Amphipathic alpha-helical antimicrobial peptide with moderate to potent activity against Gram-positive bacteria, Gram-negative bacteria and fungi (PubMed:10951191, PubMed:19056250, PubMed:23841919, PubMed:24728560, PubMed:31358802). Shows also a weak activity against biofilm of both Gram-positive and Gram-negative bacteria (PubMed:19056250). Probably acts by disturbing membrane functions with its amphipathic structure (PubMed:10951191, PubMed:23841919). Kills fungi via membranolytic action (PubMed:24728560). Enhanced sterol levels in lipid composition membranes reduce interaction of this peptide with membranes, having a protective effect against the lytic ability of the peptide (PubMed:24728560). Shows anticancer activity (PubMed:10951191). May be monomeric or may oligomerize as homodimers or homotrimers in Gram-positive and Gram-negative bacteria mimetic membranes. Contact and insertion into membrane begin at the N-terminus. Expressed by the skin dorsal glands. C-terminal amidation enhances antibacterial activity. This increase may be due to stabilization of the alpha-helical structure at the membrane interface. The primary structure of the mature peptide is identical to that of aurein-2.5 from Ranoidea raniformis (AC P69018). Belongs to the frog skin active peptide (FSAP) family. Aurein subfamily.