Inhibits high conductance calcium-activated potassium channels (By similarity). Reversibly inhibits Shaker B potassium channels. Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). The N-terminal C2-C5 disulfide bridge unique to this toxin does not appear to confer stability to the protein. Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 12 subfamily.