O16B_CONCT
ID O16B_CONCT Reviewed; 25 AA.
AC P58918;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Omega-conotoxin CVIB {ECO:0000303|PubMed:10938268};
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 PROTEIN SEQUENCE, AMIDATION AT CYS-25, SYNTHESIS, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
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.
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 (Cav). This toxin blocks N-,
CC P- and Q-type calcium channels (PubMed:10938268). It shows high
CC activities on Cav2.1/CACNA1A (IC(50)=11 nM) and Cav2.2/CACNA1B
CC (IC(50)=7.7 nM) (PubMed:10938268). In addition, it shows a higher
CC potency when Cav2.2/CACNA1B is only expressed with the ancillary
CC subunit CACNB3 (IC(50)=1.6 nM) than on Cav2.2/CACNA1B expressed with
CC the ancillary subunits CACNA2D1 and CACNB3 (IC(50)=12 nM)
CC (PubMed:19892914). Both the Cav2.2/CACNA1B block by this toxin and the
CC recovery are voltage-independent (PubMed:19892914). It is noteworthy
CC that ancillary subunits beta do not modulate recovery from this toxin
CC block, since Cav2.2/CACNA1B expressed with either the ancillary subunit
CC CACNB2a (isoform 2a) or with CACNB3 exhibits moderate recovery
CC (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; P58918; -.
DR SMR; P58918; -.
DR ConoServer; 1726; CVIB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR012321; Conotoxin_omega-typ_CS.
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; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT PEPTIDE 1..25
FT /note="Omega-conotoxin CVIB"
FT /evidence="ECO:0000269|PubMed:10938268"
FT /id="PRO_0000044482"
FT MOD_RES 25
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:10938268"
FT DISULFID 1..16
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 8..20
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 15..25
FT /evidence="ECO:0000250|UniProtKB:P05484"
SQ SEQUENCE 25 AA; 2717 MW; D41A9E5F5AFA9552 CRC64;
CKGKGASCRK TMYDCCRGSC RSGRC
