ID CXD6A_CONER Reviewed; 32 AA. AC P60513; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 1. DT 11-SEP-2007, entry version 35. DE Delta-conotoxin EVIA (Delta-EVIA). OS Conus ermineus (Atlantic fish-hunting cone). OC Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; OC Apogastropoda; Caenogastropoda; Sorbeoconcha; Hypsogastropoda; OC Neogastropoda; Conoidea; Conidae; Conus. OX NCBI_TaxID=55423; RN [1] RP PROTEIN SEQUENCE, SYNTHESIS, AND MASS SPECTROMETRY. RX PubMed=14615484; DOI=10.1074/jbc.M309576200; RA Barbier J., Lamthanh H., Le Gall F., Favreau P., Benoit E., Chen H., RA Gilles N., Ilan N., Heinemann S.H., Gordon D., Menez A., Molgo J.; RT "A delta-conotoxin from Conus ermineus venom inhibits inactivation in RT vertebrate neuronal Na+ channels but not in skeletal and cardiac RT muscles."; RL J. Biol. Chem. 279:4680-4685(2004). RN [2] RP STRUCTURE BY NMR, DISULFIDE BONDS, EFFECT DOSE, SYNTHESIS, AND RP MUTAGENESIS OF PRO-13. RX PubMed=14976206; DOI=10.1074/jbc.M309594200; RA Volpon L., Lamthanh H., Barbier J., Gilles N., Molgo J., Menez A., RA Lancelin J.-M.; RT "NMR solution structures of delta-conotoxin EVIA from Conus ermineus RT that selectively acts on vertebrate neuronal Na+ channels."; RL J. Biol. Chem. 279:21356-21366(2004). CC -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium CC channels and inhibit the inactivation process. This toxin inhibits CC sodium channel inactivation in neuronal membranes from amphibians CC and mammals (Nav1.2a, Nav1.3 and Nav1.6) upon binding to receptor CC site 6, without affecting rat skeletal muscle (Nav1.4) and human CC cardiac muscle (Nav1.5) sodium channels. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin. CC -!- MASS SPECTROMETRY: MW=3288.3; METHOD=Electrospray; RANGE=1-32; CC NOTE=PubMed:14615484. CC -!- TOXIC DOSE: Dose that produces hyperactivity (ED(50)) is 1.8 CC pmol/g body mass (native toxin), 1.9 pmol/g body mass (synthetic CC toxin) and 3.9 pmol/g body mass (P13A mutant). CC -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization CC at Leu-12-Pro-13. CC -!- SIMILARITY: Belongs to the conotoxin O superfamily. Delta-type CC family. CC -!- CAUTION: Another delta-conotoxin was named EVIA in 2001, but this CC toxin was renamed EVIB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1G1P; NMR; A=1-32. DR PDB; 1G1Z; NMR; A=1-32. DR InterPro; IPR012322; Delta_conotoxin. DR PROSITE; PS60005; DELTA_CONOTOXIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Direct protein sequencing; Hydroxylation; KW Ionic channel inhibitor; Knottin; Neurotoxin; Secreted; KW Sodium channel inhibitor; Toxin. FT PEPTIDE 1 32 Delta-conotoxin EVIA. FT /FTId=PRO_0000044868. FT MOD_RES 6 6 4-hydroxyproline. FT MOD_RES 32 32 Leucine amide. FT DISULFID 3 21 FT DISULFID 10 25 FT DISULFID 20 29 FT MUTAGEN 13 13 P->A: 2-fold decrease of activity. Exists FT only as a trans isomer. FT STRAND 13 16 FT STRAND 25 29 SQ SEQUENCE 32 AA; 3279 MW; 96C544273232D62D CRC64; DDCIKPYGFC SLPILKNGLC CSGACVGVCA DL //