Venom serine protease that activates factor V (F5) in a calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule. Induces the coagulation of mammalian plasma. Fully activates human clotting factor V by a single cleavage at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2. Inhibited by D-Phe-Pro-Arg-chloromethyl ketone (FPRCK) (97%), PMSF (76%), and benzamidine (50%). Is not inhibited by BPTI, antithrombin and EDTA. Monomer. Expressed by the venom gland. There are three isoproteins of RVV-V, designated RVV-V alpha, V-beta, and V-gamma. Has no proteolytic effect on factor VIII, factor XIII, fibrinogen, and prothrombin. Belongs to the peptidase S1 family. Snake venom subfamily.