical to said lectin-complement pathway activating protein, wherein said first polypeptide sequence is capable of activating the lectin-complement pathway: and ii) A second polypeptide sequence derived from a collectin, or a functional homologue at least 70% identical to said collectin, wherein said second polypeptide sequence is capable of associating with one or more carbohydrates; wherein said complement activating protein is not a collectin. 2. The fusion protein as claimed in claim 1, wherein said first polypeptide sequence is capable of associating with at least one MASP protein. 3. The fusion protein as claimed in claim 1, wherein said first polypeptide sequence is capable of associating with a MASP protein selected from the group consisting of MASP-1, MASP-2 and MASP-3 or functional homologues or variants hereof. 4. The fusion protein as claimed in claim 1, wherein the complement activating protein is a ficolin. 5. The fusion protein as claimed in claim 4, wherein the ficolin is selected from the group consisting of L-ficolin, H-ficolin and M-ficolin. 6. The fusion protein as claimed in claim 4, wherein the ficolin is L-ficolin. 7. The fusion protein as claimed in claim 1 wherein the first polypeptide sequence * comprises the collagen-like domain of a ficolin or a functional homologue or variant thereof. 8. The fusion protein as claimed in claim 1, wherein the first polypeptide sequence comprises the cysteine-rich region of a ficolin or a functional homologue thereof. 9. The fusion protein as claimed in claim 1, wherein the first polypeptide sequence comprises the cysteine-rich region and the collagen-like domain of a ficolin or a functional homologue or variant thereof. 10. The fusion protein as claimed in claim 1, wherein the first polypeptide sequence comprises amino acids 1-77 of the L-ficolin sequence of figure 1 (SEQ ID. NO 125). 11. The fusion protein as claimed in claim 1, wherein the collectin is selected from the group consisting of MBL (mannose-binding lectin), SP-A (lung surfactant protein A), SP-D (lung surfactant protein D), BK (or BC, bovine conglutinin) and CL-43 (collectin-43). 12. The fusion protein as claimed in claim 15, wherein the collectin is MBL. 13. The fusion protein as claimed in claim 1, wherein the second polypeptide sequence comprises the CRD domain of a collectin or a functional homologue or vaiant thereof. 14. The fusion protein as claimed in claim 1, wherein the second polypeptide sequence comprises the CRD domain of MBL. 15.* The fusion protein as claimed in claim 1, wherein the second polypeptide • sequence comprises the neck region of MBL. 16. The fusion protein as claimed in claim 1, wherein the second polypeptide sequence comprises the collagen-like domain of MBL. 17. The fusion protein as claimed in claim I, wherein the second polypeptide sequence comprises the neck region and the CRD domain of MBL. 18. The fusion protein as claimed in claim 1, wherein the second polypeptide sequence comprises the collagen-like domain, the neck region and the CRD domain do main of MBL. 19. The fusion protein as claimed in claim 1, wherein the second polypeptide sequence comprises amino acids 80-228 of the MBL sequence shown in figure 2 (SEQID.N0 126). 20. The fusion protein as claimed in claim 1, wherein the fusion protein comprises the cysteine-rich region and the collagen-like domain of L-ficolin and the CRD domain of MBL. 21. The fusion protein as claimed in claim 1, wherein the fusion protein comprises the cysteine-rich region of L-ficolin and the collagen-like domain, the neck region and the CRD domain of MBL. 22. The fusion protein as claimed in claim 1, wherein the fusion protein comprises the amino acid sequence as defined by the sequence shown in figure 3 (SEQ ID. NO. 127), or a functional homologue at least 70% identical thereto. 23. The fusion protein as claimed in claim 1, wherein the fusion protein consists of the amino acid sequence as defined by the sequence shown in figure 3 (SEQ ID. NO. 127). 24. An isolated nucleic acid comprising a nucleotide sequence encoding the fusion protein as claimed in any of claims 1 to 23. 25. A vector as herein described comprising the nucleic acid sequence as claimed in claim 24. 26. A microbial cell as herein described comprising the vector as claimed in claim 25. 27. A fusion protein as claimed in any of claims 1 to 23 for use as a medicament. 28. A medicament comprising the fusion protein as claimed in any of claims 1 to 23.

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