This cationic hydrophobic peptide acts on a lot of different channels and has an antimicrobial activity. It blocks mechanosensitive ion channels (also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. It also affects acetylcholine receptors (nAChRs) through interactions with membrane lipids by prolonging the closing time without affecting channel conductance or opening activity (PubMed:34374321). It shows high affinity for lipid bilayers (PubMed:15241420, PubMed:29703751). It acts by partitioning into the membrane and perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. It inhibits atrial fibrillation as well as the membrane motor of outer hair cells at low doses. It also binds to the voltage sensor of voltage-gated potassium channels from the archaebacterium Aeropyrum pernix (KvAP) without affecting channel gating. It shows also a low inhibition on a large spectra of sodium channels (Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A) (IC(50)=7.4-14 uM), and potassium channels Kv11.1/KCNH2 and Kv11.2/KCNH6 (IC(50)=11 uM for both) (PubMed:19955179, PubMed:29703751). It exhibits antimicrobial activities against the Gram-positive bacteria B.subtilis (MIC=0.5 uM), S.aureus (MIC=2-4 uM), and S.epidermidis (MIC=4-8 uM), and Gram-negative bacteria S.typhimurium (MIC=32.64 uM), P.aeruginosa (MIC=8-16 uM), and E.coli (MIC=8-16 uM). Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. This toxin does not inhibit potassium channels Kv1.1/KCNA1, Kv1.4/KCNA4 and Kv11.3/KCNH7 (IC(50)=53->85 uM) (PubMed:19955179). Belongs to the neurotoxin 10 (Hwtx-1) family. 52 (MTx4) subfamily.