matrix metalloproteinase-24; MMP-24; membrane-type matrix metalloproteinase 5; MT-MMP 5;membrane-type-5 matrix metalloproteinase; MT5-MMP (MMP24, MT5MMP)

Function: - activates progelatinase A - may also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate & chondroitin sulfate proteoglycans - partially cleaves fibronectin, but not collagen type 1, nor laminin (putative) - precursor is cleaved by a furin endopeptidase Cofactor: - binds 1 Zn⁺² per subunit (putative) - Ca⁺² (putative) 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: - cell membrane; extracellular side (putative) - processed form: secreted, extracellular space, extracellular matrix - shed from cell surface as soluble proteinase, by a proteolytic cleavage (putative) Expression: - predominantly expressed in brain, kidney, pancreas & lung Pathology: - overexpressed in a series of brain tumors, including astrocytomas & glioblastomas

Properties

SIZE: entity length = 645 aa MW = 73 kD COMPARTMENT: plasma membrane MOTIF: signal sequence {1-52} Cysteine switch {137-144} MOTIF: Zn+2-binding site SITE: 139-139 arginine-rich region {149-152} MOTIF: arginine residue (SEVERAL) Zn+2-binding site SITE: 282-282 glutamate residue {E283} Zn+2-binding site SITE: 286-286 Zn+2-binding site SITE: 292-292 cysteine residue {C380} MODIFICATION: cysteine residue {C569} Hemopexin-like 1 {384-427} Hemopexin-like 2 {429-473} Hemopexin-like 3 {476-522} Hemopexin-like 4 {524-569} MOTIF: cysteine residue {C569} MODIFICATION: cysteine residue {C380} transmembrane domain {603-623} Thr phosphorylation site {T629}

Database Correlations

OMIM 604871 UniProt Q9Y5R2 PFAM correlations Entrez Gene 10893 Kegg hsa:10893

References

UniProt :accession Q9Y5R2