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. May activate progelatinase A.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.,
Membrane ; Single-pass type I membrane protein ; Extracellular side .
Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.
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