ID   CA13_CONVC              Reviewed;          64 AA.
AC   E2DIH6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Conotoxin Vc1.3;
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], SYNTHESIS OF 45-60, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo, and Venom duct;
RX   PubMed=21504902; DOI=10.1074/jbc.m110.217703;
RA   Safavi-Hemami H., Siero W.A., Kuang Z., Williamson N.A., Karas J.A.,
RA   Page L.R., Macmillan D., Callaghan B., Kompella S.N., Adams D.J.,
RA   Norton R.S., Purcell A.W.;
RT   "Embryonic toxin expression in the cone snail Conus victoriae: primed to
RT   kill or divergent function?";
RL   J. Biol. Chem. 286:22546-22557(2011).
CC   -!- FUNCTION: May act as a toxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21504902}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:21504902}.
CC   -!- DEVELOPMENTAL STAGE: Mostly expressed in embryos. Also slightly
CC       expressed in adults, but the toxin is not found in adult venom.
CC       {ECO:0000269|PubMed:21504902}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not show activity on alpha-3/beta-2
CC       (CHRNA3/CHRNB2), alpha-7 (CHRNA7), alpha-9/alpha-10 (CHRNA9/CHRNA10),
CC       alpha-3/beta-4 (CHRNA3/CHRNB4), alpha-4/beta-2 (CHRNA4/CHRNB2) and
CC       alpha-4/beta-4 (CHRNA4/CHRNB4) acetylcholine receptors. Does not show
CC       inhibition on high-voltage activated (HVA) calcium channels currents
CC       that are mediated by GABA-B receptors. {ECO:0000305|PubMed:21504902}.
CC   -!- SIMILARITY: Belongs to the conotoxin A 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   EMBL; GU046309; ADC80510.1; -; mRNA.
DR   AlphaFoldDB; E2DIH6; -.
DR   ConoServer; 4201; Vc1.3 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..43
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425161"
FT   PEPTIDE         45..60
FT                   /note="Conotoxin Vc1.3"
FT                   /id="PRO_0000425162"
FT   MOD_RES         60
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   64 AA;  6896 MW;  F633B76797CF432E CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRASDG RKAAASDLIT LTIKGCCSDP PCIANNPDLC
     GRRR