matrix metalloproteinase-25; matrixin 25; membrane-type matrix metalloproteinase 6; leukolysin; membrane-type-6 matrix metalloproteinase; MT6-MMP (MMP25, MMPL1, MT6MMP)

Function: - may activate progelatinase A - 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; lipid-anchor, GPI-anchor, extracellular side - secreted, extracellular space, extracellular matrix Expression: - expressed predominantly in leukocytes, lung & spleen Pathology: - expressed also in colon carcinoma, astrocytoma & glioblastomas

Properties

SIZE: entity length = 562 aa MW = 63 kD COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-21} Cysteine switch {88-95} MOTIF: Zn+2-binding site SITE: 90-90 arginine-rich region {103-107} MOTIF: arginine residue (SEVERAL) Zn+2-binding site SITE: 233-233 glutamate residue {E234} Zn+2-binding site SITE: 237-237 Zn+2-binding site SITE: 243-243 cysteine residue {C317} MODIFICATION: cysteine residue {C508} Hemopexin-like 1 {321-365} Hemopexin-like 2 {370-412} Hemopexin-like 3 {416-462} Hemopexin-like 4 {464-508} MOTIF: cysteine residue {C508} MODIFICATION: cysteine residue {C317} glycosyl phosphatidylinositol [GPI] membrane anchor {N539}

Database Correlations

OMIM 608482 UniProt Q9NPA2 PFAM correlations Entrez Gene 64386 Kegg hsa:64386

References

UniProt :accession Q9NPA2