Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. Binds 1 zinc ion per subunit. 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.