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matrix metalloproteinase-23; MMP-23; matrix metallopeptidase 21; MMP-21; matrix metalloprotease 22; MMP-22; femalysin; MIFR-1 (MMP23A, MMP23B, MMP22)
Function:
1) protease
2) inhibited by TIMP2
3) proteolytic cleavage might yield an active form
Structure:
1) belongs to the peptidase M10A family
2) N-glycosylated
3) contains 1 Ig-like C2-type domain (immunoglobulin-like domain)
Cofactor: binds 1 Zn+2 per subunit
Compartment:
- membrane, cytoplasm, perinuclear region
- secreted form produced by proteolytic cleavage
Alternative splicing: named isoforms=3
Expression: expressed in ovary, testis, prostate
General
matrixin or matrix metalloproteinase
Properties
SIZE: MW = 44 kD
entity length = 390 aa
COMPARTMENT: cytoplasm
cell nucleus
MOTIF: transmembrane domain {20-40}
proteolytic site {78-79}
N-glycosylation site {N92}
N-glycosylation site {N148}
Zn+2-binding site
SITE: 211-211
glutamate residue {E212}
Zn+2-binding site
SITE: 215-215
Zn+2-binding site
SITE: 221-221
N-glycosylation site {N232}
immunoglobulin superfamily domain {295-380}
MOTIF: N-glycosylation site {N316}
cysteine residue {C321}
MODIFICATION: cysteine residue {C370}
cysteine residue {C370}
MODIFICATION: cysteine residue {C321}
Database Correlations
OMIM correlations
UniProt O75900
LOCUS-LINK correlations
References
UniProt :accession O75900