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matrix metalloproteinase-13 (matrixin-13, collagenase-3, MMP13)
Function:
- degrades collagen type 1
- does not act on gelatin or casein
- could have a role in tumoral process
Cofactor:
- binds 4 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
- contains 4 hemopexin-like domains
Expression: seems to be specific to breast carcinomas
Pathology:
- defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2
General
collagenase
matrixin or matrix metalloproteinase
Properties
SIZE: entity length = 471 aa
MW = 54 kD
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-19}
Cysteine switch {94-101}
MOTIF: Zn+2-binding site
SITE: 96-96
N-glycosylation site {N117}
N-glycosylation site {N152}
Ca+2-binding site
SITE: 162-162
Zn+2-binding site
SITE: 172-172
Zn+2-binding site
SITE: 174-174
Ca+2-binding site
SITE: 179-179
Ca+2-binding site
SITE: 180-180
Zn+2-binding site
SITE: 187-187
Ca+2-binding site
SITE: 194-194
Ca+2-binding site
SITE: 196-196
Ca+2-binding site
SITE: 198-198
Zn+2-binding site
SITE: 200-200
Ca+2-binding site
SITE: 205-205
Zn+2-binding site
SITE: 222-222
glutamate residue {E223}
Zn+2-binding site
SITE: 226-226
Zn+2-binding site
SITE: 232-232
cysteine residue {C284}
MODIFICATION: cysteine residue {C471}
Hemopexin-like 1 {290-332}
MOTIF: Ca+2-binding site
SITE: 291-291
Ca+2-binding site
SITE: 293-293
Hemopexin-like 2 {334-377}
MOTIF: Ca+2-binding site
SITE: 335-335
Ca+2-binding site
SITE: 337-337
Hemopexin-like 3 {382-429}
MOTIF: Ca+2-binding site
SITE: 383-383
Ca+2-binding site
SITE: 385-385
Hemopexin-like 4 {431-471}
MOTIF: Ca+2-binding site
SITE: 432-432
Ca+2-binding site
SITE: 434-434
cysteine residue {C471}
MODIFICATION: cysteine residue {C284}
Database Correlations
OMIM correlations
MORBIDMAP 600108
UniProt P45452
PFAM correlations
Entrez Gene 4322
Kegg hsa:4322
References
- OMIM :accession 600108
- UniProt :accession P45452