Weak blocker of potassium channels Kv1.1/KCNA1 (IC(50)=578.5 nM-9.9 uM) and Kv1.6/KCNA6 (~60% block at 30 uM of toxin) (PubMed:22305749, PubMed:26724500). Acts by binding to the pore and occluding it (PubMed:22305749). Has a voltage-dependent mode of action, which can be explained by a high content of basic residues causing repulsions at higher membrane voltages (PubMed:22305749). Shows a weak interaction with muscle-type nicotinic acetylcholine receptors (nAChR), since it inhibits alpha-bungarotoxin binding to muscle-type nAChR from T.californica (IC(50)=1.4 uM) (PubMed:31276191). This suggests it probably weakly inhibits muscle nAChR (PubMed:31276191). The mode of binding to potassium channels of this toxin differs from its homologs (including HefuTx1), since it lacks the key aromatic residue of the functionnal dyad. In contrast, its functionally important site is composed of a number of basic residues (PubMed:32172732). Expressed by the venom gland. Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)). Does not block or very poorly blocks Kv1.2/KCNA2, Kv1.3/KCNA3 (20%), Kv1.4/KCNA4 (13%), Kv1.5/KCNA5, Kv1.8/KCNA10, Kv2.1/KCNB1, Kv3.1/KCNC1, Kv4.2/KCND2, KCa2.3/KCNN3, KCa3.1/KCNN4 (PubMed:22305749). May not inhibit neuronal human alpha-7 nAChR, since it does not inhibit alpha-7 alpha-bungarotoxin binding (IC(50)=64 uM) (PubMed:31276191). Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor kappa-KTx family. Kappa-KTx 5 subfamily.