Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose, MHD=0.86 ug) when subcutaneously injected into mice. Has potent fibrinogenolytic activity on alpha-chain of fibrinogen (FGA). Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)-Leu(15) and Tyr(16)-Leu(17) followed by His(10)-Leu(11) and Phe(24)-Phe(25). Binds 1 zinc ion per subunit. Inhibited by EDTA, EGTA and 1,10-phenanthroline. Addition of Mg(2+) or Ca(2+) increases the casein hydrolysis rate. Monomer. Expressed by the venom gland. N-glycosylated. Contains 16 disulfide bonds. Does not degrade beta- and gamma-chains of fibrinogen. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.