ID   CT5C_CONVC              Reviewed;          54 AA.
AC   P69766;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Conotoxin vc5c {ECO:0000303|PubMed:16574181};
DE   AltName: Full=Vc5.2 {ECO:0000303|PubMed:15170751};
DE   Flags: Precursor; Fragment;
OS   Conus victoriae (Queen Victoria cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=319920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=15170751; DOI=10.1002/jms.624;
RA   Jakubowski J.A., Keays D.A., Kelley W.P., Sandall D.W., Bingham J.-P.,
RA   Livett B.G., Gayler K.R., Sweedler J.V.;
RT   "Determining sequences and post-translational modifications of novel
RT   conotoxins in Conus victoriae using cDNA sequencing and mass
RT   spectrometry.";
RL   J. Mass Spectrom. 39:548-557(2004).
RN   [2]
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-50, BROMINATION AT TRP-51, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16574181; DOI=10.1016/j.toxicon.2006.01.021;
RA   Jakubowski J.A., Kelley W.P., Sweedler J.V.;
RT   "Screening for post-translational modifications in conotoxins using liquid
RT   chromatography/mass spectrometry: an important component of conotoxin
RT   discovery.";
RL   Toxicon 47:688-699(2006).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC).
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P69766; -.
DR   ConoServer; 1522; VcVC precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Bromination; Cleavage on pair of basic residues; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Secreted; Signal; Toxin.
FT   SIGNAL          <1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..43
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000035045"
FT   PEPTIDE         44..54
FT                   /note="Conotoxin vc5c"
FT                   /id="PRO_0000035046"
FT   MOD_RES         50
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:16574181"
FT   MOD_RES         51
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:16574181"
FT   NON_TER         1
SQ   SEQUENCE   54 AA;  6107 MW;  312189153AA57BD7 CRC64;
     VILLLLIASI PSDAVQLKTK DDMPLASFHG NARRTLQMLS NKRICCYPNE WCCD