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mannan-binding lectin serine protease 2; MBL-associated serine protease 2; mannose-binding protein-associated serine protease 2; MASP-2; contains: mannan-binding lectin serine protease 2 A chain; mannan-binding lectin serine protease 2 B chain (MASP2)
Function:
- serine protease
- role in activation of the complement system via mannose-binding lectin
- after activation by auto-catalytic cleavage it cleaves complement-C2 & complement-C4, leading to their activation & to the formation of C3 convertase
- selective cleavage after Arg-223 in complement-C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) & after Arg-76 in complement-C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile)
- iron & 2-oxoglutarate dependent 3-hydroxylation of Asp & Asn is (R) stereospecific within EGF domains
- activated by cleavage after Arg-444
- uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage
- binds MBL2
- isoform 2 binds to MASP1
- binds SERPING1
- dimerization & MBL2 binding requires Ca+2
Structure:
- homodimer; disulfide-linked
- belongs to the peptidase S1 family
- contains 2 CUB domains
- contains 1 EGF-like domain
- contains 1 peptidase S1 domain
- contains 2 Sushi (CCP/SCR) domains
Compartment: secreted
Alternative splicing: named isoforms=2
Expression: plasma
Pathology:
- defects in MASP2 are the cause of MASP2 deficiency
Related
lectin
mannan (mannosan)
mannose
General
Ca+2 binding protein
glycoprotein
secreted protein
serine protease
Properties
SIZE: entity length = 686 aa
MW = 76 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-15}
CUB domain {16-137}
MOTIF: Ca+2-binding site
SITE: 67-67
cysteine residue {C72}
MODIFICATION: cysteine residue {C90}
Ca+2-binding site
SITE: 75-75
cysteine residue {C90}
MODIFICATION: cysteine residue {C72}
Ca+2-binding site
SITE: 120-120
Ca+2-binding site
SITE: 122-122
Ca+2-binding site
SITE: 123-123
EGF domain {138-181}
MOTIF: Ca+2-binding site
SITE: 138-138
Ca+2-binding site
SITE: 139-139
Ca+2-binding site
SITE: 141-141
cysteine residue {C142}
MODIFICATION: cysteine residue {C156}
cysteine residue {C152}
MODIFICATION: cysteine residue {C165}
cysteine residue {C156}
MODIFICATION: cysteine residue {C142}
Ca+2-binding site
SITE: 158-158
Ca+2-binding site
SITE: 159-159
Ca+2-binding site
SITE: 162-162
cysteine residue {C165}
MODIFICATION: cysteine residue {C152}
cysteine residue {C167}
MODIFICATION: cysteine residue {C180}
cysteine residue {C180}
MODIFICATION: cysteine residue {C167}
CUB domain {184-296}
MOTIF: cysteine residue {C184}
MODIFICATION: cysteine residue {C211}
cysteine residue {C211}
MODIFICATION: cysteine residue {C184}
cysteine residue {C241}
MODIFICATION: cysteine residue {C259}
cysteine residue {C259}
MODIFICATION: cysteine residue {C241}
Sushi domain {298-363}
MOTIF: cysteine residue {C300}
MODIFICATION: cysteine residue {C348}
cysteine residue {C328}
MODIFICATION: cysteine residue {C361}
cysteine residue {C348}
MODIFICATION: cysteine residue {C300}
cysteine residue {C361}
MODIFICATION: cysteine residue {C328}
Sushi domain {364-432}
MOTIF: cysteine residue {C366}
MODIFICATION: cysteine residue {C412}
cysteine residue {C396}
MODIFICATION: cysteine residue {C430}
cysteine residue {C412}
MODIFICATION: cysteine residue {C366}
cysteine residue {C430}
MODIFICATION: cysteine residue {C396}
cysteine residue {C434}
MODIFICATION: cysteine residue {C-INTERCHAIN}
proteolytic site {444-445}
S1 domain {445-684}
MOTIF: histidine residue {H483}
aspartate residue {D532}
cysteine residue {C598}
MODIFICATION: cysteine residue {C618}
cysteine residue {C618}
MODIFICATION: cysteine residue {C598}
cysteine residue {C629}
MODIFICATION: cysteine residue {C660}
serine residue {S633}
cysteine residue {C660}
MODIFICATION: cysteine residue {C629}
Database Correlations
OMIM correlations
MORBIDMAP 605102
UniProt O00187
PFAM correlations
Entrez Gene 10747
Kegg hsa:10747
ENZYME 3.4.21.104
References
- UniProt :accession O00187
- MASP2base; MASP2 mutation db
http://bioinf.uta.fi/MASP2base/