Toxin with unknown function in healthy organisms. On glioma cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2 at the surface of glioma cells. This complex is then internalized via caveolae, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation (By similarity). Has been shown to weakly inhibit TRPV1 channels (PubMed:29483648). Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family.