Insecticidal presynaptic neurotoxin that induces massive neurotransmitter release at insect (but not vertebrate) neuromuscular junctions. Native toxin forms cation-permeable pores (with high permeability to calcium) in lipid membranes locust muscle membrane and artificial lipid bilayers (By similarity). May bind to insect neurexin-1 homolog, insect adhesion G protein-coupled receptor L1 homolog, and insect receptor-type tyrosine-protein phosphatase S homolog, and induces neurotransmitter exocytosis both by forming tetrameric pores in membranes and signaling via G protein-coupled receptor (By similarity). Oligomerization is a process independent of divalent cations (By similarity). The toxin forms channels with 0.55-0.58 nm entrance diameter and a relatively small conductance in planar phospholipid membranes (By similarity). Homotetramer in membranes. Forms a membrane channel in the prey. Expressed by the venom gland. The H8 helix is predicted to insert into membranes and form pores by assembling into tetramers. The helix is contained within a helical bundle domain that undergoes significant conformational changes during pore formation to allow exposure of the H8 transmembrane helix and transition of the toxin from a soluble monomer to a transmembrane tetramer. Iso and Leu residues are assigned by comparison with orthologs. Belongs to the cationic peptide 01 (latrotoxin) family. 02 (alpha-latroinsectotoxin) subfamily.