ID   O16D_CONCN              Reviewed;          32 AA.
AC   P0CC15;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Delta-conotoxin-like CnVID {ECO:0000303|PubMed:19457347, ECO:0000303|PubMed:25352593};
DE            Short=Delta-CnVID {ECO:0000303|PubMed:19457347, ECO:0000303|PubMed:25352593};
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-6 AND PRO-14, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RA   Favreau P.;
RT   "Physico-chemical and pharmacological study of new toxins from the
RT   piscivorous cone snail Conus consors.";
RL   Thesis (1999), University of La Rochelle, France.
RN   [2]
RP   SEQUENCE REVISION TO 25.
RA   Biass D., Favreau P.;
RL   Unpublished observations (MAY-2011).
RN   [3]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, AND DISULFIDE
RP   BOND.
RC   TISSUE=Venom;
RX   PubMed=25352593; DOI=10.1074/jbc.m114.610436;
RA   Peigneur S., Paolini-Bertrand M., Gaertner H., Biass D., Violette A.,
RA   Stoecklin R., Favreau P., Tytgat J., Hartley O.;
RT   "Delta-conotoxins synthesized using an acid-cleavable solubility tag
RT   approach reveal key structural determinants for NaV subtype selectivity.";
RL   J. Biol. Chem. 289:35341-35350(2014).
RN   [4]
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=19457347; DOI=10.1016/j.jprot.2009.01.019;
RA   Biass D., Dutertre S., Gerbault A., Menou J.L., Offord R., Favreau P.,
RA   Stocklin R.;
RT   "Comparative proteomic study of the venom of the piscivorous cone snail
RT   Conus consors.";
RL   J. Proteomics 72:210-218(2009).
CC   -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC       channels (Nav) and inhibit the inactivation process. This toxin acts on
CC       Nav1.2/SCN2A, Nav1.3/SCN3A and Nav1.6/SCN8A (EC(50)=1.7 uM).
CC       {ECO:0000269|PubMed:25352593}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19457347}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:19457347}.
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). {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3539.41; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:19457347};
CC   -!- MASS SPECTROMETRY: Mass=3539.45; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:25352593};
CC   -!- MISCELLANEOUS: Found in the dissected venom (DV), but not in the
CC       injectable (milked) venom (IV). {ECO:0000305|PubMed:19457347}.
CC   -!- MISCELLANEOUS: Does not have activity on rNav1.4/SCN4A, hNav1.5/SCN5A,
CC       Nav1.7/SCN9A, rNav1.8/SCN10A, DmNav1/para, Kv1.1/KCNA1, Kv1.3/KCNA3,
CC       Kv1.4/KCNA4, Kv1.5/KCNA5, Kv11.1/ERG1/HERG and shaker.
CC       {ECO:0000269|PubMed:25352593}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CC15; -.
DR   SMR; P0CC15; -.
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; Hydroxylation;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..32
FT                   /note="Delta-conotoxin-like CnVID"
FT                   /id="PRO_0000390925"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|Ref.1"
FT   MOD_RES         14
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|Ref.1"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000269|PubMed:25352593"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000269|PubMed:25352593"
FT   DISULFID        17..27
FT                   /evidence="ECO:0000269|PubMed:25352593"
SQ   SEQUENCE   32 AA;  3516 MW;  0D5D99D84539EFEE CRC64;
     DECFSPGTFC GFKPGLCCSA RCFSLFCISL EF