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matrix metalloproteinase-14 (matrixin-14, membrane-type matrix metalloproteinase 1, MMP14, MTMMP1, MT1MMP, MMP- X1, MT1-MMP)
Function:
- seems to specifically activate progelatinase A
- precursor is cleaved by a furin endopeptidase
- endopeptidase activity
- activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38
- other bonds hydrolyzed include 35-gly-|-Ile-36 in the propeptide of collagenase 3, & 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 & 354-Gln-|-Thr-355 in the aggrecan interglobular domain
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, melanosome
- identified by mass spectrometry in melanosome fractions from stage 1 to stage 4
Expression: stromal cells of colon, breast, & head & neck
Pathology:
- may thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface
General
collagenase
matrixin or matrix metalloproteinase
membrane protein
Properties
SIZE: entity length = 582 aa
MW = 66 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-20}
Cysteine switch {91-98}
MOTIF: Zn+2-binding site
SITE: 93-93
Zn+2-binding site
SITE: 239-239
glutamate residue {E240}
Zn+2-binding site
SITE: 243-243
Zn+2-binding site
SITE: 249-249
cysteine residue {C319}
MODIFICATION: cysteine residue {C508}
Hemopexin-like 1 {323-366}
Hemopexin-like 2 {368-412}
Hemopexin-like 3 {415-461}
Hemopexin-like 4 {463-508}
MOTIF: cysteine residue {C508}
MODIFICATION: cysteine residue {C319}
transmembrane domain {542-562}
Database Correlations
OMIM 600754
UniProt P50281
PFAM correlations
Entrez Gene 4323
Kegg hsa:4323
ENZYME 3.4.24.80
References
UniProt :accession P50281