ID   O164_CONVC              Reviewed;          81 AA.
AC   P69761;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Omega-conotoxin-like Vc6.4;
DE   Flags: Precursor;
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).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels. Act on high voltage-activated
CC       (HVA) calcium currents in molluscan neurons (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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   AlphaFoldDB; P69761; -.
DR   SMR; P69761; -.
DR   ConoServer; 1426; Vc6.4 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   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..51
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000034972"
FT   PEPTIDE         53..81
FT                   /note="Omega-conotoxin-like Vc6.4"
FT                   /id="PRO_0000034973"
FT   DISULFID        55..72
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        62..76
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   81 AA;  8933 MW;  2E51F1F5A020F1E0 CRC64;
     MKLTCVMIVA VLFLTANTFV TAVPHSSNVL ENLYLKARHE MENPEASKLN TRYDCEPPGN
     FCGMIKVGPP CCSGWCFFAC A