Gating-modifier toxin that targets voltage-gated sodium channels. According to Deuis et al., 2017, it shows a preferential activity on Nav1.7/SCN9A (Nav1.7/SCN9A (IC(50)=0.9-4.4 nM)) (PubMed:28106092). However, another study shows a much less potent activity on Nav1.7/SCN9A (IC(50)=1457 nM) (PubMed:31234412). Also shows weaker effects on hNav1.1/SCN1A (IC(50)=37 nM), hNav1.2/SCN2A (IC(50)=124 nM), hNav1.3/SCN3A (IC(50)=210 nM), hNav1.4/SCN4A (IC(50)=144 nM), hNav1.5/SCN5A (IC(50)=800 nM), hNav1.6/SCN8A (IC(50)=129 nM), hNav1.9/SCN11A (IC(50)=2427 nM) (PubMed:28106092). On Nav1.7/SCN9A, the toxin acts by shifting the voltage-dependence of activation to more depolarized potentials, whereas it does not cause significant effect on the voltage-dependence of activation on other sodium channels (PubMed:28106092). Minor effects are observed on the voltage-dependence of steady-state fast inactivation for all sodium channels tested (Nav1.1/SCN1A-Nav1.8/SCN10A) (PubMed:28106092). By testing the toxin on channel chimera, it has been shown to interact with the S3-S4 linkers in DII and DIV domains of Nav1.7/SCN9A (PubMed:28106092). In vivo, when tested on the OD1-induced mouse model of Nav1.7/SCN9A-mediated pain, the toxin dose-dependently reduces pain behaviors (PubMed:28106092). Expressed by the venom gland. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Monoisotopic mass. This toxin may represent a lead for the development of novel analgesic agents. When injected with an opioid analgesic drug, it provides an enhanced and effective therapeutic approach to the treatment and/or prevention of pain. Shows no or weak effect on hNav1.8/SCN10A (IC(50)=50 uM), rKv2.1/KCNB1 (up to 300 nM) and hCav1.2/CACNA1C, hCav2.2/CACNA1B, alpha-7/SCN9A nAChR, alpha-3/SCN3A nAChR (up to 10 uM). Belongs to the neurotoxin 10 (Hwtx-1) family. 28 (Jztx-11) subfamily.