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matrix metalloproteinase-10 (matrixin-10, stromelysin-2, transin-2, MMP10, STMY2)
Function:
1) degradation of:
a) fibronectin
b) gelatins of type 1, 3, 4, 5
c) weakly collagen 3, 4, & 5
d) activates procollagenase
2) similar to stromelysin 1, but action on collagen 3, 4, & 5 is weak
Cofactor:
- binds 2 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 cysteine from the Zn+2 upon the activation-peptide release activates the enzyme
- belongs to the peptidase M10A family
- contains 4 hemopexin-like domains
General
matrixin or matrix metalloproteinase
Properties
SIZE: entity length = 476 aa
MW = 54 kD
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-17}
Cysteine switch {89-96}
MOTIF: Zn+2-binding site
SITE: 91-91
Zn+2-binding site
SITE: 217-217
glutamate residue {E218}
Zn+2-binding site
SITE: 221-221
Zn+2-binding site
SITE: 227-227
cysteine residue {C289}
MODIFICATION: cysteine residue {C476}
Hemopexin-like 1 {295-337}
Hemopexin-like 2 {339-382}
Hemopexin-like 3 {387-434}
Hemopexin-like 4 {436-476}
MOTIF: cysteine residue {C476}
MODIFICATION: cysteine residue {C289}
SECRETED-BY: fibroblast
Database Correlations
OMIM 185260
UniProt P09238
PFAM correlations
Entrez Gene 4319
Kegg hsa:4319
ENZYME 3.4.24.22
References
UniProt :accession P09238