ID   O163_CONVR              Reviewed;          79 AA.
AC   Q5K0C5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Conotoxin Vi6.3 {ECO:0000305};
DE   AltName: Full=virgo 10 {ECO:0000303|PubMed:15652641};
DE   Flags: Precursor;
OS   Conus virgo (Virgin cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX   NCBI_TaxID=89427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=15652641; DOI=10.1016/j.peptides.2004.10.027;
RA   Kauferstein S., Melaun C., Mebs D.;
RT   "Direct cDNA cloning of novel conopeptide precursors of the O-
RT   superfamily.";
RL   Peptides 26:361-367(2005).
CC   -!- FUNCTION: Ion channel inhibitor that inhibits the increase in
CC       intracellular calcium upon depolarization in DRG neurons. In vivo, both
CC       intraperitoneal and intracranial injections into mice induce
CC       hyperactivity. {ECO:0000250|UniProtKB:Q5K0C7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15652641}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:15652641}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
CC   -!- CAUTION: There is a sequence conflict at position 79 between the
CC       sequence from NCBI (CAH64856; Leu) and the sequence shown in fig.1
CC       (Pro) of Kauferstein et al., 2005. {ECO:0000305|PubMed:15652641}.
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DR   EMBL; AJ851183; CAH64856.1; -; mRNA.
DR   AlphaFoldDB; Q5K0C5; -.
DR   SMR; Q5K0C5; -.
DR   ConoServer; 1072; Vi6.3 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Knottin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..47
FT                   /evidence="ECO:0000250|UniProtKB:Q5K0C7"
FT                   /id="PRO_0000034999"
FT   PEPTIDE         48..79
FT                   /note="Conotoxin Vi6.3"
FT                   /evidence="ECO:0000250|UniProtKB:Q5K0C7"
FT                   /id="PRO_0000035000"
FT   MOD_RES         60
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q5K0C7"
FT   MOD_RES         63
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q5K0C7"
FT   DISULFID        49..62
FT                   /evidence="ECO:0000250|UniProtKB:P60179"
FT   DISULFID        56..67
FT                   /evidence="ECO:0000250|UniProtKB:P60179"
FT   DISULFID        61..77
FT                   /evidence="ECO:0000250|UniProtKB:P60179"
SQ   SEQUENCE   79 AA;  8508 MW;  4C89477A6E0E5C50 CRC64;
     MKLTCVLIIT VLFLTASQLI TADYSRDQRQ YRAVRLGDEM RNFKGARDCG GQGEGCYTQP
     CCPGLRCRGG GTGGGACQL