Toxin with unknown function in healthy organisms. On glioma cells, inhibits chloride currents in a voltage-dependent manner (when tested on gliomas cells) (PubMed:17166663). Also interacts with MMP2 and significantly inhibits its catalytic activity (PubMed:21424168). May be internalized with chloride channels (probably ClC-3/CLCN3) and MMP2, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation. Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Monoisotopic mass. This protein could be exploited as a potential therapeutic for glioma diagnosis and therapy, since it significantly inhibits the proliferation and metastasis of glioma cells, and has selective affinity to glioma cells. Does not inhibit potassium and sodium currents. Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family.