matrix metalloproteinase-3 (matrixin-3, stromelysin-1, transin-1, SL-1, MMP3, STMY1)

Function: 1) degradation of a) fibronectin b) laminin c) gelatins of type 1, 3, 4, & 5 d) collagens 3, 4, 9, 10 e) cartilage proteoglycans 2) activates procollagenase 3) preferential cleavage where P1', P2' & P3' are hydrophobic residues 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 Laboratory: - stromelysin-1 in serum/plasma

General

Ca+2 binding protein glycoprotein matrixin or matrix metalloproteinase

Properties

SIZE: entity length = 477 aa MW = 54 kD COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-17} Cysteine switch {90-97} MOTIF: Zn+2-binding site SITE: 92-92 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 cysteine residue {C290} MODIFICATION: cysteine residue {C477} Hemopexin-like 1 {296-338} MOTIF: Ca+2-binding site SITE: 297-297 Hemopexin-like 2 {340-383} Hemopexin-like 3 {388-435} MOTIF: Ca+2-binding site SITE: 389-389 Hemopexin-like 4 {437-477} MOTIF: Ca+2-binding site SITE: 438-438 cysteine residue {C477} MODIFICATION: cysteine residue {C290} SECRETED-BY: fibroblast

Database Correlations

OMIM correlations MORBIDMAP 164015 UniProt P08254 PFAM correlations Entrez Gene 4314 Kegg hsa:4314 ENZYME 3.4.24.17