Potent fibrinogenolytic protease which cleaves mainly the Aalpha chain of fibrinogen (FGA) and slightly the Bbeta (FGB) and the gamma (FGG) chains (PubMed:8193588, PubMed:7488093). May possess hemorrhagic activity (PubMed:7488093). Compared to other SVMP, the substrate-binding pocket is relatively shallow (PubMed:12077431). Is less susceptible to tripeptide inhibitors than TM-1 (AC U3KRG1) and TM-2 (PubMed:9703966). Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). Binds 1 zinc ion per subunit. Inhibited by EDTA and 1,10-phenanthroline (PubMed:8193588). Is also inhibited by endogenous tripeptide inhibitors pyroGlu-Asn-Trp, pyroGlu-Gln-Trp, and pyroGlu-Lys-Trp (PubMed:9703966, PubMed:12071970). Monomer. Expressed by the venom gland. The N-terminus is blocked. This disintegrin is 100% identical to the disintegrin of AC E9NW27, another disintegrin of the P-II subfamily of Protobothrops mucrosquamatus. The disintegrin belongs to the medium disintegrin subfamily. Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily. Extended N-terminus.