MASP2_HUMAN
ID MASP2_HUMAN Reviewed; 686 AA.
AC O00187; A8K458; A8MWJ2; O75754; Q5TEQ5; Q5TER0; Q96QG4; Q9BZH0; Q9H498;
AC Q9H499; Q9UBP3; Q9UC48; Q9ULC7; Q9UMV3; Q9Y270;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Mannan-binding lectin serine protease 2;
DE EC=3.4.21.104;
DE AltName: Full=MBL-associated serine protease 2;
DE AltName: Full=Mannose-binding protein-associated serine protease 2;
DE Short=MASP-2;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 2 A chain;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 2 B chain;
DE Flags: Precursor;
GN Name=MASP2;
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).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX PubMed=10330290; DOI=10.1093/intimm/11.5.859;
RA Takahashi M., Endo Y., Fujita T., Matsushita M.;
RT "A truncated form of mannose-binding lectin-associated serine protease
RT (MASP)-2 expressed by alternative polyadenylation is a component of the
RT lectin complement pathway.";
RL Int. Immunol. 11:859-863(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ACTIVATION BY
RP PROTEOLYTIC CLEAVAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=10092804;
RA Stover C.M., Thiel S., Thelen M., Lynch N.J., Vorup-Jensen T.,
RA Jensenius J.C., Schwaeble W.J.;
RT "Two constituents of the initiation complex of the mannan-binding lectin
RT activation pathway of complement are encoded by a single structural gene.";
RL J. Immunol. 162:3481-3490(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W., Laursen S.B.,
RA Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U., Reid K.B.M.,
RA Jensenius J.C.;
RT "Identification and characterization of a novel protein of the human
RT complement system, mannan-binding lectin-associated serine protease-2
RT (MASP-2).";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-371.
RA Takahashi M., Fujita T.;
RT "Partial genomic structure of human MBL-associated serine protease (MASP)-2
RT (from exon 1 to exon 5).";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Park D., Kim B., Baek K., Yoon J.;
RT "Structure of human MASP-2 gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
RP PROTEIN SEQUENCE OF 30-45.
RC TISSUE=Urine;
RX PubMed=8618346; DOI=10.1016/s0022-5347(01)66119-6;
RA Rasmussen H.H., Orntoft T.F., Wolf H., Celis J.E.;
RT "Towards a comprehensive database of proteins from the urine of patients
RT with bladder cancer.";
RL J. Urol. 155:2113-2119(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-284 AND 364-686, AND VARIANT
RP ALA-377.
RX PubMed=11426320; DOI=10.1038/sj.gene.6363745;
RA Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C.,
RA Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S.,
RA Fujita T., Schwaeble W.;
RT "The human gene for mannan-binding lectin-associated serine protease-2
RT (MASP-2), the effector component of the lectin route of complement
RT activation, is part of a tightly linked gene cluster on chromosome 1p36.2-
RT 3.";
RL Genes Immun. 2:119-127(2001).
RN [11]
RP FUNCTION, 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 16-181 (ISOFORM 2),
RP CHARACTERIZATION OF VARIANT GLY-120, CALCIUM-BINDING SITES, DIMERIZATION,
RP MUTAGENESIS OF TYR-74; TYR-121 AND GLU-124, INTERACTION WITH MBL2 AND FCN2,
RP AND DISULFIDE BONDS.
RX PubMed=15117939; DOI=10.1074/jbc.m402687200;
RA Gregory L.A., Thielens N.M., Matsushita M., Sorensen R., Arlaud G.J.,
RA Fontecilla-Camps J.-C., Gaboriaud C.;
RT "The X-ray structure of human mannan-binding lectin-associated protein 19
RT (MAp19) and its interaction site with mannan-binding lectin and L-
RT ficolin.";
RL J. Biol. Chem. 279:29391-29397(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 363-686, AND DISULFIDE BONDS.
RX PubMed=15364579; DOI=10.1016/j.jmb.2004.07.014;
RA Harmat V., Gal P., Kardos J., Szilagyi K., Ambrus G., Vegh B.,
RA Naray-Szabo G., Zavodszky P.;
RT "The structure of MBL-associated serine protease-2 reveals that identical
RT substrate specificities of C1s and MASP-2 are realized through different
RT sets of enzyme-substrate interactions.";
RL J. Mol. Biol. 342:1533-1546(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 287-686, AUTOCATALYTIC CLEAVAGE
RP AT ARG-444, AND MUTAGENESIS OF ARG-444.
RX PubMed=16040602; DOI=10.1074/jbc.m506051200;
RA Gal P., Harmat V., Kocsis A., Bian T., Barna L., Ambrus G., Vegh B.,
RA Balczer J., Sim R.B., Naray-Szabo G., Zavodszky P.;
RT "A true autoactivating enzyme. Structural insight into mannose-binding
RT lectin-associated serine protease-2 activations.";
RL J. Biol. Chem. 280:33435-33444(2005).
RN [15]
RP VARIANT MASPD GLY-120, AND CHARACTERIZATION OF VARIANT MASPD GLY-120.
RX PubMed=12904520; DOI=10.1056/nejmoa022836;
RA Stengaard-Pedersen K., Thiel S., Gadjeva M., Moller-Kristensen M.,
RA Sorensen R., Jensen L.T., Sjoeholm A.G., Fugger L., Jensenius J.C.;
RT "Inherited deficiency of mannan-binding lectin-associated serine protease
RT 2.";
RL N. Engl. J. Med. 349:554-560(2003).
RN [16]
RP VARIANTS GLN-99; CYS-118; GLY-120 AND LEU-126.
RX PubMed=16029433; DOI=10.1111/j.1399-0039.2005.00436.x;
RA Lozano F., Suarez B., Munoz A., Jensenius J.C., Mensa J., Vives J.,
RA Horcajada J.P.;
RT "Novel MASP2 variants detected among North African and Sub-Saharan
RT individuals.";
RL Tissue Antigens 66:131-135(2005).
RN [17]
RP VARIANTS MASPD GLY-120; LEU-126 AND HIS-ASN-HIS-156 INS, VARIANTS GLN-99;
RP CYS-118 AND ALA-377, AND CHARACTERIZATION OF VARIANT ALA-377.
RX PubMed=17252003; DOI=10.1038/sj.gene.6364373;
RA Thiel S., Steffensen R., Christensen I.J., Ip W.K., Lau Y.L., Reason I.J.,
RA Eiberg H., Gadjeva M., Ruseva M., Jensenius J.C.;
RT "Deficiency of mannan-binding lectin associated serine protease-2 due to
RT missense polymorphisms.";
RL Genes Immun. 8:154-163(2007).
RN [18]
RP VARIANTS MET-128 AND MET-405.
RX PubMed=25930971; DOI=10.1111/cge.12605;
RA Srour M., Hamdan F.F., Gan-Or Z., Labuda D., Nassif C., Oskoui M.,
RA Gana-Weisz M., Orr-Urtreger A., Rouleau G.A., Michaud J.L.;
RT "A homozygous mutation in SLC1A4 in siblings with severe intellectual
RT disability and microcephaly.";
RL Clin. Genet. 88:E1-E4(2015).
CC -!- FUNCTION: Serum protease that plays an important role in the activation
CC of the complement system via mannose-binding lectin. After activation
CC by auto-catalytic cleavage it cleaves C2 and C4, leading to their
CC activation and to the formation of C3 convertase.
CC {ECO:0000269|PubMed:10946292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage after Arg-223 in complement component C2 (-
CC Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement
CC component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104;
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to
CC MASP1. Binds SERPING1. Dimerization and MBL2 binding requires calcium
CC ions. {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:15117939,
CC ECO:0000269|PubMed:15364579}.
CC -!- INTERACTION:
CC O00187; P11226: MBL2; NbExp=6; IntAct=EBI-7965040, EBI-5325353;
CC O00187; P05155: SERPING1; NbExp=3; IntAct=EBI-7965040, EBI-1223454;
CC O00187; PRO_0000042699 [P0C0L5]; NbExp=4; IntAct=EBI-7965040, EBI-26369106;
CC O00187-1; P48740-1: MASP1; NbExp=8; IntAct=EBI-26357096, EBI-16138717;
CC O00187-1; P48740-2: MASP1; NbExp=4; IntAct=EBI-26357096, EBI-26435098;
CC O00187-1; P48740-3: MASP1; NbExp=7; IntAct=EBI-26357096, EBI-26435118;
CC O00187-2; O00187-2: MASP2; NbExp=2; IntAct=EBI-26356134, EBI-26356134;
CC O00187-2; P11226: MBL2; NbExp=3; IntAct=EBI-26356134, EBI-5325353;
CC PRO_0000027598; P11226: MBL2; NbExp=2; IntAct=EBI-25426044, EBI-5325353;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00187-1; Sequence=Displayed;
CC Name=2; Synonyms=MAp19, Small MBL-associated protein, sMAP;
CC IsoId=O00187-2; Sequence=VSP_005383, VSP_005384;
CC -!- TISSUE SPECIFICITY: Plasma.
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: Activated by cleavage after Arg-444. The uncleaved zymogen is
CC inactive towards synthetic substrates, but has sufficient activity to
CC effect autocatalytic cleavage.
CC -!- DISEASE: MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results
CC in autoimmune manifestations, recurrent severe infections, and chronic
CC inflammatory disease. {ECO:0000269|PubMed:12904520,
CC ECO:0000269|PubMed:17252003}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=MASP2base; Note=MASP2 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/MASP2base/";
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DR EMBL; Y09926; CAA71059.1; -; mRNA.
DR EMBL; AB008047; BAA78616.1; -; mRNA.
DR EMBL; Y18281; CAB50728.1; -; mRNA.
DR EMBL; Y18282; CAB50729.1; -; mRNA.
DR EMBL; Y18283; CAB50730.1; -; mRNA.
DR EMBL; Y18284; CAB50731.1; -; mRNA.
DR EMBL; Y18286; CAB50732.1; -; Genomic_DNA.
DR EMBL; Y18286; CAB50733.1; -; Genomic_DNA.
DR EMBL; Y18287; CAB50734.1; -; Genomic_DNA.
DR EMBL; Y18287; CAB50735.1; -; Genomic_DNA.
DR EMBL; X98400; CAA67050.1; -; mRNA.
DR EMBL; AB033742; BAA85658.1; -; Genomic_DNA.
DR EMBL; AB033742; BAA85659.1; -; Genomic_DNA.
DR EMBL; AF321558; AAG50275.1; -; Genomic_DNA.
DR EMBL; AF321562; AAG50274.1; -; Genomic_DNA.
DR EMBL; AF321558; AAG50274.1; JOINED; Genomic_DNA.
DR EMBL; AF321559; AAG50274.1; JOINED; Genomic_DNA.
DR EMBL; AF321560; AAG50274.1; JOINED; Genomic_DNA.
DR EMBL; AF321561; AAG50274.1; JOINED; Genomic_DNA.
DR EMBL; AK290823; BAF83512.1; -; mRNA.
DR EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ297949; CAC17138.1; -; Genomic_DNA.
DR EMBL; AJ297949; CAC17139.1; -; Genomic_DNA.
DR EMBL; AJ300188; CAC15568.1; -; Genomic_DNA.
DR CCDS; CCDS123.1; -. [O00187-1]
DR CCDS; CCDS124.1; -. [O00187-2]
DR PIR; A59271; A59271.
DR RefSeq; NP_006601.2; NM_006610.3. [O00187-1]
DR RefSeq; NP_631947.1; NM_139208.2. [O00187-2]
DR PDB; 1Q3X; X-ray; 2.23 A; A/B=363-686.
DR PDB; 1SZB; X-ray; 2.50 A; A/B=16-181.
DR PDB; 1ZJK; X-ray; 2.18 A; A=287-686.
DR PDB; 3TVJ; X-ray; 1.28 A; A=363-444, B=445-686.
DR PDB; 4FXG; X-ray; 3.75 A; G/I=291-444, H/J=445-686.
DR PDB; 5JPM; X-ray; 3.75 A; G/I=291-444, H/J=445-686.
DR PDBsum; 1Q3X; -.
DR PDBsum; 1SZB; -.
DR PDBsum; 1ZJK; -.
DR PDBsum; 3TVJ; -.
DR PDBsum; 4FXG; -.
DR PDBsum; 5JPM; -.
DR AlphaFoldDB; O00187; -.
DR SMR; O00187; -.
DR BioGRID; 115970; 19.
DR ComplexPortal; CPX-6203; MBL2-MASP2 lectin-protease complex.
DR ComplexPortal; CPX-6237; FCN1-MASP2 lectin-protease complex.
DR ComplexPortal; CPX-6238; FCN2-MASP2 lectin-protease complex.
DR ComplexPortal; CPX-6239; FCN3-MASP2 lectin-protease complex.
DR ComplexPortal; CPX-6240; CL-LK-MASP2 lectin-protease complex.
DR IntAct; O00187; 15.
DR MINT; O00187; -.
DR STRING; 9606.ENSP00000383690; -.
DR BindingDB; O00187; -.
DR ChEMBL; CHEMBL4295646; -.
DR DrugBank; DB04527; beta-Hydroxyasparagine.
DR DrugBank; DB16418; Narsoplimab.
DR MEROPS; S01.229; -.
DR GlyGen; O00187; 1 site.
DR iPTMnet; O00187; -.
DR PhosphoSitePlus; O00187; -.
DR BioMuta; MASP2; -.
DR CPTAC; non-CPTAC-2683; -.
DR jPOST; O00187; -.
DR MassIVE; O00187; -.
DR PaxDb; O00187; -.
DR PeptideAtlas; O00187; -.
DR PRIDE; O00187; -.
DR ProteomicsDB; 47767; -. [O00187-1]
DR ProteomicsDB; 47768; -. [O00187-2]
DR ABCD; O00187; 10 sequenced antibodies.
DR Antibodypedia; 27998; 375 antibodies from 27 providers.
DR DNASU; 10747; -.
DR Ensembl; ENST00000400897.8; ENSP00000383690.3; ENSG00000009724.17. [O00187-1]
DR Ensembl; ENST00000400898.3; ENSP00000383691.3; ENSG00000009724.17. [O00187-2]
DR GeneID; 10747; -.
DR KEGG; hsa:10747; -.
DR MANE-Select; ENST00000400897.8; ENSP00000383690.3; NM_006610.4; NP_006601.2.
DR UCSC; uc001aru.4; human. [O00187-1]
DR CTD; 10747; -.
DR DisGeNET; 10747; -.
DR GeneCards; MASP2; -.
DR HGNC; HGNC:6902; MASP2.
DR HPA; ENSG00000009724; Tissue enriched (liver).
DR MalaCards; MASP2; -.
DR MIM; 605102; gene.
DR MIM; 613791; phenotype.
DR neXtProt; NX_O00187; -.
DR OpenTargets; ENSG00000009724; -.
DR Orphanet; 331187; Immunodeficiency due to MASP-2 deficiency.
DR PharmGKB; PA30645; -.
DR VEuPathDB; HostDB:ENSG00000009724; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; O00187; -.
DR OMA; YTCAHDG; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; O00187; -.
DR TreeFam; TF330373; -.
DR BRENDA; 3.4.21.104; 2681.
DR PathwayCommons; O00187; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation. [O00187-1]
DR Reactome; R-HSA-166663; Initial triggering of complement. [O00187-1]
DR Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface. [O00187-1]
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. [O00187-1]
DR SABIO-RK; O00187; -.
DR SignaLink; O00187; -.
DR SIGNOR; O00187; -.
DR BioGRID-ORCS; 10747; 16 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; O00187; -.
DR GenomeRNAi; 10747; -.
DR Pharos; O00187; Tchem.
DR PRO; PR:O00187; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00187; protein.
DR Bgee; ENSG00000009724; Expressed in right lobe of liver and 102 other tissues.
DR Genevisible; O00187; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IDA:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0001855; F:complement component C4b binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008233; F:peptidase activity; IDA: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:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:ComplexPortal.
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 Gene3D; 2.40.10.10; -; 2.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR037571; MASP2.
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; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255:SF10; PTHR24255:SF10; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF07645; EGF_CA; 1.
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; SM00181; EGF; 1.
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; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autocatalytic cleavage; Calcium;
KW Complement pathway; Direct protein sequencing; Disease variant;
KW Disulfide bond; EGF-like domain; Hydrolase; Hydroxylation; Immunity;
KW Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..686
FT /note="Mannan-binding lectin serine protease 2"
FT /id="PRO_0000027598"
FT CHAIN 16..444
FT /note="Mannan-binding lectin serine protease 2 A chain"
FT /id="PRO_0000027599"
FT CHAIN 445..686
FT /note="Mannan-binding lectin serine protease 2 B chain"
FT /id="PRO_0000027600"
FT DOMAIN 16..137
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 138..181
FT /note="EGF-like; calcium-binding"
FT DOMAIN 184..296
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 298..363
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 364..432
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 445..684
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 483
FT /note="Charge relay system"
FT ACT_SITE 532
FT /note="Charge relay system"
FT ACT_SITE 633
FT /note="Charge relay system"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 122
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 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 158
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 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 444..445
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:16040602"
FT MOD_RES 158
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..90
FT DISULFID 142..156
FT DISULFID 152..165
FT DISULFID 167..180
FT DISULFID 184..211
FT /evidence="ECO:0000250"
FT DISULFID 241..259
FT /evidence="ECO:0000250"
FT DISULFID 300..348
FT /evidence="ECO:0000250"
FT DISULFID 328..361
FT /evidence="ECO:0000250"
FT DISULFID 366..412
FT DISULFID 396..430
FT DISULFID 434..552
FT /note="Interchain (between A and B chains)"
FT DISULFID 598..618
FT DISULFID 629..660
FT VAR_SEQ 182..185
FT /note="ALCS -> EQSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10092804,
FT ECO:0000303|PubMed:10330290"
FT /id="VSP_005383"
FT VAR_SEQ 186..686
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10092804,
FT ECO:0000303|PubMed:10330290"
FT /id="VSP_005384"
FT VARIANT 99
FT /note="R -> Q (in dbSNP:rs61735600)"
FT /evidence="ECO:0000269|PubMed:16029433,
FT ECO:0000269|PubMed:17252003"
FT /id="VAR_025344"
FT VARIANT 118
FT /note="R -> C (in dbSNP:rs147270785)"
FT /evidence="ECO:0000269|PubMed:16029433,
FT ECO:0000269|PubMed:17252003"
FT /id="VAR_025345"
FT VARIANT 120
FT /note="D -> G (in MASPD; found in a patient suffering from
FT frequent infections and chronic inflammatory disease;
FT strongly decreases affinity for MBL2 and FCN2;
FT dbSNP:rs72550870)"
FT /evidence="ECO:0000269|PubMed:12904520,
FT ECO:0000269|PubMed:15117939, ECO:0000269|PubMed:16029433,
FT ECO:0000269|PubMed:17252003"
FT /id="VAR_025346"
FT VARIANT 126
FT /note="P -> L (in MASPD; dbSNP:rs56392418)"
FT /evidence="ECO:0000269|PubMed:16029433,
FT ECO:0000269|PubMed:17252003"
FT /id="VAR_025347"
FT VARIANT 128
FT /note="T -> M (in dbSNP:rs141145402)"
FT /evidence="ECO:0000269|PubMed:25930971"
FT /id="VAR_075087"
FT VARIANT 155
FT /note="H -> R (in dbSNP:rs2273343)"
FT /id="VAR_028784"
FT VARIANT 156
FT /note="C -> CHNH (in MASPD)"
FT /id="VAR_065814"
FT VARIANT 371
FT /note="D -> Y (in dbSNP:rs12711521)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_028785"
FT VARIANT 377
FT /note="V -> A (associated with reduced MASP2 levels in
FT plasma; no effect on catalytic activity; dbSNP:rs2273346)"
FT /evidence="ECO:0000269|PubMed:11426320,
FT ECO:0000269|PubMed:17252003"
FT /id="VAR_028786"
FT VARIANT 405
FT /note="V -> M (in dbSNP:rs61735594)"
FT /evidence="ECO:0000269|PubMed:25930971"
FT /id="VAR_075088"
FT VARIANT 439
FT /note="R -> H (in dbSNP:rs12085877)"
FT /id="VAR_028787"
FT MUTAGEN 74
FT /note="Y->A: Strongly decreases affinity for MBL2.
FT Decreases affinity for FCN2."
FT /evidence="ECO:0000269|PubMed:15117939"
FT MUTAGEN 121
FT /note="Y->A: Strongly decreases affinity for MBL2, but not
FT for FCN2."
FT /evidence="ECO:0000269|PubMed:15117939"
FT MUTAGEN 124
FT /note="E->A: Decreases affinity for MBL2. Slight decrease
FT in affinity for FCN2."
FT /evidence="ECO:0000269|PubMed:15117939"
FT MUTAGEN 444
FT /note="R->Q: Abolishes autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:16040602"
FT CONFLICT 41
FT /note="N -> S (in Ref. 7; BAF83512)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> P (in Ref. 7; BAF83512)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..299
FT /note="QP -> HA (in Ref. 1; CAA71059, 3; CAB50733/CAB50735,
FT 4; CAA67050 and 6; AAG50274)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..362
FT /note="Missing (in Ref. 3; CAB50733/CAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="L -> LCS (in Ref. 3; CAB50733/CAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="T -> A (in Ref. 7; BAF83512)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="G -> E (in Ref. 6; AAG50274)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="G -> E (in Ref. 6; AAG50274)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..462
FT /note="Missing (in Ref. 3; CAB50733/CAB50735)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> LIL (in Ref. 3; CAB50733/CAB50735)"
FT /evidence="ECO:0000305"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1SZB"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 74..89
FT /evidence="ECO:0007829|PDB:1SZB"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1SZB"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:3TVJ"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 459..473
FT /evidence="ECO:0007829|PDB:3TVJ"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:3TVJ"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:3TVJ"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 510..519
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:3TVJ"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:3TVJ"
FT HELIX 595..603
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:1ZJK"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:3TVJ"
FT TURN 642..645
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 646..659
FT /evidence="ECO:0007829|PDB:3TVJ"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:3TVJ"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:3TVJ"
FT HELIX 676..685
FT /evidence="ECO:0007829|PDB:3TVJ"
SQ SEQUENCE 686 AA; 75702 MW; ED952085FA115E21 CRC64;
MRLLTLLGLL CGSVATPLGP KWPEPVFGRL ASPGFPGEYA NDQERRWTLT APPGYRLRLY
FTHFDLELSH LCEYDFVKLS SGAKVLATLC GQESTDTERA PGKDTFYSLG SSLDITFRSD
YSNEKPFTGF EAFYAAEDID ECQVAPGEAP TCDHHCHNHL GGFYCSCRAG YVLHRNKRTC
SALCSGQVFT QRSGELSSPE YPRPYPKLSS CTYSISLEEG FSVILDFVES FDVETHPETL
CPYDFLKIQT DREEHGPFCG KTLPHRIETK SNTVTITFVT DESGDHTGWK IHYTSTAQPC
PYPMAPPNGH VSPVQAKYIL KDSFSIFCET GYELLQGHLP LKSFTAVCQK DGSWDRPMPA
CSIVDCGPPD DLPSGRVEYI TGPGVTTYKA VIQYSCEETF YTMKVNDGKY VCEADGFWTS
SKGEKSLPVC EPVCGLSART TGGRIYGGQK AKPGDFPWQV LILGGTTAAG ALLYDNWVLT
AAHAVYEQKH DASALDIRMG TLKRLSPHYT QAWSEAVFIH EGYTHDAGFD NDIALIKLNN
KVVINSNITP ICLPRKEAES FMRTDDIGTA SGWGLTQRGF LARNLMYVDI PIVDHQKCTA
AYEKPPYPRG SVTANMLCAG LESGGKDSCR GDSGGALVFL DSETERWFVG GIVSWGSMNC
GEAGQYGVYT KVINYIPWIE NIISDF
