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matrix metalloproteinase-15 (matrixin-15, membrane-type matrix metalloproteinase 2, MTMMP2, MMP15, MT2MMP, SMCP-2)
Function:
- endopeptidase that degrades various components of the extracellular matrix
- may activate progelatinase A
- precursor is cleaved by a furin endopeptidase
Cofactor:
- binds 1 Zn+2 per subunit (putative)
- Ca+2 (putative)
Structure:
- conserved Cys present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme;
- dissociation of the Cys from the Zn+2 upon the activation-peptide release activates the enzyme
- belongs to the peptidase M10A family
- contains 4 hemopexin-like domains
Compartment: membrane
Expression:
- expressed in liver, placenta, testis, colon & intestine > pancreas, kidney, lung, heart & skeletal muscle
General
hydrolase
matrixin or matrix metalloproteinase
membrane protein
Properties
SIZE: entity length = 669 aa
MW = 76 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-41}
Cysteine switch {109-116}
MOTIF: Zn+2-binding site
SITE: 111-111
N-glycosylation site {N150}
Zn+2-binding site
SITE: 259-259
glutamate residue {E260}
Zn+2-binding site
SITE: 263-263
Zn+2-binding site
SITE: 269-269
proline-rich region
SITE: 331-340
MOTIF: proline residue (SEVERAL)
cysteine residue {C370}
MODIFICATION: cysteine residue {C559}
Hemopexin-like 1 {374-417}
Hemopexin-like 2 {419-463}
Hemopexin-like 3 {466-512}
Hemopexin-like 4 {514-559}
MOTIF: cysteine residue {C559}
MODIFICATION: cysteine residue {C370}
transmembrane domain {626-646}
Database Correlations
OMIM 602261
UniProt P51511
PFAM correlations
Entrez Gene 4324
Kegg hsa:4324
References
UniProt :accession P51511