Snake venom phospholipase A2 (PLA2) homolog that lacks enzymatic activity. Shows high myotoxin activities (PubMed:16442348, PubMed:9637370, PubMed:31748642). Also shows neurotoxicity, since it induces muscle paralysis when tested on mouse phrenic-diaphragm preparations (PubMed:16442348, PubMed:23810946, PubMed:26457430, PubMed:30679550). Displays edema-inducing activities (PubMed:9637370, PubMed:16442348, PubMed:26457430). Also displays antimicrobial activity against E.coli and C.albicans, as well as antitumoral activity against some human and mice cell lines (PubMed:16442348). In addition, it is effective as parasiticidal agent against Leishmania sp. and S.mansoni (PubMed:16442348). It also disrupts negatively charged liposomes in a dose- and temperature-dependent manner and shows toxicity by intraperitoneal route (PubMed:16442348). In contrast to other phospholipase A2-like toxins, this myotoxin does not require fatty acid binding to be active (PubMed:29287778). Myotoxic activity is inhibited by suramin and rosmarinic acid (PubMed:26457430, PubMed:30679550). Cytotoxic and myotoxic activities are inhibited by pre-incubation with varespladib (PubMed:31748642). Suramin inhibits this myotoxin by (i) direct blockage of the MDoS and MDiS, preventing the toxin/membrane interaction and disruption and (ii) formation of an oligomeric complex, resulting in a tetrameric configuration for which both MDoS and MDiS becomes physically inaccessible, thus avoiding any possibility of toxin-membrane interaction or disruption (PubMed:26457430). Heparin completely inhibits the cytotoxic and bactericidal activities, but only partially the myotoxic, edema-inducing and lethal effects (PubMed:9637370). Homodimer; non-covalently linked (probable alternative/compact dimer conformation) (Ref.4, PubMed:26457430, PubMed:29287778, PubMed:30679550). Expressed by the venom gland. Lacks hemorrhagic, anticoagulant and coagulant activities. Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily. Does not bind calcium as one of the calcium-binding sites is lost (Asp->Lys in position 48, which corresponds to 'Lys-49' in the current nomenclature).