Snake venom phospholipase A2 homolog that lacks enzymatic activity (PubMed:28265084). In vivo, it displays local myotoxin and edema-inducing activities and is lethal by intraperitoneal injection (PubMed:10620318, PubMed:33865953). The myotoxicity effect is weaker in comparison to other myotoxins, probably due to the formation of high molecular weight complexes and to the oligomeric conformation (conventional dimer) (PubMed:10620318, PubMed:23573271). It shows specificity toward neurons and myotubes, but not on a variety of other cell types (PubMed:28265084, PubMed:10620318). This PLA2 excites a cohort of sensory neurons via ATP release and consequent activation of P2RX2 and/or P2RX3 purinergic receptors (PubMed:28265084). Pannexin hemichannels act as downstream mediators of toxin-evoked ATP release (PubMed:28265084). In vivo, it elicits nonneurogenic inflammatory pain, thermal hyperalgesia, and mechanical allodynia, of which the latter is completely dependent on purinergic signaling (PubMed:28265084). Myotoxin activity is inhibited by suramin and varespladib (PubMed:29985425, PubMed:33865953). Inhibition by suramin may be caused by (i) distortion of MDiS from both monomers impairing the membrane disruption mechanism by the toxin and (ii) surface electrostatic changes of the complex that interfere with the toxin membrane dockage process (putative-MDoS is partially hidden) (PubMed:29985425). Inhibition by varespladib is probably through varespladib binding to MDoS (PubMed:33865953). Monomer in solution (PubMed:29985425). Homodimer; non-covalently linked (probable conventional/extended dimer conformation) (PubMed:10620318, PubMed:23573271). Homotetramer (dimer of homodimer (probable conventional/extended dimer conformation)); non-covalently linked (PubMed:16511185, PubMed:23573271). Homooligomer (PubMed:10620318, PubMed:23573271). Expressed by the venom gland. LD(50) is 8.5 mg/kg by intraperitoneal injection into mice. 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 64, which corresponds to 'Lys-49' in the current nomenclature).