Zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. Binds 1 zinc ion per subunit. Monomer (PubMed:17485084) or heterodimer; non-covalently linked (PubMed:17497365). Interacts with fibrillar collagen. Expressed by the venom gland. The N-terminus is blocked. Average mass. Catrocollastatin-C represents at least 0.5% of the total protein in the venom. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIb sub-subfamily.