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Database: UniProt
Entry: P48740
LinkDB: P48740
Original site: P48740 
ID   MASP1_HUMAN             Reviewed;         699 AA.
AC   P48740; A8K542; A8K6M1; B4E2L7; O95570; Q68D21; Q8IUV8; Q96RS4;
AC   Q9UF09;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 3.
DT   10-APR-2019, entry version 188.
DE   RecName: Full=Mannan-binding lectin serine protease 1;
DE            EC=3.4.21.-;
DE   AltName: Full=Complement factor MASP-3;
DE   AltName: Full=Complement-activating component of Ra-reactive factor;
DE   AltName: Full=Mannose-binding lectin-associated serine protease 1;
DE            Short=MASP-1;
DE   AltName: Full=Mannose-binding protein-associated serine protease;
DE   AltName: Full=Ra-reactive factor serine protease p100;
DE            Short=RaRF;
DE   AltName: Full=Serine protease 5;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
DE   Contains:
DE     RecName: Full=Mannan-binding lectin serine protease 1 light chain;
DE   Flags: Precursor;
GN   Name=MASP1; Synonyms=CRARF, CRARF1, PRSS5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=8240317; DOI=10.1006/bbrc.1993.2349;
RA   Takada F., Takayama Y., Hatsuse H., Kawakami M.;
RT   "A new member of the C1s family of complement proteins found in a
RT   bactericidal factor, Ra-reactive factor, in human serum.";
RL   Biochem. Biophys. Res. Commun. 196:1003-1009(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal liver;
RX   PubMed=8018603; DOI=10.1093/intimm/6.4.665;
RA   Sato T., Endo Y., Matsushita M., Fujita T.;
RT   "Molecular characterization of a novel serine protease involved in
RT   activation of the complement system by mannose-binding protein.";
RL   Int. Immunol. 6:665-669(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=8921412; DOI=10.1093/intimm/8.9.1355;
RA   Endo Y., Sato T., Matsushita M., Fujita T.;
RT   "Exon structure of the gene encoding the human mannose-binding
RT   protein-associated serine protease light chain: comparison with
RT   complement C1r and C1s genes.";
RL   Int. Immunol. 8:1355-1358(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10475605; DOI=10.1016/S0161-5890(99)00070-X;
RA   Takayama Y., Takada F., Nowatari M., Kawakami M., Matsu-ura N.;
RT   "Gene structure of the P100 serine-protease component of the human Ra-
RT   reactive factor.";
RL   Mol. Immunol. 36:505-514(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 450-474;
RP   506-526; 539-555; 577-590; 613-621 AND 679-695 (ISOFORM 2), FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=11485744; DOI=10.1016/S1074-7613(01)00161-3;
RA   Dahl M.R., Thiel S., Matsushita M., Fujita T., Willis A.C.,
RA   Christensen T., Vorup-Jensen T., Jensenius J.C.;
RT   "MASP-3 and its association with distinct complexes of the mannan-
RT   binding lectin complement activation pathway.";
RL   Immunity 15:127-135(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   TISSUE=Placenta, Teratocarcinoma, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Fetal brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 20-29 AND 449-458, SIGNAL SEQUENCE CLEAVAGE SITE,
RP   AUTOCATALYTIC CLEAVAGE AT ARG-448, GLYCOSYLATION, HOMODIMERIZATION,
RP   AND INTERACTION WITH MBL2.
RX   PubMed=11290788; DOI=10.4049/jimmunol.166.8.5068;
RA   Thielens N.M., Cseh S., Thiel S., Vorup-Jensen T., Rossi V.,
RA   Jensenius J.C., Arlaud G.J.;
RT   "Interaction properties of human mannan-binding lectin (MBL)-
RT   associated serine proteases-1 and -2, MBL-associated protein 19, and
RT   MBL.";
RL   J. Immunol. 166:5068-5077(2001).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=9367419; DOI=10.1111/j.1365-2249.1997.tb08334.x;
RA   Terai I., Kobayashi K., Matsushita M., Fujita T.;
RT   "Human serum mannose-binding lectin (MBL)-associated serine protease-1
RT   (MASP-1): determination of levels in body fluids and identification of
RT   two forms in serum.";
RL   Clin. Exp. Immunol. 110:317-323(1997).
RN   [13]
RP   INTERACTION WITH MBL2.
RC   TISSUE=Liver;
RX   PubMed=9087411; DOI=10.1038/386506a0;
RA   Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W.J., Laursen S.B.,
RA   Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U.,
RA   Reid K.B.M., Jensenius J.C.;
RT   "A second serine protease associated with mannan-binding lectin that
RT   activates complement.";
RL   Nature 386:506-510(1997).
RN   [14]
RP   INTERACTION WITH FCN2.
RX   PubMed=10679061; DOI=10.4049/jimmunol.164.5.2281;
RA   Matsushita M., Endo Y., Fujita T.;
RT   "Complement-activating complex of ficolin and mannose-binding lectin-
RT   associated serine protease.";
RL   J. Immunol. 164:2281-2284(2000).
RN   [15]
RP   INTERACTION WITH MBL2.
RX   PubMed=10878362; DOI=10.4049/jimmunol.165.2.878;
RA   Thiel S., Petersen S.V., Vorup-Jensen T., Matsushita M., Fujita T.,
RA   Stover C.M., Schwaeble W.J., Jensenius J.C.;
RT   "Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s,
RT   MBL-associated serine proteases 1 and 2, and the MBL-associated
RT   protein MAp19.";
RL   J. Immunol. 165:878-887(2000).
RN   [16]
RP   CATALYTIC ACTIVITY, AND INTERACTION WITH SERPING1.
RX   PubMed=10946292; DOI=10.4049/jimmunol.165.5.2637;
RA   Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.;
RT   "Proteolytic activities of two types of mannose-binding lectin-
RT   associated serine protease.";
RL   J. Immunol. 165:2637-2642(2000).
RN   [17]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=11527969; DOI=10.1074/jbc.M105934200;
RA   Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C.,
RA   Arlaud G.J.;
RT   "Substrate specificities of recombinant mannan-binding lectin-
RT   associated serine proteases-1 and -2.";
RL   J. Biol. Chem. 276:40880-40887(2001).
RN   [18]
RP   INTERACTION WITH FCN3.
RX   PubMed=11907111; DOI=10.4049/jimmunol.168.7.3502;
RA   Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H.,
RA   Fujita T.;
RT   "Activation of the lectin complement pathway by H-ficolin (Hakata
RT   antigen).";
RL   J. Immunol. 168:3502-3506(2002).
RN   [19]
RP   INTERACTION WITH FCN2.
RX   PubMed=12421953; DOI=10.4049/jimmunol.169.10.5735;
RA   Cseh S., Vera L., Matsushita M., Fujita T., Arlaud G.J.,
RA   Thielens N.M.;
RT   "Characterization of the interaction between L-ficolin/p35 and mannan-
RT   binding lectin-associated serine proteases-1 and -2.";
RL   J. Immunol. 169:5735-5743(2002).
RN   [20]
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12538697; DOI=10.4049/jimmunol.170.3.1374;
RA   Ambrus G., Gal P., Kojima M., Szilagyi K., Balczer J., Antal J.,
RA   Graf L., Laich A., Moffatt B.E., Schwaeble W., Sim R.B., Zavodszky P.;
RT   "Natural substrates and inhibitors of mannan-binding lectin-associated
RT   serine protease-1 and -2: a study on recombinant catalytic
RT   fragments.";
RL   J. Immunol. 170:1374-1382(2003).
RN   [21]
RP   CHARACTERIZATION (ISOFORM 2), MUTAGENESIS OF SER-646, AND
RP   AUTOCATALYTIC CLEAVAGE.
RX   PubMed=15034049; DOI=10.4049/jimmunol.172.7.4342;
RA   Zundel S., Cseh S., Lacroix M., Dahl M.R., Matsushita M.,
RA   Andrieu J.-P., Schwaeble W.J., Jensenius J.C., Fujita T., Arlaud G.J.,
RA   Thielens N.M.;
RT   "Characterization of recombinant mannan-binding lectin-associated
RT   serine protease (MASP)-3 suggests an activation mechanism different
RT   from that of MASP-1 and MASP-2.";
RL   J. Immunol. 172:4342-4350(2004).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-178; ASN-385 AND
RP   ASN-407, AND GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-533 AND
RP   ASN-599 (ISOFORM 2).
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [23]
RP   CATALYTIC ACTIVITY (ISOFORM 2).
RX   PubMed=16554018; DOI=10.1016/j.abb.2006.02.006;
RA   Cortesio C.L., Jiang W.;
RT   "Mannan-binding lectin-associated serine protease 3 cleaves synthetic
RT   peptides and insulin-like growth factor-binding protein 5.";
RL   Arch. Biochem. Biophys. 449:164-170(2006).
RN   [24]
RP   FUNCTION (ISOFORMS 1 AND 2).
RX   PubMed=17182967; DOI=10.1093/intimm/dxl131;
RA   Moeller-Kristensen M., Thiel S., Sjoeholm A., Matsushita M.,
RA   Jensenius J.C.;
RT   "Cooperation between MASP-1 and MASP-2 in the generation of C3
RT   convertase through the MBL pathway.";
RL   Int. Immunol. 19:141-149(2007).
RN   [25]
RP   GLYCOSYLATION AT ASN-178 AND ASN-385.
RX   PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA   Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA   Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core
RT   fucosylated glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [26]
RP   INTERACTION WITH COLEC11.
RX   PubMed=20956340; DOI=10.4049/jimmunol.1002185;
RA   Hansen S., Selman L., Palaniyar N., Ziegler K., Brandt J., Kliem A.,
RA   Jonasson M., Skjoedt M.O., Nielsen O., Hartshorn K., Joergensen T.J.,
RA   Skjoedt K., Holmskov U.;
RT   "Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin
RT   with microbial-binding activity.";
RL   J. Immunol. 185:6096-6104(2010).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-295 IN COMPLEX WITH
RP   CALCIUM IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDE
RP   BONDS, CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2,
RP   AND MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123;
RP   GLU-125; HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 AND
RP   GLU-286.
RX   PubMed=18596036; DOI=10.1074/jbc.M803551200;
RA   Teillet F., Gaboriaud C., Lacroix M., Martin L., Arlaud G.J.,
RA   Thielens N.M.;
RT   "Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and
RT   identification of its interaction sites with mannan-binding lectin and
RT   ficolins.";
RL   J. Biol. Chem. 283:25715-25724(2008).
RN   [28]
RP   VARIANTS 3MC1 TYR-497; ARG-630 AND GLU-666 (ISOFORM 2), INVOLVEMENT IN
RP   3MC1, AND FUNCTION.
RX   PubMed=21258343; DOI=10.1038/ng.757;
RA   Rooryck C., Diaz-Font A., Osborn D.P., Chabchoub E.,
RA   Hernandez-Hernandez V., Shamseldin H., Kenny J., Waters A.,
RA   Jenkins D., Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F.,
RA   Bitner-Glindzicz M., Lees M., Hennekam R., Stanier P., Burns A.J.,
RA   Peeters H., Alkuraya F.S., Beales P.L.;
RT   "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause
RT   3MC syndrome.";
RL   Nat. Genet. 43:197-203(2011).
RN   [29]
RP   VARIANTS 3MC1 GLU-484; ASN-553 AND TYR-663 (ISOFORM 2).
RX   PubMed=26419238; DOI=10.1186/s13023-015-0345-3;
RA   Atik T., Koparir A., Bademci G., Foster J. II, Altunoglu U.,
RA   Mutlu G.Y., Bowdin S., Elcioglu N., Tayfun G.A., Atik S.S., Ozen M.,
RA   Ozkinay F., Alanay Y., Kayserili H., Thiel S., Tekin M.;
RT   "Novel MASP1 mutations are associated with an expanded phenotype in
RT   3MC1 syndrome.";
RL   Orphanet J. Rare Dis. 10:128-128(2015).
RN   [30]
RP   VARIANT 3MC1 3-TRP--ASN-699 DEL.
RX   PubMed=28301481; DOI=10.1371/journal.pgen.1006679;
RA   Munye M.M., Diaz-Font A., Ocaka L., Henriksen M.L., Lees M., Brady A.,
RA   Jenkins D., Morton J., Hansen S.W., Bacchelli C., Beales P.L.,
RA   Hernandez-Hernandez V.;
RT   "COLEC10 is mutated in 3MC patients and regulates early craniofacial
RT   development.";
RL   PLoS Genet. 13:E1006679-E1006679(2017).
CC   -!- FUNCTION: Functions in the lectin pathway of complement, which
CC       performs a key role in innate immunity by recognizing pathogens
CC       through patterns of sugar moieties and neutralizing them. The
CC       lectin pathway is triggered upon binding of mannan-binding lectin
CC       (MBL) and ficolins to sugar moieties which leads to activation of
CC       the associated proteases MASP1 and MASP2. Functions as an
CC       endopeptidase and may activate MASP2 or C2 or directly activate C3
CC       the key component of complement reaction. Isoform 2 may have an
CC       inhibitory effect on the activation of the lectin pathway of
CC       complement or may cleave IGFBP5. Also plays a role in development
CC       (PubMed:21258343). {ECO:0000269|PubMed:11485744,
CC       ECO:0000269|PubMed:21258343}.
CC   -!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M.
CC       {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
CC         KM=310 uM for Bz-Arg-OEt (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
CC         KM=4.8 uM for C2 (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
CC   -!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2,
CC       FCN2 and FCN3; triggers the lectin pathway of complement through
CC       activation of C3. Interacts with SERPING1. Interacts with COLEC11;
CC       probably triggers the lectin pathway of complement
CC       (PubMed:20956340). {ECO:0000269|PubMed:10679061,
CC       ECO:0000269|PubMed:10878362, ECO:0000269|PubMed:10946292,
CC       ECO:0000269|PubMed:11290788, ECO:0000269|PubMed:11907111,
CC       ECO:0000269|PubMed:12421953, ECO:0000269|PubMed:18596036,
CC       ECO:0000269|PubMed:20956340, ECO:0000269|PubMed:9087411}.
CC   -!- INTERACTION:
CC       P11226:MBL2; NbExp=3; IntAct=EBI-16138717, EBI-5325353;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11485744}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P48740-1; Sequence=Displayed;
CC       Name=2; Synonyms=MASP-3;
CC         IsoId=P48740-2; Sequence=VSP_036812, VSP_036813;
CC         Note=Contains a N-linked (GlcNAc...) asparagine at position 533
CC         (PubMed:16335952). Contains a N-linked (GlcNAc...) asparagine at
CC         position 599 (PubMed:16335952). Variant in position: 497:H->Y
CC         (in 3MC1) (PubMed:21258343). Variant in position: 630:C->R (in
CC         3MC1) (PubMed:21258343). Variant in position: 666:G->E (in 3MC1)
CC         (PubMed:21258343). Variant in position: 484:G->E (in 3MC1)
CC         (PubMed:26419238). Variant in position: 553:D->N (in 3MC1)
CC         (PubMed:26419238). Variant in position: 663:D->Y (in 3MC1)
CC         (PubMed:26419238). {ECO:0000269|PubMed:16335952,
CC         ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:26419238};
CC       Name=3;
CC         IsoId=P48740-3; Sequence=VSP_036810, VSP_036811;
CC       Name=4;
CC         IsoId=P48740-4; Sequence=VSP_036809, VSP_036812, VSP_036813;
CC   -!- TISSUE SPECIFICITY: Protein of the plasma which is primarily
CC       expressed by liver. {ECO:0000269|PubMed:11485744,
CC       ECO:0000269|PubMed:8018603, ECO:0000269|PubMed:8240317,
CC       ECO:0000269|PubMed:9367419}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Autoproteolytic processing of the proenzyme produces the
CC       active enzyme composed on the heavy and the light chain held
CC       together by a disulfide bond. Isoform 1 but not isoform 2 is
CC       activated through autoproteolytic processing.
CC       {ECO:0000269|PubMed:11290788}.
CC   -!- DISEASE: 3MC syndrome 1 (3MC1) [MIM:257920]: A form of 3MC
CC       syndrome, an autosomal recessive disorder characterized by facial
CC       dysmorphism, craniosynostosis, learning disability, and genital,
CC       limb and vesicorenal anomalies. Facial features include
CC       hypertelorism, blepharophimosis, blepharoptosis and highly arched
CC       eyebrows, cleft lip and/or palate. The term 3MC syndrome includes
CC       Carnevale, Mingarelli, Malpuech, and Michels syndromes.
CC       {ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:26419238,
CC       ECO:0000269|PubMed:28301481}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39724.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; D17525; BAA04477.1; -; mRNA.
DR   EMBL; D28593; BAA05928.1; -; mRNA.
DR   EMBL; D61695; BAA34864.1; -; Genomic_DNA.
DR   EMBL; AB007617; BAA89206.1; -; Genomic_DNA.
DR   EMBL; AF284421; AAK84071.1; -; mRNA.
DR   EMBL; AK291157; BAF83846.1; -; mRNA.
DR   EMBL; AK291686; BAF84375.1; -; mRNA.
DR   EMBL; AK304334; BAG65179.1; -; mRNA.
DR   EMBL; CR749615; CAH18409.1; -; mRNA.
DR   EMBL; AC007920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78153.1; -; Genomic_DNA.
DR   EMBL; BC039724; AAH39724.1; ALT_INIT; mRNA.
DR   EMBL; BC106945; AAI06946.1; -; mRNA.
DR   EMBL; BC106946; AAI06947.1; -; mRNA.
DR   CCDS; CCDS33907.1; -. [P48740-1]
DR   CCDS; CCDS33908.1; -. [P48740-2]
DR   CCDS; CCDS33909.1; -. [P48740-3]
DR   PIR; I54763; I54763.
DR   RefSeq; NP_001027019.1; NM_001031849.2. [P48740-3]
DR   RefSeq; NP_001870.3; NM_001879.5. [P48740-1]
DR   RefSeq; NP_624302.1; NM_139125.3. [P48740-2]
DR   RefSeq; XP_016862361.1; XM_017006872.1. [P48740-4]
DR   UniGene; Hs.89983; -.
DR   PDB; 3DEM; X-ray; 2.30 A; A/B=20-297.
DR   PDB; 3GOV; X-ray; 2.55 A; A=298-448, B=449-699.
DR   PDB; 4AQB; X-ray; 4.20 A; A=20-363.
DR   PDB; 4DJZ; X-ray; 3.20 A; A/C=298-448, B/D=449-699.
DR   PDB; 4IGD; X-ray; 2.50 A; A=298-699.
DR   PDB; 4IW4; X-ray; 3.20 A; E/F=625-696.
DR   PDB; 4KKD; X-ray; 2.60 A; A/B=298-696.
DR   PDBsum; 3DEM; -.
DR   PDBsum; 3GOV; -.
DR   PDBsum; 4AQB; -.
DR   PDBsum; 4DJZ; -.
DR   PDBsum; 4IGD; -.
DR   PDBsum; 4IW4; -.
DR   PDBsum; 4KKD; -.
DR   ProteinModelPortal; P48740; -.
DR   SMR; P48740; -.
DR   BioGrid; 111629; 21.
DR   DIP; DIP-61382N; -.
DR   IntAct; P48740; 18.
DR   MINT; P48740; -.
DR   MEROPS; S01.132; -.
DR   GlyConnect; 1488; -.
DR   iPTMnet; P48740; -.
DR   PhosphoSitePlus; P48740; -.
DR   BioMuta; MASP1; -.
DR   DMDM; 218512135; -.
DR   jPOST; P48740; -.
DR   PeptideAtlas; P48740; -.
DR   PRIDE; P48740; -.
DR   ProteomicsDB; 55936; -.
DR   ProteomicsDB; 55937; -. [P48740-2]
DR   ProteomicsDB; 55938; -. [P48740-3]
DR   ProteomicsDB; 55939; -. [P48740-4]
DR   TopDownProteomics; P48740-3; -. [P48740-3]
DR   Ensembl; ENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
DR   Ensembl; ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
DR   Ensembl; ENST00000337774; ENSP00000336792; ENSG00000127241. [P48740-1]
DR   Ensembl; ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
DR   GeneID; 5648; -.
DR   KEGG; hsa:5648; -.
DR   UCSC; uc003frh.3; human. [P48740-1]
DR   CTD; 5648; -.
DR   DisGeNET; 5648; -.
DR   EuPathDB; HostDB:ENSG00000127241.16; -.
DR   GeneCards; MASP1; -.
DR   HGNC; HGNC:6901; MASP1.
DR   HPA; HPA001617; -.
DR   HPA; HPA009641; -.
DR   MalaCards; MASP1; -.
DR   MIM; 257920; phenotype.
DR   MIM; 600521; gene.
DR   neXtProt; NX_P48740; -.
DR   OpenTargets; ENSG00000127241; -.
DR   Orphanet; 293843; 3MC syndrome.
DR   PharmGKB; PA30644; -.
DR   GeneTree; ENSGT00950000183084; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; P48740; -.
DR   KO; K03992; -.
DR   OMA; DLSQRWV; -.
DR   OrthoDB; 156878at2759; -.
DR   PhylomeDB; P48740; -.
DR   TreeFam; TF330373; -.
DR   BRENDA; 3.4.21.B7; 2681.
DR   Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR   Reactome; R-HSA-166663; Initial triggering of complement.
DR   Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR   Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR   SABIO-RK; P48740; -.
DR   ChiTaRS; MASP1; human.
DR   EvolutionaryTrace; P48740; -.
DR   GeneWiki; MASP1_(protein); -.
DR   GenomeRNAi; 5648; -.
DR   PRO; PR:P48740; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000127241; Expressed in 161 organ(s), highest expression level in ectocervix.
DR   ExpressionAtlas; P48740; baseline and differential.
DR   Genevisible; P48740; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006956; P:complement activation; TAS:Reactome.
DR   GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
DR   GO; GO:0045916; P:negative regulation of complement activation; IDA:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autocatalytic cleavage; Calcium;
KW   Complement activation lectin pathway; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immunity;
KW   Innate immunity; Metal-binding; Polymorphism; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:11290788}.
FT   CHAIN        20    699       Mannan-binding lectin serine protease 1.
FT                                /FTId=PRO_0000027592.
FT   CHAIN        20    448       Mannan-binding lectin serine protease 1
FT                                heavy chain.
FT                                /FTId=PRO_0000027593.
FT   CHAIN       449    699       Mannan-binding lectin serine protease 1
FT                                light chain.
FT                                /FTId=PRO_0000027594.
FT   DOMAIN       20    138       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      139    182       EGF-like; calcium-binding.
FT   DOMAIN      185    297       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      299    364       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      365    434       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      449    696       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION       20    278       Interaction with FCN2.
FT   REGION       20    184       Homodimerization. {ECO:0000250}.
FT   REGION       20    184       Interaction with MBL2.
FT   ACT_SITE    490    490       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    552    552       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    646    646       Charge relay system. {ECO:0000250}.
FT   METAL        68     68       Calcium 1.
FT   METAL        76     76       Calcium 1.
FT   METAL       121    121       Calcium 1.
FT   METAL       123    123       Calcium 1; via carbonyl oxygen.
FT   METAL       139    139       Calcium 2.
FT   METAL       140    140       Calcium 2; via carbonyl oxygen.
FT   METAL       142    142       Calcium 2.
FT   METAL       159    159       Calcium 2.
FT   METAL       160    160       Calcium 2; via carbonyl oxygen.
FT   METAL       163    163       Calcium 2; via carbonyl oxygen.
FT   METAL       235    235       Calcium 3.
FT   METAL       245    245       Calcium 3.
FT   METAL       282    282       Calcium 3.
FT   METAL       284    284       Calcium 3; via carbonyl oxygen.
FT   SITE        448    449       Cleavage; by autolysis.
FT                                {ECO:0000269|PubMed:11290788}.
FT   MOD_RES     159    159       (3R)-3-hydroxyasparagine. {ECO:0000255}.
FT   CARBOHYD     49     49       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:11290788,
FT                                ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:18596036,
FT                                ECO:0000269|PubMed:19139490}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:11290788,
FT                                ECO:0000269|PubMed:16335952}.
FT   DISULFID     73     91       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    143    157       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    153    166       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    168    181       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    185    212       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    242    260       {ECO:0000269|PubMed:18596036}.
FT   DISULFID    301    349       {ECO:0000250}.
FT   DISULFID    329    362       {ECO:0000250}.
FT   DISULFID    367    414       {ECO:0000250}.
FT   DISULFID    397    432       {ECO:0000250}.
FT   DISULFID    436    572       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DISULFID    475    491       {ECO:0000250}.
FT   DISULFID    614    631       {ECO:0000250}.
FT   DISULFID    642    672       {ECO:0000250}.
FT   VAR_SEQ       1    113       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_036809.
FT   VAR_SEQ     364    380       IVDCRAPGELEHGLITF -> KNEIDLESELKSEQVTE
FT                                (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_036810.
FT   VAR_SEQ     381    699       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_036811.
FT   VAR_SEQ     435    435       V -> ECGQPSRSLPSLVKRIIGGRNAEPGLFPWQALIVVE
FT                                DTSRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTTVIPV
FT                                SKEHVTVYLGLHDVRDKSGAVNSSAARVVLHPDFNIQNYNH
FT                                DIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMLGLVAGW
FT                                GISNPNVTVDEIISSGTRTLSDVLQYVKLPVVPHAECKTSY
FT                                ESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDLS
FT                                QRWVVQGLVSWGGPEECGSKQVYGVYTKVSNYVDWVWEQMG
FT                                LPQSVVEPQVER (in isoform 2 and isoform
FT                                4). {ECO:0000303|PubMed:11485744,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_036812.
FT   VAR_SEQ     436    699       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:11485744,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_036813.
FT   VARIANT       3    699       Missing (in 3MC1).
FT                                {ECO:0000269|PubMed:28301481}.
FT                                /FTId=VAR_078814.
FT   VARIANT      21     21       T -> I (in dbSNP:rs1062049).
FT                                /FTId=VAR_051831.
FT   VARIANT     568    568       V -> A (in dbSNP:rs13322090).
FT                                /FTId=VAR_051832.
FT   VARIANT     679    679       G -> R (in dbSNP:rs3774266).
FT                                /FTId=VAR_051833.
FT   MUTAGEN      68     68       E->A,Q: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN      77     77       Y->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN      99     99       E->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     121    121       D->A,N: Loss of interaction with FNC2 and
FT                                FCN3 and partial loss of interaction with
FT                                MBL2. {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     122    122       F->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     123    123       S->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     125    125       E->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     237    237       H->A: Loss of interaction with FCN2, FCN3
FT                                and MBL2. {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     239    239       E->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     244    244       Y->A: Loss of interaction with FCN2, FCN3
FT                                and MBL2. {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     262    262       E->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     274    274       S->A: Partial loss of interaction with
FT                                FCN2 and FCN3. No effect on interaction
FT                                with MBL2. {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     283    283       N->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     286    286       E->A: Partial loss of interaction with
FT                                FCN2, FCN3 and MBL2.
FT                                {ECO:0000269|PubMed:18596036}.
FT   MUTAGEN     646    646       S->A: No autoproteolytic processing.
FT                                {ECO:0000269|PubMed:15034049}.
FT   CONFLICT      2      2       R -> K (in Ref. 6; BAF84375).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       T -> A (in Ref. 7; CAH18409).
FT                                {ECO:0000305}.
FT   CONFLICT    232    232       F -> L (in Ref. 6; BAF84375).
FT                                {ECO:0000305}.
FT   CONFLICT    235    235       E -> Q (in Ref. 2; BAA05928 and 3;
FT                                BAA34864). {ECO:0000305}.
FT   CONFLICT    285    285       G -> A (in Ref. 2; BAA05928, 3; BAA34864
FT                                and 4; BAA89206). {ECO:0000305}.
FT   CONFLICT    392    392       E -> G (in Ref. 6; BAF83846).
FT                                {ECO:0000305}.
FT   CONFLICT    499    499       E -> G (in Ref. 2; BAA05928).
FT                                {ECO:0000305}.
FT   CONFLICT    499    499       E -> K (in Ref. 1; BAA04477 and 4;
FT                                BAA89206). {ECO:0000305}.
FT   CONFLICT    527    527       D -> A (in Ref. 3; BAA34864).
FT                                {ECO:0000305}.
FT   CONFLICT    543    543       Q -> K (in Ref. 1; BAA04477).
FT                                {ECO:0000305}.
FT   CONFLICT    552    552       D -> V (in Ref. 3; BAA34864).
FT                                {ECO:0000305}.
FT   CONFLICT    643    643       A -> S (in Ref. 1; BAA04477).
FT                                {ECO:0000305}.
FT   STRAND       28     32       {ECO:0000244|PDB:3DEM}.
FT   TURN         34     37       {ECO:0000244|PDB:3DEM}.
FT   STRAND       42     51       {ECO:0000244|PDB:3DEM}.
FT   STRAND       56     66       {ECO:0000244|PDB:3DEM}.
FT   HELIX        71     73       {ECO:0000244|PDB:3DEM}.
FT   STRAND       75     81       {ECO:0000244|PDB:3DEM}.
FT   STRAND       86     90       {ECO:0000244|PDB:3DEM}.
FT   STRAND       92     99       {ECO:0000244|PDB:3DEM}.
FT   STRAND      110    120       {ECO:0000244|PDB:3DEM}.
FT   STRAND      130    139       {ECO:0000244|PDB:3DEM}.
FT   TURN        142    144       {ECO:0000244|PDB:3DEM}.
FT   STRAND      154    160       {ECO:0000244|PDB:3DEM}.
FT   STRAND      163    167       {ECO:0000244|PDB:3DEM}.
FT   STRAND      192    199       {ECO:0000244|PDB:3DEM}.
FT   TURN        200    203       {ECO:0000244|PDB:3DEM}.
FT   STRAND      211    217       {ECO:0000244|PDB:3DEM}.
FT   STRAND      223    228       {ECO:0000244|PDB:3DEM}.
FT   STRAND      238    244       {ECO:0000244|PDB:3DEM}.
FT   STRAND      246    251       {ECO:0000244|PDB:3DEM}.
FT   STRAND      254    259       {ECO:0000244|PDB:3DEM}.
FT   STRAND      261    263       {ECO:0000244|PDB:3DEM}.
FT   STRAND      273    280       {ECO:0000244|PDB:3DEM}.
FT   STRAND      291    297       {ECO:0000244|PDB:3DEM}.
FT   STRAND      310    314       {ECO:0000244|PDB:4IGD}.
FT   STRAND      317    320       {ECO:0000244|PDB:4IGD}.
FT   STRAND      324    329       {ECO:0000244|PDB:4IGD}.
FT   STRAND      333    337       {ECO:0000244|PDB:4IGD}.
FT   STRAND      340    349       {ECO:0000244|PDB:4IGD}.
FT   STRAND      355    357       {ECO:0000244|PDB:4IGD}.
FT   STRAND      361    364       {ECO:0000244|PDB:4IGD}.
FT   STRAND      376    382       {ECO:0000244|PDB:4IGD}.
FT   STRAND      392    397       {ECO:0000244|PDB:4IGD}.
FT   TURN        399    401       {ECO:0000244|PDB:4IGD}.
FT   STRAND      402    404       {ECO:0000244|PDB:4IGD}.
FT   HELIX       405    407       {ECO:0000244|PDB:4IGD}.
FT   STRAND      411    414       {ECO:0000244|PDB:4IGD}.
FT   TURN        416    418       {ECO:0000244|PDB:4DJZ}.
FT   STRAND      420    422       {ECO:0000244|PDB:4IGD}.
FT   TURN        423    425       {ECO:0000244|PDB:4IGD}.
FT   STRAND      426    428       {ECO:0000244|PDB:4DJZ}.
FT   STRAND      432    434       {ECO:0000244|PDB:4IGD}.
FT   STRAND      463    468       {ECO:0000244|PDB:4IGD}.
FT   STRAND      473    480       {ECO:0000244|PDB:4IGD}.
FT   TURN        481    483       {ECO:0000244|PDB:4IGD}.
FT   STRAND      484    487       {ECO:0000244|PDB:4IGD}.
FT   HELIX       489    491       {ECO:0000244|PDB:4IGD}.
FT   TURN        505    507       {ECO:0000244|PDB:4IGD}.
FT   TURN        511    513       {ECO:0000244|PDB:4IGD}.
FT   STRAND      514    519       {ECO:0000244|PDB:4IGD}.
FT   STRAND      522    525       {ECO:0000244|PDB:4IGD}.
FT   STRAND      531    540       {ECO:0000244|PDB:4IGD}.
FT   TURN        546    549       {ECO:0000244|PDB:4IGD}.
FT   STRAND      554    560       {ECO:0000244|PDB:4IGD}.
FT   STRAND      565    567       {ECO:0000244|PDB:3GOV}.
FT   STRAND      583    591       {ECO:0000244|PDB:4IGD}.
FT   STRAND      594    596       {ECO:0000244|PDB:4IGD}.
FT   STRAND      602    609       {ECO:0000244|PDB:4IGD}.
FT   HELIX       611    618       {ECO:0000244|PDB:4IGD}.
FT   HELIX       619    621       {ECO:0000244|PDB:4IGD}.
FT   STRAND      629    632       {ECO:0000244|PDB:4IGD}.
FT   STRAND      649    654       {ECO:0000244|PDB:4IGD}.
FT   TURN        655    658       {ECO:0000244|PDB:4IGD}.
FT   STRAND      659    666       {ECO:0000244|PDB:4IGD}.
FT   HELIX       672    675       {ECO:0000244|PDB:4IGD}.
FT   STRAND      677    683       {ECO:0000244|PDB:4IGD}.
FT   HELIX       684    687       {ECO:0000244|PDB:4IGD}.
FT   HELIX       688    695       {ECO:0000244|PDB:4IGD}.
SQ   SEQUENCE   699 AA;  79247 MW;  5B37C7FB9F51FD1D CRC64;
     MRWLLLYYAL CFSLSKASAH TVELNNMFGQ IQSPGYPDSY PSDSEVTWNI TVPDGFRIKL
     YFMHFNLESS YLCEYDYVKV ETEDQVLATF CGRETTDTEQ TPGQEVVLSP GSFMSITFRS
     DFSNEERFTG FDAHYMAVDV DECKEREDEE LSCDHYCHNY IGGYYCSCRF GYILHTDNRT
     CRVECSDNLF TQRTGVITSP DFPNPYPKSS ECLYTIELEE GFMVNLQFED IFDIEDHPEV
     PCPYDYIKIK VGPKVLGPFC GEKAPEPIST QSHSVLILFH SDNSGENRGW RLSYRAAGNE
     CPELQPPVHG KIEPSQAKYF FKDQVLVSCD TGYKVLKDNV EMDTFQIECL KDGTWSNKIP
     TCKIVDCRAP GELEHGLITF STRNNLTTYK SEIKYSCQEP YYKMLNNNTG IYTCSAQGVW
     MNKVLGRSLP TCLPVCGLPK FSRKLMARIF NGRPAQKGTT PWIAMLSHLN GQPFCGGSLL
     GSSWIVTAAH CLHQSLDPED PTLRDSDLLS PSDFKIILGK HWRLRSDENE QHLGVKHTTL
     HPQYDPNTFE NDVALVELLE SPVLNAFVMP ICLPEGPQQE GAMVIVSGWG KQFLQRFPET
     LMEIEIPIVD HSTCQKAYAP LKKKVTRDMI CAGEKEGGKD ACAGDSGGPM VTLNRERGQW
     YLVGTVSWGD DCGKKDRYGV YSYIHHNKDW IQRVTGVRN
//
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