ID   O16A_CONEB              Reviewed;          31 AA.
AC   A0A0F6QDA5;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Delta-conotoxin-like ErVIA {ECO:0000303|PubMed:25848010};
DE   Flags: Precursor; Fragment;
OS   Conus eburneus (Ivory cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Tesselliconus.
OX   NCBI_TaxID=101300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 5-31, IDENTIFICATION
RP   BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=25848010; DOI=10.1073/pnas.1424435112;
RA   Aman J.W., Imperial J.S., Ueberheide B., Zhang M.M., Aguilar M., Taylor D.,
RA   Watkins M., Yoshikami D., Showers-Corneli P., Safavi-Hemami H., Biggs J.,
RA   Teichert R.W., Olivera B.M.;
RT   "Insights into the origins of fish hunting in venomous cone snails from
RT   studies of Conus tessulatus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:5087-5092(2015).
CC   -!- FUNCTION: This toxin activates voltage-gated sodium channels. It shifts
CC       the voltage-dependence of activation to more hyperpolarized potentials
CC       but has only little effect on channel inactivation. It is active on
CC       Nav1.3/SCN3A (EC(50)=3.98 nM), Nav1.4/SCN4A (EC(50)=4.99 nM),
CC       Nav1.6/SCN8A (EC(50)=1.27 nM) and Nav1.7/SCN9A (EC(50)=2.42 nM)
CC       voltage-gated sodium channels. In vivo, it induces nocifensive or pain-
CC       like behaviors in mice when injected intraplantarly.
CC       {ECO:0000250|UniProtKB:P0DL67}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25848010}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:25848010}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60513}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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   EMBL; KR013220; AKD43185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F6QDA5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   PROPEP          <1..4
FT                   /id="PRO_0000439828"
FT   PEPTIDE         5..31
FT                   /note="Delta-conotoxin-like ErVIA"
FT                   /evidence="ECO:0000269|PubMed:25848010"
FT                   /id="PRO_0000439829"
FT   DISULFID        5..21
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
FT   DISULFID        12..25
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
FT   DISULFID        20..29
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
FT   NON_TER         1
SQ   SEQUENCE   31 AA;  3203 MW;  9E56DEA5913D1CD0 CRC64;
     LNKRCAGIGS FCGLPGLVDC CSGRCFIVCL P