ID CXDA_CONER STANDARD; PRT; 32 AA. AC P60513; DT 15-MAR-2004 (Rel. 43, Created) DT 15-MAR-2004 (Rel. 43, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) 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 SEQUENCE, SYNTHESIS, AND MASS SPECTROMETRY. RX PubMed=14615484; 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 RT in vertebrate neuronal Na+ channels but not in skeletal and cardiac RT muscles."; RL J. Biol. Chem. 279:4680-4685(2004). CC -!- FUNCTION: Delta-conotoxins bind to voltage-sensitive sodium CC channel (VSSC) and inhibit the inactivation process. This toxin CC inhibits sodium channel inactivation in neuronal membranes from CC amphibians and mammals (Nav1.2a, Nav1.3, and Nav1.6) upon binding CC to receptor site 6, without affecting rat skeletal muscle (Nav1.4) CC and human cardiac muscle (Nav1.5) sodium channels. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. CC -!- PTM: Exists in two forms, due to cis-trans isomerization at Leu- CC 12-Pro-13. CC -!- MASS SPECTROMETRY: MW=3288.3; METHOD=Electrospray. CC -!- SIMILARITY: Belongs to the conotoxin O-superfamily. Delta-type CC family. 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; 01-NOV-00. DR PDB; 1G1Z; 01-NOV-00. KW Toxin; Neurotoxin; Ionic channel inhibitor; Sodium channel inhibitor; KW Amidation; Hydroxylation; 3D-structure. FT DISULFID 3 21 FT DISULFID 10 25 FT DISULFID 20 29 FT MOD_RES 6 6 HYDROXYLATION. FT MOD_RES 32 32 AMIDATION. SQ SEQUENCE 32 AA; 3279 MW; 96C544273232D62D CRC64; DDCIKPYGFC SLPILKNGLC CSGACVGVCA DL //