Zinc metalloprotease-disintegrin AAV1: snake venom zinc metalloprotease that binds to the platelet collagen receptor glycoprotein VI (GP6) thus inhibiting collagen- and convulxin- (a GP6 agonist) induced platelet aggregation and the tyrosine phosphorylation of intracellular signaling proteins (LAT, SYK, p76SLP76, PIK3C, and PLCG2) that follows GP6 activation. Interestingly, blocks platelet aggregation but does not affect shape change. Also degrades the Aalpha chain of fibrinogen (FGA), followed by the Bbeta chain (FGB). Disintegrin AAV1-C: 30 kDa fragment of AAV1 autoproteolysed in absence of Ca(2+) that shows more potent inhibition of convulxin-induced platelet aggregation than AAV1. Binds 1 zinc ion per subunit. The proteinase activity is slightly enhanced by Ca(2+) and Mg(2+). Inhibited by EDTA and phenanthroline, but not by PMSF. Monomeric (57 kDa), and polymeric (180 kDa) forms have been detected under non-reducing conditions on SDS-PAGE, whereas only one monomeric form is observed under reducing conditions. Expressed by the venom gland. N-glycosylated. Does not cleave glycoprotein VI (GP6), gelatin (an irreversibly hydrolyzed form of collagen), fibronectin, prothrombin, and gamma chain of fibrinogen. May not bind to alpha-2/beta-1 integrin (ITGA2/ITGB1) (PubMed:17029743). Belongs to the venom metalloproteinase (M12B) family. P-III subfamily.