Amphipathic alpha-helical antimicrobial peptide with highly potent activity against Gram-positive bacteria, and potent activity Gram-negative bacteria and fungi (MIC=2-30 uM) (PubMed:18584916, PubMed:18795798, PubMed:28319176). Acts through membranolytic mechanism involving rapid membrane permeabilization and depolarization (PubMed:28319176, PubMed:18795798). Shows a direct extra-cellular antiviral activity probably through degradation of the viral envelope (PubMed:30669255). Also shows a weak indirect antiviral activity by inhibiting virus replication (PubMed:30669255). Also displays anti-trypanosoma and anti-leishmania (prosmastigotes and axenic amastigotes) activity through membranolytic mechanism (PubMed:18584916, PubMed:25668079). Also induces apoptosis in leishmania promastigotes at high peptide concentrations (PubMed:28319176). Shows moderate hemolytic activity (LC(50)=25 uM) (PubMed:18584916, PubMed:18795798). In contrast to many antibiotics, this peptide does not induce bacterial resistance (PubMed:28319176). May insert into the lipid bilayer with an in-plane (parallel) orientation. Expressed by the skin glands. Attractive candidate as antimicrobial coating agent. When this peptide is covalently grafted to a surface, the adhering bacteria are most probably permeabilized (killed or at least damaged), thus unable to grow. Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.