matrix metalloproteinase-27; matrixin 27 (MMP27)

Function: - matrix metalloproteinases degrade protein components of the extracellular matrix, including fibronectin, laminin, gelatins &/or collagens Cofactor: - binds 4 Ca⁺² per subunit - binds 2 Zn⁺² per subunit Structure: - the conserved Cys present in the cysteine-switch motif binds the catalytic Zn⁺², thus inhibiting the enzyme - dissociation of Cys from Zn⁺² upon activation- peptide release activates the enzyme - belongs to the peptidase M10A family - contains 4 hemopexin-like domains Compartment: secreted Expression: expressed in B-cells

General

Ca+2 binding protein glycoprotein matrixin or matrix metalloproteinase

Properties

SIZE: MW = 59 kD entity length = 513 aa COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-17} Cysteine switch {91-91} N-glycosylation site {N110} Ca+2-binding site SITE: 121-121 Ca+2-binding site SITE: 155-155 Zn+2-binding site SITE: 165-165 Ca+2-binding site SITE: 173-173 Ca+2-binding site SITE: 174-174 Ca+2-binding site SITE: 178-178 Zn+2-binding site SITE: 181-181 Ca+2-binding site SITE: 188-188 Ca+2-binding site SITE: 192-192 Zn+2-binding site SITE: 194-194 Ca+2-binding site SITE: 196-196 Ca+2-binding site SITE: 199-199 Zn+2-binding site SITE: 216-216 glutamate residue {E217} Zn+2-binding site SITE: 220-220 Zn+2-binding site SITE: 226-226 cysteine residue {C279} MODIFICATION: cysteine residue {C465} Hemopexin-like 1 {285-327} MOTIF: Ca+2-binding site SITE: 286-286 Hemopexin-like 2 {329-371} Hemopexin-like 3 {376-423} MOTIF: Ca+2-binding site SITE: 377-377 Hemopexin-like 4 {425-465} MOTIF: Ca+2-binding site SITE: 426-426 cysteine residue {C465} MODIFICATION: cysteine residue {C279}

Database Correlations

UniProt Q9H306 PFAM correlations Entrez Gene 60466 Kegg hsa:64066