MASP1_HUMAN
ID MASP1_HUMAN Reviewed; 699 AA.
AC P48740; A8K542; A8K6M1; B4E2L7; O95570; Q68D21; Q8IUV8; Q96RS4; Q9UF09;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 206.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 protein-
RT associated serine protease light chain: comparison with complement C1r and
RT 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., Christensen T.,
RA Vorup-Jensen T., Jensenius J.C.;
RT "MASP-3 and its association with distinct complexes of the mannan-binding
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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, AND
RP 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)-associated
RT serine proteases-1 and -2, MBL-associated protein 19, and 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 two
RT 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., Reid K.B.M.,
RA 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, MBL-
RT associated serine proteases 1 and 2, and the MBL-associated protein
RT 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-associated
RT serine protease.";
RL J. Immunol. 165:2637-2642(2000).
RN [17]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=11527969; DOI=10.1074/jbc.m105934200;
RA Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C., Arlaud G.J.;
RT "Substrate specificities of recombinant mannan-binding lectin-associated
RT 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., 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., 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., Graf L.,
RA 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 fragments.";
RL J. Immunol. 170:1374-1382(2003).
RN [21]
RP CHARACTERIZATION (ISOFORM 2), MUTAGENESIS OF SER-646, AND AUTOCATALYTIC
RP CLEAVAGE.
RX PubMed=15034049; DOI=10.4049/jimmunol.172.7.4342;
RA Zundel S., Cseh S., Lacroix M., Dahl M.R., Matsushita M., Andrieu J.-P.,
RA Schwaeble W.J., Jensenius J.C., Fujita T., Arlaud G.J., Thielens N.M.;
RT "Characterization of recombinant mannan-binding lectin-associated serine
RT protease (MASP)-3 suggests an activation mechanism different from that of
RT 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 ASN-599
RP (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., Moore R.J.,
RA 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 convertase
RT 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., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT 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 with
RT 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 CALCIUM
RP IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDE BONDS,
RP CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2, AND
RP MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123; GLU-125;
RP HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 AND 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., Jenkins D.,
RA Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F., Bitner-Glindzicz M.,
RA Lees M., Hennekam R., Stanier P., Burns A.J., Peeters H., Alkuraya F.S.,
RA Beales P.L.;
RT "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC
RT 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., Mutlu G.Y.,
RA Bowdin S., Elcioglu N., Tayfun G.A., Atik S.S., Ozen M., Ozkinay F.,
RA Alanay Y., Kayserili H., Thiel S., Tekin M.;
RT "Novel MASP1 mutations are associated with an expanded phenotype in 3MC1
RT 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 performs
CC a key role in innate immunity by recognizing pathogens through patterns
CC of sugar moieties and neutralizing them. The lectin pathway is
CC triggered upon binding of mannan-binding lectin (MBL) and ficolins to
CC sugar moieties which leads to activation of the associated proteases
CC MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2
CC or C2 or directly activate C3 the key component of complement reaction.
CC Isoform 2 may have an inhibitory effect on the activation of the lectin
CC pathway of complement or may cleave IGFBP5. Also plays a role in
CC development (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, FCN2
CC and FCN3; triggers the lectin pathway of complement through activation
CC of C3. Interacts with SERPING1. Interacts with COLEC11; probably
CC triggers the lectin pathway of complement (PubMed:20956340).
CC {ECO:0000269|PubMed:10679061, ECO:0000269|PubMed:10878362,
CC ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11290788,
CC ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:12421953,
CC ECO:0000269|PubMed:18596036, ECO:0000269|PubMed:20956340,
CC ECO:0000269|PubMed:9087411}.
CC -!- INTERACTION:
CC P48740-1; O00187-1: MASP2; NbExp=8; IntAct=EBI-16138717, EBI-26357096;
CC P48740-1; P11226: MBL2; NbExp=9; IntAct=EBI-16138717, EBI-5325353;
CC P48740-2; Q15485: FCN2; NbExp=2; IntAct=EBI-26435098, EBI-7468784;
CC P48740-2; O75636: FCN3; NbExp=5; IntAct=EBI-26435098, EBI-11786958;
CC P48740-2; P48740-3: MASP1; NbExp=2; IntAct=EBI-26435098, EBI-26435118;
CC P48740-2; O00187-1: MASP2; NbExp=4; IntAct=EBI-26435098, EBI-26357096;
CC P48740-2; P11226: MBL2; NbExp=8; IntAct=EBI-26435098, EBI-5325353;
CC P48740-2; P23827: eco; Xeno; NbExp=3; IntAct=EBI-26435098, EBI-1029159;
CC P48740-3; O75636: FCN3; NbExp=3; IntAct=EBI-26435118, EBI-11786958;
CC P48740-3; P48740-3: MASP1; NbExp=3; IntAct=EBI-26435118, EBI-26435118;
CC P48740-3; O00187-1: MASP2; NbExp=7; IntAct=EBI-26435118, EBI-26357096;
CC P48740-3; P11226: MBL2; NbExp=7; IntAct=EBI-26435118, EBI-5325353;
CC PRO_0000027592; P11226: MBL2; NbExp=2; IntAct=EBI-26356151, 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 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 expressed
CC by liver. {ECO:0000269|PubMed:11485744, ECO:0000269|PubMed:8018603,
CC ECO:0000269|PubMed:8240317, ECO:0000269|PubMed:9367419}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Autoproteolytic processing of the proenzyme produces the active
CC enzyme composed on the heavy and the light chain held together by a
CC disulfide bond. Isoform 1 but not isoform 2 is activated through
CC autoproteolytic processing. {ECO:0000269|PubMed:11290788}.
CC -!- DISEASE: 3MC syndrome 1 (3MC1) [MIM:257920]: A form of 3MC syndrome, an
CC autosomal recessive disorder characterized by facial dysmorphism,
CC craniosynostosis, learning disability, and genital, limb and
CC vesicorenal anomalies. Facial features include hypertelorism,
CC blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip
CC and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli,
CC Malpuech, and Michels syndromes. {ECO:0000269|PubMed:21258343,
CC ECO:0000269|PubMed:26419238, ECO:0000269|PubMed:28301481}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 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 AlphaFoldDB; P48740; -.
DR SMR; P48740; -.
DR BioGRID; 111629; 24.
DR ComplexPortal; CPX-6170; MBL2-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6172; FCN1-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6178; FCN2-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6179; FCN3-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6181; CL-LK-MASP1 lectin-protease complex.
DR DIP; DIP-61382N; -.
DR IntAct; P48740; 33.
DR MINT; P48740; -.
DR BindingDB; P48740; -.
DR ChEMBL; CHEMBL4295768; -.
DR MEROPS; S01.132; -.
DR MEROPS; S01.198; -.
DR GlyConnect; 1488; 6 N-Linked glycans (3 sites).
DR GlyGen; P48740; 4 sites, 9 N-linked glycans (3 sites).
DR iPTMnet; P48740; -.
DR PhosphoSitePlus; P48740; -.
DR BioMuta; MASP1; -.
DR DMDM; 218512135; -.
DR CPTAC; non-CPTAC-2682; -.
DR jPOST; P48740; -.
DR MassIVE; P48740; -.
DR PeptideAtlas; P48740; -.
DR PRIDE; P48740; -.
DR ProteomicsDB; 55936; -. [P48740-1]
DR ProteomicsDB; 55937; -. [P48740-2]
DR ProteomicsDB; 55938; -. [P48740-3]
DR ProteomicsDB; 55939; -. [P48740-4]
DR TopDownProteomics; P48740-3; -. [P48740-3]
DR Antibodypedia; 889; 374 antibodies from 28 providers.
DR DNASU; 5648; -.
DR Ensembl; ENST00000169293.10; ENSP00000169293.6; ENSG00000127241.18. [P48740-3]
DR Ensembl; ENST00000296280.11; ENSP00000296280.7; ENSG00000127241.18. [P48740-2]
DR Ensembl; ENST00000337774.10; ENSP00000336792.5; ENSG00000127241.18. [P48740-1]
DR Ensembl; ENST00000392472.6; ENSP00000376264.2; ENSG00000127241.18. [P48740-4]
DR GeneID; 5648; -.
DR KEGG; hsa:5648; -.
DR MANE-Select; ENST00000296280.11; ENSP00000296280.7; NM_139125.4; NP_624302.1. [P48740-2]
DR UCSC; uc003frh.3; human. [P48740-1]
DR CTD; 5648; -.
DR DisGeNET; 5648; -.
DR GeneCards; MASP1; -.
DR HGNC; HGNC:6901; MASP1.
DR HPA; ENSG00000127241; Tissue enhanced (heart muscle, liver).
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 VEuPathDB; HostDB:ENSG00000127241; -.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; P48740; -.
DR OMA; RYSGFMA; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; P48740; -.
DR TreeFam; TF330373; -.
DR BRENDA; 3.4.21.B7; 2681.
DR PathwayCommons; P48740; -.
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 Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SABIO-RK; P48740; -.
DR SignaLink; P48740; -.
DR SIGNOR; P48740; -.
DR BioGRID-ORCS; 5648; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; MASP1; human.
DR EvolutionaryTrace; P48740; -.
DR GeneWiki; MASP1_(protein); -.
DR GenomeRNAi; 5648; -.
DR Pharos; P48740; Tchem.
DR PRO; PR:P48740; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P48740; protein.
DR Bgee; ENSG00000127241; Expressed in endocervix and 134 other tissues.
DR ExpressionAtlas; P48740; baseline and differential.
DR Genevisible; P48740; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
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:1905370; C:serine-type endopeptidase complex; IDA:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:ComplexPortal.
DR GO; GO:0045916; P:negative regulation of complement activation; IDA:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR DisProt; DP02816; -. [P48740-3]
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; Direct protein sequencing;
KW Disease variant; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase;
KW Hydroxylation; Immunity; Innate immunity; Metal-binding; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:11290788"
FT CHAIN 20..699
FT /note="Mannan-binding lectin serine protease 1"
FT /id="PRO_0000027592"
FT CHAIN 20..448
FT /note="Mannan-binding lectin serine protease 1 heavy chain"
FT /id="PRO_0000027593"
FT CHAIN 449..699
FT /note="Mannan-binding lectin serine protease 1 light chain"
FT /id="PRO_0000027594"
FT DOMAIN 20..138
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 139..182
FT /note="EGF-like; calcium-binding"
FT DOMAIN 185..297
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 299..364
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 365..434
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 449..696
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 20..278
FT /note="Interaction with FCN2"
FT REGION 20..184
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 20..184
FT /note="Interaction with MBL2"
FT ACT_SITE 490
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 552
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 646
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT SITE 448..449
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:11290788"
FT MOD_RES 159
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11290788,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:18596036, ECO:0000269|PubMed:19139490"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11290788,
FT ECO:0000269|PubMed:16335952"
FT DISULFID 73..91
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 143..157
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 153..166
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 168..181
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 185..212
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 242..260
FT /evidence="ECO:0000269|PubMed:18596036"
FT DISULFID 301..349
FT /evidence="ECO:0000250"
FT DISULFID 329..362
FT /evidence="ECO:0000250"
FT DISULFID 367..414
FT /evidence="ECO:0000250"
FT DISULFID 397..432
FT /evidence="ECO:0000250"
FT DISULFID 436..572
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 475..491
FT /evidence="ECO:0000250"
FT DISULFID 614..631
FT /evidence="ECO:0000250"
FT DISULFID 642..672
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036809"
FT VAR_SEQ 364..380
FT /note="IVDCRAPGELEHGLITF -> KNEIDLESELKSEQVTE (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_036810"
FT VAR_SEQ 381..699
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_036811"
FT VAR_SEQ 435
FT /note="V -> ECGQPSRSLPSLVKRIIGGRNAEPGLFPWQALIVVEDTSRVPNDKWF
FT GSGALLSASWILTAAHVLRSQRRDTTVIPVSKEHVTVYLGLHDVRDKSGAVNSSAARVV
FT LHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMLGLVAGWGISNPN
FT VTVDEIISSGTRTLSDVLQYVKLPVVPHAECKTSYESRSGNYSVTENMFCAGYYEGGKD
FT TCLGDSGGAFVIFDDLSQRWVVQGLVSWGGPEECGSKQVYGVYTKVSNYVDWVWEQMGL
FT PQSVVEPQVER (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11485744,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_036812"
FT VAR_SEQ 436..699
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11485744,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_036813"
FT VARIANT 3..699
FT /note="Missing (in 3MC1)"
FT /evidence="ECO:0000269|PubMed:28301481"
FT /id="VAR_078814"
FT VARIANT 21
FT /note="T -> I (in dbSNP:rs1062049)"
FT /id="VAR_051831"
FT VARIANT 568
FT /note="V -> A (in dbSNP:rs13322090)"
FT /id="VAR_051832"
FT VARIANT 679
FT /note="G -> R (in dbSNP:rs3774266)"
FT /id="VAR_051833"
FT MUTAGEN 68
FT /note="E->A,Q: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 77
FT /note="Y->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 99
FT /note="E->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 121
FT /note="D->A,N: Loss of interaction with FNC2 and FCN3 and
FT partial loss of interaction with MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 122
FT /note="F->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 123
FT /note="S->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 125
FT /note="E->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 237
FT /note="H->A: Loss of interaction with FCN2, FCN3 and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 239
FT /note="E->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 244
FT /note="Y->A: Loss of interaction with FCN2, FCN3 and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 262
FT /note="E->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 274
FT /note="S->A: Partial loss of interaction with FCN2 and
FT FCN3. No effect on interaction with MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 283
FT /note="N->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 286
FT /note="E->A: Partial loss of interaction with FCN2, FCN3
FT and MBL2."
FT /evidence="ECO:0000269|PubMed:18596036"
FT MUTAGEN 646
FT /note="S->A: No autoproteolytic processing."
FT /evidence="ECO:0000269|PubMed:15034049"
FT CONFLICT 2
FT /note="R -> K (in Ref. 6; BAF84375)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> A (in Ref. 7; CAH18409)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="F -> L (in Ref. 6; BAF84375)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> Q (in Ref. 2; BAA05928 and 3; BAA34864)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="G -> A (in Ref. 2; BAA05928, 3; BAA34864 and 4;
FT BAA89206)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="E -> G (in Ref. 6; BAF83846)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="E -> G (in Ref. 2; BAA05928)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="E -> K (in Ref. 1; BAA04477 and 4; BAA89206)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="D -> A (in Ref. 3; BAA34864)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="Q -> K (in Ref. 1; BAA04477)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="D -> V (in Ref. 3; BAA34864)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="A -> S (in Ref. 1; BAA04477)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3DEM"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:3DEM"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3DEM"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:3DEM"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:3DEM"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:4DJZ"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4DJZ"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 531..540
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 554..560
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:3GOV"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 602..609
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 611..618
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:4IGD"
FT TURN 655..658
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:4IGD"
FT STRAND 677..683
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 684..687
FT /evidence="ECO:0007829|PDB:4IGD"
FT HELIX 688..695
FT /evidence="ECO:0007829|PDB:4IGD"
FT CARBOHYD P48740-2:533
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD P48740-2:599
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VARIANT P48740-2:484
FT /note="G -> E (in 3MC1; dbSNP:rs759368047)"
FT /evidence="ECO:0000269|PubMed:26419238"
FT /id="VAR_082900"
FT VARIANT P48740-2:497
FT /note="H -> Y (in 3MC1; dbSNP:rs387906752)"
FT /evidence="ECO:0000269|PubMed:21258343"
FT /id="VAR_082901"
FT VARIANT P48740-2:553
FT /note="D -> N (in 3MC1; dbSNP:rs779329363)"
FT /evidence="ECO:0000269|PubMed:26419238"
FT /id="VAR_082902"
FT VARIANT P48740-2:630
FT /note="C -> R (in 3MC1; dbSNP:rs387906753)"
FT /evidence="ECO:0000269|PubMed:21258343"
FT /id="VAR_082903"
FT VARIANT P48740-2:663
FT /note="D -> Y (in 3MC1)"
FT /evidence="ECO:0000269|PubMed:26419238"
FT /id="VAR_082904"
FT VARIANT P48740-2:666
FT /note="G -> E (in 3MC1; dbSNP:rs387906754)"
FT /evidence="ECO:0000269|PubMed:21258343"
FT /id="VAR_082905"
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
