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matrix metalloproteinase-1; matrixin-1; interstitial collagenase; fibroblast collagenase (MMP1, CLG)
Function:
- cleaves collagens of types 1, 2, & 3 at one site in the helical domain
- also cleaves collagens of types 7 & 10
- in case of HIV infection, interacts & cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity
- can be activated without removal of the activation peptide
- undergoes autolytic cleavage to two major forms (22 kD & 27 kD (a minor form (25 kD) is the glycosylated form of the 22 kD form)
- the 27 kD form has no activity while the 22/25 kD form can act as activator for collagenase
- cleavage of the triple helix of collagen at about 3/4 of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain
- cleaves synthetic substrates & alpha-macroglobulins at bonds where P1' is a hydrophobic residue
Cofactor:
- binds 4 Ca+2 per subunit
- binds 2 Zn+2 per subunit
Structure:
- two distinct domains in this protein
a) catalytic N-terminal
b) C-terminal, involved in substrate specificity & in binding TIMP (tissue inhibitor of metalloproteinases)
- conserved cysteine 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
Compartment: secreted
General
matrixin or matrix metalloproteinase
Properties
SIZE: entity length = 469 aa
MW = 54 kD
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-19}
Cysteine switch {90-97}
MOTIF: Zn+2-binding site
SITE: 92-92
Metalloprotease {98-276}
MOTIF: N-glycosylation site {N120}
Ca+2-binding site
SITE: 124-124
Ca+2-binding site
SITE: 158-158
Zn+2-binding site
SITE: 168-168
Zn+2-binding site
SITE: 170-170
Ca+2-binding site
SITE: 175-175
Ca+2-binding site
SITE: 176-176
Ca+2-binding site
SITE: 178-178
Ca+2-binding site
SITE: 180-180
Zn+2-binding site
SITE: 183-183
Ca+2-binding site
SITE: 190-190
Ca+2-binding site
SITE: 192-192
Ca+2-binding site
SITE: 194-194
Zn+2-binding site
SITE: 196-196
Ca+2-binding site
SITE: 198-198
Ca+2-binding site
SITE: 199-199
Ca+2-binding site
SITE: 201-201
Zn+2-binding site
SITE: 218-218
glutamate residue {E219}
Zn+2-binding site
SITE: 222-222
Zn+2-binding site
SITE: 228-228
peptide motif {269-270}
cysteine residue {C278}
MODIFICATION: cysteine residue {C466}
Hemopexin-like 1 {284-326}
MOTIF: Ca+2-binding site
SITE: 285-285
Hemopexin-like 2 {328-372}
MOTIF: Ca+2-binding site
SITE: 329-329
Hemopexin-like 3 {377-424}
MOTIF: Ca+2-binding site
SITE: 378-378
Hemopexin-like 4 {426-466}
MOTIF: Ca+2-binding site
SITE: 427-427
cysteine residue {C466}
MODIFICATION: cysteine residue {C278}
Database Correlations
OMIM 120353
UniProt P03956
PFAM correlations
Entrez Gene 4312
Kegg hsa:4312
ENZYME 3.4.24.7
References
- UniProt :accession P03956
- Wikipedia; Note: collagenase entry
http://en.wikipedia.org/wiki/collagenase