Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. Binds 4 Ca(2+) ions per subunit. Binds 2 Zn(2+) ions per subunit. Can be activated without removal of the activation peptide. 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. Undergoes autolytic cleavage to produce a N-terminal fragment having reduced collagenolytic activity. Tyrosine phosphorylated in platelets by PKDCC/VLK. Belongs to the peptidase M10A family.