Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. Binds 1 zinc ion per subunit. 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. 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. The precursor is cleaved by a furin endopeptidase. Belongs to the peptidase M10A family.