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Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]

 MASP1_HUMAN             Reviewed;         699 AA.
P48740; A8K542; A8K6M1; B4E2L7; O95570; Q68D21; Q8IUV8; Q96RS4;
Q9UF09;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 3.
25-APR-2018, entry version 180.
RecName: Full=Mannan-binding lectin serine protease 1;
EC=3.4.21.-;
AltName: Full=Complement factor MASP-3;
AltName: Full=Complement-activating component of Ra-reactive factor;
AltName: Full=Mannose-binding lectin-associated serine protease 1;
Short=MASP-1;
AltName: Full=Mannose-binding protein-associated serine protease;
AltName: Full=Ra-reactive factor serine protease p100;
Short=RaRF;
AltName: Full=Serine protease 5;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
Contains:
RecName: Full=Mannan-binding lectin serine protease 1 light chain;
Flags: Precursor;
Name=MASP1; Synonyms=CRARF, CRARF1, PRSS5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=8240317; DOI=10.1006/bbrc.1993.2349;
Takada F., Takayama Y., Hatsuse H., Kawakami M.;
"A new member of the C1s family of complement proteins found in a
bactericidal factor, Ra-reactive factor, in human serum.";
Biochem. Biophys. Res. Commun. 196:1003-1009(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Fetal liver;
PubMed=8018603; DOI=10.1093/intimm/6.4.665;
Sato T., Endo Y., Matsushita M., Fujita T.;
"Molecular characterization of a novel serine protease involved in
activation of the complement system by mannose-binding protein.";
Int. Immunol. 6:665-669(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8921412; DOI=10.1093/intimm/8.9.1355;
Endo Y., Sato T., Matsushita M., Fujita T.;
"Exon structure of the gene encoding the human mannose-binding
protein-associated serine protease light chain: comparison with
complement C1r and C1s genes.";
Int. Immunol. 8:1355-1358(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10475605; DOI=10.1016/S0161-5890(99)00070-X;
Takayama Y., Takada F., Nowatari M., Kawakami M., Matsu-ura N.;
"Gene structure of the P100 serine-protease component of the human Ra-
reactive factor.";
Mol. Immunol. 36:505-514(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 450-474;
506-526; 539-555; 577-590; 613-621 AND 679-695 (ISOFORM 2), FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11485744; DOI=10.1016/S1074-7613(01)00161-3;
Dahl M.R., Thiel S., Matsushita M., Fujita T., Willis A.C.,
Christensen T., Vorup-Jensen T., Jensenius J.C.;
"MASP-3 and its association with distinct complexes of the mannan-
binding lectin complement activation pathway.";
Immunity 15:127-135(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Placenta, Teratocarcinoma, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Fetal brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 20-29 AND 449-458, SIGNAL SEQUENCE CLEAVAGE SITE,
AUTOCATALYTIC CLEAVAGE AT ARG-448, GLYCOSYLATION, HOMODIMERIZATION,
AND INTERACTION WITH MBL2.
PubMed=11290788; DOI=10.4049/jimmunol.166.8.5068;
Thielens N.M., Cseh S., Thiel S., Vorup-Jensen T., Rossi V.,
Jensenius J.C., Arlaud G.J.;
"Interaction properties of human mannan-binding lectin (MBL)-
associated serine proteases-1 and -2, MBL-associated protein 19, and
MBL.";
J. Immunol. 166:5068-5077(2001).
[12]
TISSUE SPECIFICITY.
PubMed=9367419; DOI=10.1111/j.1365-2249.1997.tb08334.x;
Terai I., Kobayashi K., Matsushita M., Fujita T.;
"Human serum mannose-binding lectin (MBL)-associated serine protease-1
(MASP-1): determination of levels in body fluids and identification of
two forms in serum.";
Clin. Exp. Immunol. 110:317-323(1997).
[13]
INTERACTION WITH MBL2.
TISSUE=Liver;
PubMed=9087411; DOI=10.1038/386506a0;
Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W.J., Laursen S.B.,
Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U.,
Reid K.B.M., Jensenius J.C.;
"A second serine protease associated with mannan-binding lectin that
activates complement.";
Nature 386:506-510(1997).
[14]
INTERACTION WITH FCN2.
PubMed=10679061; DOI=10.4049/jimmunol.164.5.2281;
Matsushita M., Endo Y., Fujita T.;
"Complement-activating complex of ficolin and mannose-binding lectin-
associated serine protease.";
J. Immunol. 164:2281-2284(2000).
[15]
INTERACTION WITH MBL2.
PubMed=10878362; DOI=10.4049/jimmunol.165.2.878;
Thiel S., Petersen S.V., Vorup-Jensen T., Matsushita M., Fujita T.,
Stover C.M., Schwaeble W.J., Jensenius J.C.;
"Interaction of C1q and mannan-binding lectin (MBL) with C1r, C1s,
MBL-associated serine proteases 1 and 2, and the MBL-associated
protein MAp19.";
J. Immunol. 165:878-887(2000).
[16]
CATALYTIC ACTIVITY, AND INTERACTION WITH SERPING1.
PubMed=10946292; DOI=10.4049/jimmunol.165.5.2637;
Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.;
"Proteolytic activities of two types of mannose-binding lectin-
associated serine protease.";
J. Immunol. 165:2637-2642(2000).
[17]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
REGULATION.
PubMed=11527969; DOI=10.1074/jbc.M105934200;
Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C.,
Arlaud G.J.;
"Substrate specificities of recombinant mannan-binding lectin-
associated serine proteases-1 and -2.";
J. Biol. Chem. 276:40880-40887(2001).
[18]
INTERACTION WITH FCN3.
PubMed=11907111; DOI=10.4049/jimmunol.168.7.3502;
Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H.,
Fujita T.;
"Activation of the lectin complement pathway by H-ficolin (Hakata
antigen).";
J. Immunol. 168:3502-3506(2002).
[19]
INTERACTION WITH FCN2.
PubMed=12421953; DOI=10.4049/jimmunol.169.10.5735;
Cseh S., Vera L., Matsushita M., Fujita T., Arlaud G.J.,
Thielens N.M.;
"Characterization of the interaction between L-ficolin/p35 and mannan-
binding lectin-associated serine proteases-1 and -2.";
J. Immunol. 169:5735-5743(2002).
[20]
ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12538697; DOI=10.4049/jimmunol.170.3.1374;
Ambrus G., Gal P., Kojima M., Szilagyi K., Balczer J., Antal J.,
Graf L., Laich A., Moffatt B.E., Schwaeble W., Sim R.B., Zavodszky P.;
"Natural substrates and inhibitors of mannan-binding lectin-associated
serine protease-1 and -2: a study on recombinant catalytic
fragments.";
J. Immunol. 170:1374-1382(2003).
[21]
CHARACTERIZATION (ISOFORM 2), MUTAGENESIS OF SER-646, AND
AUTOCATALYTIC CLEAVAGE.
PubMed=15034049; DOI=10.4049/jimmunol.172.7.4342;
Zundel S., Cseh S., Lacroix M., Dahl M.R., Matsushita M.,
Andrieu J.-P., Schwaeble W.J., Jensenius J.C., Fujita T., Arlaud G.J.,
Thielens N.M.;
"Characterization of recombinant mannan-binding lectin-associated
serine protease (MASP)-3 suggests an activation mechanism different
from that of MASP-1 and MASP-2.";
J. Immunol. 172:4342-4350(2004).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-178; ASN-385 AND
ASN-407, AND GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-533 AND
ASN-599 (ISOFORM 2).
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[23]
CATALYTIC ACTIVITY (ISOFORM 2).
PubMed=16554018; DOI=10.1016/j.abb.2006.02.006;
Cortesio C.L., Jiang W.;
"Mannan-binding lectin-associated serine protease 3 cleaves synthetic
peptides and insulin-like growth factor-binding protein 5.";
Arch. Biochem. Biophys. 449:164-170(2006).
[24]
FUNCTION (ISOFORMS 1 AND 2).
PubMed=17182967; DOI=10.1093/intimm/dxl131;
Moeller-Kristensen M., Thiel S., Sjoeholm A., Matsushita M.,
Jensenius J.C.;
"Cooperation between MASP-1 and MASP-2 in the generation of C3
convertase through the MBL pathway.";
Int. Immunol. 19:141-149(2007).
[25]
GLYCOSYLATION AT ASN-178 AND ASN-385.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[26]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-295 IN COMPLEX WITH
CALCIUM IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDE
BONDS, CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2,
AND MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123;
GLU-125; HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 AND
GLU-286.
PubMed=18596036; DOI=10.1074/jbc.M803551200;
Teillet F., Gaboriaud C., Lacroix M., Martin L., Arlaud G.J.,
Thielens N.M.;
"Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and
identification of its interaction sites with mannan-binding lectin and
ficolins.";
J. Biol. Chem. 283:25715-25724(2008).
[27]
VARIANTS 3MC1 TYR-497; ARG-630 AND GLU-666 (ISOFORM 2), AND
INVOLVEMENT IN 3MC1.
PubMed=21258343; DOI=10.1038/ng.757;
Rooryck C., Diaz-Font A., Osborn D.P., Chabchoub E.,
Hernandez-Hernandez V., Shamseldin H., Kenny J., Waters A.,
Jenkins D., Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F.,
Bitner-Glindzicz M., Lees M., Hennekam R., Stanier P., Burns A.J.,
Peeters H., Alkuraya F.S., Beales P.L.;
"Mutations in lectin complement pathway genes COLEC11 and MASP1 cause
3MC syndrome.";
Nat. Genet. 43:197-203(2011).
[28]
VARIANTS 3MC1 GLU-484; ASN-553 AND TYR-663 (ISOFORM 2).
PubMed=26419238; DOI=10.1186/s13023-015-0345-3;
Atik T., Koparir A., Bademci G., Foster J. II, Altunoglu U.,
Mutlu G.Y., Bowdin S., Elcioglu N., Tayfun G.A., Atik S.S., Ozen M.,
Ozkinay F., Alanay Y., Kayserili H., Thiel S., Tekin M.;
"Novel MASP1 mutations are associated with an expanded phenotype in
3MC1 syndrome.";
Orphanet J. Rare Dis. 10:128-128(2015).
[29]
VARIANT 3MC1 3-TRP--ASN-699 DEL.
PubMed=28301481; DOI=10.1371/journal.pgen.1006679;
Munye M.M., Diaz-Font A., Ocaka L., Henriksen M.L., Lees M., Brady A.,
Jenkins D., Morton J., Hansen S.W., Bacchelli C., Beales P.L.,
Hernandez-Hernandez V.;
"COLEC10 is mutated in 3MC patients and regulates early craniofacial
development.";
PLoS Genet. 13:E1006679-E1006679(2017).
-!- FUNCTION: Functions in the lectin pathway of complement, which
performs a key role in innate immunity by recognizing pathogens
through patterns of sugar moieties and neutralizing them. The
lectin pathway is triggered upon binding of mannan-binding lectin
(MBL) and ficolins to sugar moieties which leads to activation of
the associated proteases MASP1 and MASP2. Functions as an
endopeptidase and may activate MASP2 or C2 or directly activate C3
the key component of complement reaction. Isoform 2 may have an
inhibitory effect on the activation of the lectin pathway of
complement or may cleave IGFBP5. {ECO:0000269|PubMed:11485744}.
-!- ENZYME REGULATION: Inhibited by SERPING1 and A2M.
{ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius)
{ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
KM=310 uM for Bz-Arg-OEt (at 30 degrees Celsius)
{ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
KM=4.8 uM for C2 (at 37 degrees Celsius)
{ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697};
-!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2,
FCN2 and FCN3; triggers the lectin pathway of complement through
activation of C3. Interacts with SERPING1.
{ECO:0000269|PubMed:10679061, ECO:0000269|PubMed:10878362,
ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11290788,
ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:12421953,
ECO:0000269|PubMed:18596036, ECO:0000269|PubMed:9087411}.
-!- INTERACTION:
P11226:MBL2; NbExp=3; IntAct=EBI-16138717, EBI-5325353;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11485744}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P48740-1; Sequence=Displayed;
Name=2; Synonyms=MASP-3;
IsoId=P48740-2; Sequence=VSP_036812, VSP_036813;
Note=Contains a N-linked (GlcNAc...) asparagine at position 533
(PubMed:16335952). Contains a N-linked (GlcNAc...) asparagine at
position 599 (PubMed:16335952). Variant in position: 497:H->Y
(in 3MC1) (PubMed:21258343). Variant in position: 630:C->R (in
3MC1) (PubMed:21258343). Variant in position: 666:G->E (in 3MC1)
(PubMed:21258343). Variant in position: 484:G->E (in 3MC1)
(PubMed:26419238). Variant in position: 553:D->N (in 3MC1)
(PubMed:26419238). Variant in position: 663:D->Y (in 3MC1)
(PubMed:26419238). {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:26419238};
Name=3;
IsoId=P48740-3; Sequence=VSP_036810, VSP_036811;
Name=4;
IsoId=P48740-4; Sequence=VSP_036809, VSP_036812, VSP_036813;
-!- TISSUE SPECIFICITY: Protein of the plasma which is primarily
expressed by liver. {ECO:0000269|PubMed:11485744,
ECO:0000269|PubMed:8018603, ECO:0000269|PubMed:8240317,
ECO:0000269|PubMed:9367419}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type
(By similarity). {ECO:0000250}.
-!- PTM: Autoproteolytic processing of the proenzyme produces the
active enzyme composed on the heavy and the light chain held
together by a disulfide bond. Isoform 1 but not isoform 2 is
activated through autoproteolytic processing.
{ECO:0000269|PubMed:11290788}.
-!- DISEASE: 3MC syndrome 1 (3MC1) [MIM:257920]: A form of 3MC
syndrome, an autosomal recessive disorder characterized by facial
dysmorphism, craniosynostosis, learning disability, and genital,
limb and vesicorenal anomalies. Facial features include
hypertelorism, blepharophimosis, blepharoptosis and highly arched
eyebrows, cleft lip and/or palate. The term 3MC syndrome includes
Carnevale, Mingarelli, Malpuech, and Michels syndromes.
{ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:26419238,
ECO:0000269|PubMed:28301481}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAH39724.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D17525; BAA04477.1; -; mRNA.
EMBL; D28593; BAA05928.1; -; mRNA.
EMBL; D61695; BAA34864.1; -; Genomic_DNA.
EMBL; AB007617; BAA89206.1; -; Genomic_DNA.
EMBL; AF284421; AAK84071.1; -; mRNA.
EMBL; AK291157; BAF83846.1; -; mRNA.
EMBL; AK291686; BAF84375.1; -; mRNA.
EMBL; AK304334; BAG65179.1; -; mRNA.
EMBL; CR749615; CAH18409.1; -; mRNA.
EMBL; AC007920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78153.1; -; Genomic_DNA.
EMBL; BC039724; AAH39724.1; ALT_INIT; mRNA.
EMBL; BC106945; AAI06946.1; -; mRNA.
EMBL; BC106946; AAI06947.1; -; mRNA.
CCDS; CCDS33907.1; -. [P48740-1]
CCDS; CCDS33908.1; -. [P48740-2]
CCDS; CCDS33909.1; -. [P48740-3]
PIR; I54763; I54763.
RefSeq; NP_001027019.1; NM_001031849.2. [P48740-3]
RefSeq; NP_001870.3; NM_001879.5. [P48740-1]
RefSeq; NP_624302.1; NM_139125.3. [P48740-2]
RefSeq; XP_016862361.1; XM_017006872.1. [P48740-4]
UniGene; Hs.89983; -.
PDB; 3DEM; X-ray; 2.30 A; A/B=20-297.
PDB; 3GOV; X-ray; 2.55 A; A=298-448, B=449-699.
PDB; 4AQB; X-ray; 4.20 A; A=20-363.
PDB; 4DJZ; X-ray; 3.20 A; A/C=298-448, B/D=449-699.
PDB; 4IGD; X-ray; 2.50 A; A=298-699.
PDB; 4IW4; X-ray; 3.20 A; E/F=625-696.
PDB; 4KKD; X-ray; 2.60 A; A/B=298-696.
PDBsum; 3DEM; -.
PDBsum; 3GOV; -.
PDBsum; 4AQB; -.
PDBsum; 4DJZ; -.
PDBsum; 4IGD; -.
PDBsum; 4IW4; -.
PDBsum; 4KKD; -.
ProteinModelPortal; P48740; -.
SMR; P48740; -.
BioGrid; 111629; 21.
DIP; DIP-61382N; -.
IntAct; P48740; 18.
MINT; P48740; -.
MEROPS; S01.132; -.
iPTMnet; P48740; -.
PhosphoSitePlus; P48740; -.
BioMuta; MASP1; -.
DMDM; 218512135; -.
PeptideAtlas; P48740; -.
PRIDE; P48740; -.
TopDownProteomics; P48740-3; -. [P48740-3]
Ensembl; ENST00000169293; ENSP00000169293; ENSG00000127241. [P48740-3]
Ensembl; ENST00000296280; ENSP00000296280; ENSG00000127241. [P48740-2]
Ensembl; ENST00000337774; ENSP00000336792; ENSG00000127241. [P48740-1]
Ensembl; ENST00000392472; ENSP00000376264; ENSG00000127241. [P48740-4]
GeneID; 5648; -.
KEGG; hsa:5648; -.
UCSC; uc003frh.3; human. [P48740-1]
CTD; 5648; -.
DisGeNET; 5648; -.
EuPathDB; HostDB:ENSG00000127241.16; -.
GeneCards; MASP1; -.
HGNC; HGNC:6901; MASP1.
HPA; HPA001617; -.
HPA; HPA009641; -.
MalaCards; MASP1; -.
MIM; 257920; phenotype.
MIM; 600521; gene.
neXtProt; NX_P48740; -.
OpenTargets; ENSG00000127241; -.
Orphanet; 293843; Craniofacial-ulnar-renal syndrome.
PharmGKB; PA30644; -.
GeneTree; ENSGT00760000118890; -.
HOVERGEN; HBG000559; -.
InParanoid; P48740; -.
KO; K03992; -.
OMA; DLSQRWV; -.
OrthoDB; EOG091G02DS; -.
PhylomeDB; P48740; -.
TreeFam; TF330373; -.
BRENDA; 3.4.21.B7; 2681.
Reactome; R-HSA-166662; Lectin pathway of complement activation.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
SABIO-RK; P48740; -.
ChiTaRS; MASP1; human.
EvolutionaryTrace; P48740; -.
GeneWiki; MASP1_(protein); -.
GenomeRNAi; 5648; -.
PMAP-CutDB; Q96RS4; -.
PRO; PR:P48740; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000127241; -.
CleanEx; HS_MASP1; -.
ExpressionAtlas; P48740; baseline and differential.
Genevisible; P48740; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
GO; GO:0045916; P:negative regulation of complement activation; IDA:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
CDD; cd00033; CCP; 2.
CDD; cd00041; CUB; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.60.120.290; -; 2.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00431; CUB; 2.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 2.
SMART; SM00042; CUB; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01180; CUB; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autocatalytic cleavage; Calcium;
Complement activation lectin pathway; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immunity;
Innate immunity; Metal-binding; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi.
SIGNAL 1 19 {ECO:0000269|PubMed:11290788}.
CHAIN 20 699 Mannan-binding lectin serine protease 1.
/FTId=PRO_0000027592.
CHAIN 20 448 Mannan-binding lectin serine protease 1
heavy chain.
/FTId=PRO_0000027593.
CHAIN 449 699 Mannan-binding lectin serine protease 1
light chain.
/FTId=PRO_0000027594.
DOMAIN 20 138 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 139 182 EGF-like; calcium-binding.
DOMAIN 185 297 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 299 364 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 365 434 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 449 696 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 20 278 Interaction with FCN2.
REGION 20 184 Homodimerization. {ECO:0000250}.
REGION 20 184 Interaction with MBL2.
ACT_SITE 490 490 Charge relay system. {ECO:0000250}.
ACT_SITE 552 552 Charge relay system. {ECO:0000250}.
ACT_SITE 646 646 Charge relay system. {ECO:0000250}.
METAL 68 68 Calcium 1.
METAL 76 76 Calcium 1.
METAL 121 121 Calcium 1.
METAL 123 123 Calcium 1; via carbonyl oxygen.
METAL 139 139 Calcium 2.
METAL 140 140 Calcium 2; via carbonyl oxygen.
METAL 142 142 Calcium 2.
METAL 159 159 Calcium 2.
METAL 160 160 Calcium 2; via carbonyl oxygen.
METAL 163 163 Calcium 2; via carbonyl oxygen.
METAL 235 235 Calcium 3.
METAL 245 245 Calcium 3.
METAL 282 282 Calcium 3.
METAL 284 284 Calcium 3; via carbonyl oxygen.
SITE 448 449 Cleavage; by autolysis.
{ECO:0000269|PubMed:11290788}.
MOD_RES 159 159 (3R)-3-hydroxyasparagine. {ECO:0000255}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11290788,
ECO:0000269|PubMed:16335952}.
CARBOHYD 178 178 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18596036,
ECO:0000269|PubMed:19139490}.
CARBOHYD 385 385 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11290788,
ECO:0000269|PubMed:16335952}.
DISULFID 73 91 {ECO:0000269|PubMed:18596036}.
DISULFID 143 157 {ECO:0000269|PubMed:18596036}.
DISULFID 153 166 {ECO:0000269|PubMed:18596036}.
DISULFID 168 181 {ECO:0000269|PubMed:18596036}.
DISULFID 185 212 {ECO:0000269|PubMed:18596036}.
DISULFID 242 260 {ECO:0000269|PubMed:18596036}.
DISULFID 301 349 {ECO:0000250}.
DISULFID 329 362 {ECO:0000250}.
DISULFID 367 414 {ECO:0000250}.
DISULFID 397 432 {ECO:0000250}.
DISULFID 436 572 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00059, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302}.
DISULFID 475 491 {ECO:0000250}.
DISULFID 614 631 {ECO:0000250}.
DISULFID 642 672 {ECO:0000250}.
VAR_SEQ 1 113 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036809.
VAR_SEQ 364 380 IVDCRAPGELEHGLITF -> KNEIDLESELKSEQVTE
(in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_036810.
VAR_SEQ 381 699 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_036811.
VAR_SEQ 435 435 V -> ECGQPSRSLPSLVKRIIGGRNAEPGLFPWQALIVVE
DTSRVPNDKWFGSGALLSASWILTAAHVLRSQRRDTTVIPV
SKEHVTVYLGLHDVRDKSGAVNSSAARVVLHPDFNIQNYNH
DIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMLGLVAGW
GISNPNVTVDEIISSGTRTLSDVLQYVKLPVVPHAECKTSY
ESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDDLS
QRWVVQGLVSWGGPEECGSKQVYGVYTKVSNYVDWVWEQMG
LPQSVVEPQVER (in isoform 2 and isoform
4). {ECO:0000303|PubMed:11485744,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_036812.
VAR_SEQ 436 699 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11485744,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_036813.
VARIANT 3 699 Missing (in 3MC1).
{ECO:0000269|PubMed:28301481}.
/FTId=VAR_078814.
VARIANT 21 21 T -> I (in dbSNP:rs1062049).
/FTId=VAR_051831.
VARIANT 568 568 V -> A (in dbSNP:rs13322090).
/FTId=VAR_051832.
VARIANT 679 679 G -> R (in dbSNP:rs3774266).
/FTId=VAR_051833.
MUTAGEN 68 68 E->A,Q: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 77 77 Y->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 99 99 E->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 121 121 D->A,N: Loss of interaction with FNC2 and
FCN3 and partial loss of interaction with
MBL2. {ECO:0000269|PubMed:18596036}.
MUTAGEN 122 122 F->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 123 123 S->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 125 125 E->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 237 237 H->A: Loss of interaction with FCN2, FCN3
and MBL2. {ECO:0000269|PubMed:18596036}.
MUTAGEN 239 239 E->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 244 244 Y->A: Loss of interaction with FCN2, FCN3
and MBL2. {ECO:0000269|PubMed:18596036}.
MUTAGEN 262 262 E->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 274 274 S->A: Partial loss of interaction with
FCN2 and FCN3. No effect on interaction
with MBL2. {ECO:0000269|PubMed:18596036}.
MUTAGEN 283 283 N->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 286 286 E->A: Partial loss of interaction with
FCN2, FCN3 and MBL2.
{ECO:0000269|PubMed:18596036}.
MUTAGEN 646 646 S->A: No autoproteolytic processing.
{ECO:0000269|PubMed:15034049}.
CONFLICT 2 2 R -> K (in Ref. 6; BAF84375).
{ECO:0000305}.
CONFLICT 89 89 T -> A (in Ref. 7; CAH18409).
{ECO:0000305}.
CONFLICT 232 232 F -> L (in Ref. 6; BAF84375).
{ECO:0000305}.
CONFLICT 235 235 E -> Q (in Ref. 2; BAA05928 and 3;
BAA34864). {ECO:0000305}.
CONFLICT 285 285 G -> A (in Ref. 2; BAA05928, 3; BAA34864
and 4; BAA89206). {ECO:0000305}.
CONFLICT 392 392 E -> G (in Ref. 6; BAF83846).
{ECO:0000305}.
CONFLICT 499 499 E -> G (in Ref. 2; BAA05928).
{ECO:0000305}.
CONFLICT 499 499 E -> K (in Ref. 1; BAA04477 and 4;
BAA89206). {ECO:0000305}.
CONFLICT 527 527 D -> A (in Ref. 3; BAA34864).
{ECO:0000305}.
CONFLICT 543 543 Q -> K (in Ref. 1; BAA04477).
{ECO:0000305}.
CONFLICT 552 552 D -> V (in Ref. 3; BAA34864).
{ECO:0000305}.
CONFLICT 643 643 A -> S (in Ref. 1; BAA04477).
{ECO:0000305}.
STRAND 28 32 {ECO:0000244|PDB:3DEM}.
TURN 34 37 {ECO:0000244|PDB:3DEM}.
STRAND 42 51 {ECO:0000244|PDB:3DEM}.
STRAND 56 66 {ECO:0000244|PDB:3DEM}.
HELIX 71 73 {ECO:0000244|PDB:3DEM}.
STRAND 75 81 {ECO:0000244|PDB:3DEM}.
STRAND 86 90 {ECO:0000244|PDB:3DEM}.
STRAND 92 99 {ECO:0000244|PDB:3DEM}.
STRAND 110 120 {ECO:0000244|PDB:3DEM}.
STRAND 130 139 {ECO:0000244|PDB:3DEM}.
TURN 142 144 {ECO:0000244|PDB:3DEM}.
STRAND 154 160 {ECO:0000244|PDB:3DEM}.
STRAND 163 167 {ECO:0000244|PDB:3DEM}.
STRAND 192 199 {ECO:0000244|PDB:3DEM}.
TURN 200 203 {ECO:0000244|PDB:3DEM}.
STRAND 211 217 {ECO:0000244|PDB:3DEM}.
STRAND 223 228 {ECO:0000244|PDB:3DEM}.
STRAND 238 244 {ECO:0000244|PDB:3DEM}.
STRAND 246 251 {ECO:0000244|PDB:3DEM}.
STRAND 254 259 {ECO:0000244|PDB:3DEM}.
STRAND 261 263 {ECO:0000244|PDB:3DEM}.
STRAND 273 280 {ECO:0000244|PDB:3DEM}.
STRAND 291 297 {ECO:0000244|PDB:3DEM}.
STRAND 310 314 {ECO:0000244|PDB:4IGD}.
STRAND 317 320 {ECO:0000244|PDB:4IGD}.
STRAND 324 329 {ECO:0000244|PDB:4IGD}.
STRAND 333 337 {ECO:0000244|PDB:4IGD}.
STRAND 340 349 {ECO:0000244|PDB:4IGD}.
STRAND 355 357 {ECO:0000244|PDB:4IGD}.
STRAND 361 364 {ECO:0000244|PDB:4IGD}.
STRAND 376 382 {ECO:0000244|PDB:4IGD}.
STRAND 392 397 {ECO:0000244|PDB:4IGD}.
TURN 399 401 {ECO:0000244|PDB:4IGD}.
STRAND 402 404 {ECO:0000244|PDB:4IGD}.
HELIX 405 407 {ECO:0000244|PDB:4IGD}.
STRAND 411 414 {ECO:0000244|PDB:4IGD}.
TURN 416 418 {ECO:0000244|PDB:4DJZ}.
STRAND 420 422 {ECO:0000244|PDB:4IGD}.
TURN 423 425 {ECO:0000244|PDB:4IGD}.
STRAND 426 428 {ECO:0000244|PDB:4DJZ}.
STRAND 432 434 {ECO:0000244|PDB:4IGD}.
STRAND 463 468 {ECO:0000244|PDB:4IGD}.
STRAND 473 480 {ECO:0000244|PDB:4IGD}.
TURN 481 483 {ECO:0000244|PDB:4IGD}.
STRAND 484 487 {ECO:0000244|PDB:4IGD}.
HELIX 489 491 {ECO:0000244|PDB:4IGD}.
TURN 505 507 {ECO:0000244|PDB:4IGD}.
TURN 511 513 {ECO:0000244|PDB:4IGD}.
STRAND 514 519 {ECO:0000244|PDB:4IGD}.
STRAND 522 525 {ECO:0000244|PDB:4IGD}.
STRAND 531 540 {ECO:0000244|PDB:4IGD}.
TURN 546 549 {ECO:0000244|PDB:4IGD}.
STRAND 554 560 {ECO:0000244|PDB:4IGD}.
STRAND 565 567 {ECO:0000244|PDB:3GOV}.
STRAND 583 591 {ECO:0000244|PDB:4IGD}.
STRAND 594 596 {ECO:0000244|PDB:4IGD}.
STRAND 602 609 {ECO:0000244|PDB:4IGD}.
HELIX 611 618 {ECO:0000244|PDB:4IGD}.
HELIX 619 621 {ECO:0000244|PDB:4IGD}.
STRAND 629 632 {ECO:0000244|PDB:4IGD}.
STRAND 649 654 {ECO:0000244|PDB:4IGD}.
TURN 655 658 {ECO:0000244|PDB:4IGD}.
STRAND 659 666 {ECO:0000244|PDB:4IGD}.
HELIX 672 675 {ECO:0000244|PDB:4IGD}.
STRAND 677 683 {ECO:0000244|PDB:4IGD}.
HELIX 684 687 {ECO:0000244|PDB:4IGD}.
HELIX 688 695 {ECO:0000244|PDB:4IGD}.
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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E1895h ELISA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,CRARF,CRARF1,Homo sapiens,Human,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine pr 96T
U1895h CLIA Complement factor MASP-3,Complement-activating component of Ra-reactive factor,CRARF,CRARF1,Homo sapiens,Human,Mannan-binding lectin serine protease 1,Mannose-binding lectin-associated serine pro 96T
U2234h CLIA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus
E2234r Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus


 

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