Snake venom zinc metalloprotease that causes hemorrhage and dose-dependently inhibits platelet aggregation triggered by collagen. This inhibition is due to its binding to glycoprotein VI (GP6) and collagen. The binding to GP6 results in inhibition of the signaling pathway (decrease of tyrosine phosphorylation of signaling proteins such as Syk, LAT, PI3-K and PLCgamma2). Preferentially cleaves alpha chain (FGA) of fibrinogen, followed by beta chain (FGB). Also degrades the extracellular matrix protein fibronectin (FN1), and cleaves collagen and von Willebrand factor (VWF). Binds 1 zinc ion per subunit. The proteinase activity is slightly enhanced by Ca(2+) and Mg(2+), but is completely inhibited by Zn(2+). Is completely inhibited by phenanthroline and EDTA. Not inhibited by PMSF. Monomer. Expressed by the venom gland. N-glycosylated. Does not degrade gamma chain of fibrinogen (PubMed:12008947). Does not inhibit collagen-induced platelet aggregation by activating alpha-2/beta-1 integrin (ITGA2/ITGB1), or by inhibiting alpha-IIb/beta-3 (ITGA2B/ITGB3) interaction with fibrinogen. Does not cleave platelet membrane glycoproteins, including glycoprotein VI (GP6), GPIbalpha (GP1BA) and beta-3 integrin (ITGB3) (PubMed:12008947). Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.