catalytic activity:Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.,cofactor:Binds 1 zinc ion per subunit.,cofactor:Calcium.,domain:The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.,function:Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.,
[Isoform Long]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.
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