Amphipathic peptide that shows bradykinin potentiating activity and antimicrobial activities against bacteria and fungi. Has higher antibacterial activities against Gram-negative than against Gram-positive bacteria. Also inhibits NADPH oxidase-dependent superoxide production (IC(50) is 0.4 uM on granulocytes stimulated with PMA, IC(50) is 0.51 uM on HL-60 cells undifferentiated and IC(50) is 0.53 uM on HL-60 cells treated with DMSO). The C-terminal peptide shows a higher bradykinin potentiating activity than the complete peptide. Expressed by the venom gland. Shows a very weak hemolytic activity (6 uM causes only 3.5 % of hemolysis). Shows a alpha-helical structure. The genomic DNA coding for this protein is not a continuous sequence in the genome. The transcript of this protein may be generated by trans-splicing, by which exons from two independently transcribed pre-mRNAs are joined to form a single mature transcript (PubMed:22115565). Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Long chain multifunctional peptide (group 2) family.