ID   O16A_CONNI              Reviewed;          31 AA.
AC   P56710;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Delta-conotoxin NgVIA;
OS   Conus nigropunctatus (Black-spot cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=1520089;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-6 AND PRO-14, AND SYNTHESIS.
RC   TISSUE=Venom;
RX   PubMed=7836370; DOI=10.1074/jbc.270.3.1123;
RA   Fainzilber M., Lodder J.C., Kits K.S., Kofman O., Vinnitsky I.,
RA   Van Rietschoten J., Zlotkin E., Gordon D.;
RT   "A new conotoxin affecting sodium current inactivation interacts with the
RT   delta-conotoxin receptor site.";
RL   J. Biol. Chem. 270:1123-1129(1995).
CC   -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC       channels (Nav) and inhibit the inactivation process. Potent paralytic
CC       toxin in vertebrate and invertebrate systems. Its binding appears to be
CC       voltage-dependent.
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. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
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   PIR; A55430; A55430.
DR   AlphaFoldDB; P56710; -.
DR   SMR; P56710; -.
DR   ConoServer; 1519; NgVIA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012322; Conotoxin_d-typ_CS.
DR   PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..31
FT                   /note="Delta-conotoxin NgVIA"
FT                   /id="PRO_0000044873"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:7836370"
FT   MOD_RES         14
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:7836370"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..27
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   31 AA;  3368 MW;  8387385C693118D1 CRC64;
     SKCFSPGTFC GIKPGLCCSV RCFSLFCISF E