O16A_CONCT
ID O16A_CONCT Reviewed; 71 AA.
AC P58917;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Omega-conotoxin CVIA {ECO:0000303|PubMed:10938268};
DE Flags: Precursor;
OS Conus catus (Cat cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=101291;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-70, AMIDATION AT CYS-70,
RP SYNTHESIS OF 46-70, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=10938268; DOI=10.1074/jbc.m002252200;
RA Lewis R.J., Nielsen K.J., Craik D.J., Loughnan M.L., Adams D.A.,
RA Sharpe I.A., Luchian T., Adams D.J., Bond T., Thomas L., Jones A.,
RA Matheson J.-L., Drinkwater R., Andrews P.R., Alewood P.F.;
RT "Novel omega-conotoxins from Conus catus discriminate among neuronal
RT calcium channel subtypes.";
RL J. Biol. Chem. 275:35335-35344(2000).
RN [2]
RP FUNCTION, AND SYNTHESIS OF 46-70.
RX PubMed=19892914; DOI=10.1124/mol.109.058834;
RA Berecki G., Motin L., Haythornthwaite A., Vink S., Bansal P.,
RA Drinkwater R., Wang C.I., Moretta M., Lewis R.J., Alewood P.F.,
RA Christie M.J., Adams D.J.;
RT "Analgesic (omega)-conotoxins CVIE and CVIF selectively and voltage-
RT dependently block recombinant and native N-type calcium channels.";
RL Mol. Pharmacol. 77:139-148(2010).
RN [3]
RP ERRATUM OF PUBMED:19892914.
RX DOI=10.1124/mol.80.2.356;
RA Berecki G., Motin L., Haythornthwaite A., Vink S., Bansal P.,
RA Drinkwater R., Wang C.I., Moretta M., Lewis R.J., Alewood P.F.,
RA Christie M.J., Adams D.J.;
RT "Correction to 'Analgesic omega-Conotoxins CVIE and CVIF Selectively and
RT Voltage-Dependently Block Recombinant and Native N-Type Calcium
RT Channels'.";
RL Mol. Pharmacol. 80:356-356(2011).
CC -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC block voltage-gated calcium channels. This toxin blocks N-type calcium
CC channels (Cav2.2/CACNA1B) (PubMed:10938268). Shows a weak voltage-
CC dependent reversibility (PubMed:19892914). It is noteworthy that
CC ancillary subunits beta modulate recovery from this toxin block
CC (PubMed:19892914). Cav2.2/CACNA1B expressed with the ancillary subunit
CC CACNB2a (isoform 2a) shows a low recovery from this toxin block,
CC whereas Cav2.2/CACNA1B expressed with CACNB3 does not exhibit recovery
CC at all (PubMed:19892914). {ECO:0000269|PubMed:10938268,
CC ECO:0000269|PubMed:19892914}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10938268}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:10938268}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P05484}.
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}.
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DR AlphaFoldDB; P58917; -.
DR SMR; P58917; -.
DR ConoServer; 1597; CVIA precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR InterPro; IPR004214; Conotoxin.
DR InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /evidence="ECO:0000269|PubMed:10938268"
FT /id="PRO_0000034962"
FT PEPTIDE 46..70
FT /note="Omega-conotoxin CVIA"
FT /evidence="ECO:0000269|PubMed:10938268"
FT /id="PRO_0000034963"
FT MOD_RES 70
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:10938268"
FT DISULFID 46..61
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 53..65
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 60..70
FT /evidence="ECO:0000250|UniProtKB:P05484"
SQ SEQUENCE 71 AA; 7665 MW; B99D9C7C74996D01 CRC64;
MKLTCVVIVA MLLLTACQLI TANDSRGTQK HRALRSDTKL SMSTRCKSTG ASCRRTSYDC
CTGSCRSGRC G
