ID   O16A_CONSC              Reviewed;          27 AA.
AC   P0DL67;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Delta-conotoxin SuVIA {ECO:0000303|PubMed:26156767};
DE            Short=Delta-SuVIA {ECO:0000303|PubMed:26156767};
OS   Conus suturatus (Sutured cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Tesselliconus.
OX   NCBI_TaxID=1519877;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=26156767; DOI=10.1098/rspb.2015.0817;
RA   Jin A.H., Israel M.R., Inserra M.C., Smith J.J., Lewis R.J., Alewood P.F.,
RA   Vetter I., Dutertre S.;
RT   "Delta-conotoxin SuVIA suggests an evolutionary link between ancestral
RT   predator defence and the origin of fish-hunting behaviour in carnivorous
RT   cone snails.";
RL   Proc. R. Soc. B 282:1-7(2015).
CC   -!- FUNCTION: This toxin activates voltage-gated sodium channels
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)). It
CC       shifts the voltage-dependence of activation to more hyperpolarized
CC       potentials but has only little effect on channel inactivation. In vivo,
CC       it induces nocifensive or pain-like behaviors in mice when injected
CC       intraplantarly. This is coherent with the specific defensive role
CC       deduced from its proximal position in the venom gland.
CC       {ECO:0000269|PubMed:26156767}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26156767}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct, in the proximal part
CC       (indicative of a defensive role). {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC       {ECO:0000250|UniProtKB:P0DL66}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60513}.
CC   -!- MASS SPECTROMETRY: Mass=2741.16; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:26156767};
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL67; -.
DR   SMR; P0DL67; -.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..27
FT                   /note="Delta-conotoxin SuVIA"
FT                   /evidence="ECO:0000269|PubMed:26156767"
FT                   /id="PRO_0000439827"
FT   DISULFID        1..17
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
FT   DISULFID        16..25
FT                   /evidence="ECO:0000250|UniProtKB:P60513"
SQ   SEQUENCE   27 AA;  2749 MW;  4ED9DEF2FBB14BBA CRC64;
     CAGIGSFCGL PGLVDCCSDR CFIVCLP