Snake venom phospholipase A2 (PLA2) that shows anticoagulant activities, strong myolytic activity, infiltration of polymorphonuclear cells, and edema in stromal tissues. Induces cell death of Jurkat cells in a concentration-dependent manner. Shows a low phospholipase A2 activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) Binds 1 Ca(2+) ion. Exists as a monomer in both solution and crystal states (PubMed:30787342). In the presence of SDS or probably in the presence of phospholipids, assembles to form SDS-resistant stable oligomers (PubMed:30787342). Expressed by the venom gland. Is abundantly expressed in Tokunoshima and Amami-Oshima P.flavoviridis venom, but is missing in Okinawa P.flavoviridis venom. It is thought that loss of BP-II in Okinawa P.flavoviridis is due to lack of necessity for a strong toxicity exerted by BP-II in the venom as far as they feed mostly on frogs. Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily. Binds calcium very weakly as one of the calcium-binding ligands is lost (Asp->Lys in position 64, which corresponds to 'Lys-49' in the current nomenclature).