Search
matrix metalloproteinase-7 (matrixin-7, matrin, urine metalloproteinase, pump-1 protease, matrylisin, MMP7, MPSL1, PUMP1)
Function:
- degrades casein, gelatins of types 1, 3, 4, & 5, & fibronectin
- activates procollagenase cleavage of 14-Ala-|-Leu-15 & 16-Tyr-|-Leu-17 in B chain of insulin
- no action on collagen types 1, 2, 4, 5
- cleaves gelatin chain alpha-2(I) > alpha-1(I)
Cofactor:
- binds 2 Ca+2 per subunit
- binds 2 Zn+2 per subunit
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
General
matrixin or matrix metalloproteinase
Properties
SIZE: entity length = 267 aa
MW = 30 kD
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-17}
Cysteine switch {85-92}
MOTIF: Zn+2-binding site
SITE: 87-87
Ca+2-binding site
SITE: 153-153
Zn+2-binding site
SITE: 163-163
Zn+2-binding site
SITE: 165-165
Ca+2-binding site
SITE: 170-170
Ca+2-binding site
SITE: 171-171
Ca+2-binding site
SITE: 173-173
Ca+2-binding site
SITE: 175-175
Zn+2-binding site
SITE: 178-178
Ca+2-binding site
SITE: 185-185
Ca+2-binding site
SITE: 187-187
Ca+2-binding site
SITE: 189-189
Zn+2-binding site
SITE: 191-191
Ca+2-binding site
SITE: 193-193
Ca+2-binding site
SITE: 196-196
Zn+2-binding site
SITE: 214-214
glutamate residue {E215}
Zn+2-binding site
SITE: 218-218
Zn+2-binding site
SITE: 224-224
Database Correlations
OMIM 178990
UniProt P09237
PFAM correlations
Entrez Gene 4316
KEGG correlations
ENZYME 3.4.24.23
References
UniProt :accession P09237