Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. May play a role in the deterioration of the heart wall extracellular matrix proteins during the onset of dilated cardiomyopathy. 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 N-terminus is blocked. Tyrosine phosphorylated in platelets by PKDCC/VLK. Belongs to the peptidase M10A family.