Inhibits voltage-gated potassium channel rKv1.1/KCNA1 (IC(50)=1.9 nM) (PubMed:25792741, PubMed:32733247). Also shows less potent inhibition on Kv1.2/KCNA2 (IC(50)=105.9 nM), Kv1.3/KCNA3 (IC(50)=8.9 nM), and Kv1.6/KCNA6 (IC(50)=63.4 nM) (PubMed:32733247). Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta). C-terminal amidation is not fundamental for activity. It permits a slightly higher activity on Kv1.1/KCNA1 potassium channels (native toxin IC(50)=1.9 nM), than non-amidated recombinant toxin (IC(50)=6.7 nM). The primary structure of this mature peptide is identical to that of toxin alpha-KTx 3.6 from Mesobuthus martensii (AC Q9NII7). Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 03 subfamily.