CAIB_CONGE
ID CAIB_CONGE Reviewed; 66 AA.
AC X5IGW1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 23-FEB-2022, entry version 22.
DE RecName: Full=Alpha-conotoxin GIB {ECO:0000303|PubMed:34062129};
DE Flags: Precursor;
OS Conus geographus (Geography cone) (Nubecula geographus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX NCBI_TaxID=6491;
RN [1] {ECO:0000312|EMBL:BAO65576.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=24662800; DOI=10.1038/ncomms4521;
RA Dutertre S., Jin A.-H., Vetter I., Hamilton B., Sunagar K., Lavergne V.,
RA Dutertre V., Fry B.G., Antunes A., Venter D.J., Alewood P.F., Lewis R.J.;
RT "Evolution of separate predation- and defence-evoked venoms in carnivorous
RT cone snails.";
RL Nat. Commun. 5:3521-3521(2014).
RN [2]
RP SYNTHESIS OF 50-64 AS GLOBULAR AND RIBBON ISOMER, FUNCTION, AND PROBABLE
RP AMIDATION AT GLY-64.
RX PubMed=34062129; DOI=10.1016/j.bcp.2021.114638;
RA Tae H.S., Gao B., Jin A.H., Alewood P.F., Adams D.J.;
RT "Globular and ribbon isomers of Conus geographus alpha-conotoxins
RT antagonize human nicotinic acetylcholine receptors.";
RL Biochem. Pharmacol. 190:114638-114638(2021).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC Both the globular (with C1-C3; C2-C4 disulfide pattern) and ribbon (C1-
CC C4; C2-C3) isomers reversibly inhibit human muscle-type alpha-1-beta-1-
CC delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE nAChRs (IC(50)=116 nM and
CC IC(50)=643 nM, respectively) (PubMed:34062129). Both isomers also
CC inhibit alpha-7/CHRNA7 and alpha-9-alpha-10/CHRNA9-CHRNA10 (IC(50)=1113
CC nM by globular isomer) nAChRs (PubMed:34062129).
CC {ECO:0000269|PubMed:34062129}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34062129}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:34062129}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Both the globular (with C1-C3; C2-C4 disulfide pattern)
CC and ribbon (C1-C4; C2-C3) isomers shows no or very weak activity on
CC alpha-3-beta-2/CHRNA3-CHRNB2, alpha-3-beta-4/CHRNA3-CHRNB4, and alpha-
CC 4-beta-2/CHRNA4-CHRNB2. {ECO:0000269|PubMed:34062129}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; AB910808; BAO65576.1; -; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR009958; Conotoxin_a-typ.
DR InterPro; IPR018072; Conotoxin_a-typ_CS.
DR Pfam; PF07365; Toxin_8; 1.
DR PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Amidation;
KW Cleavage on pair of basic residues; Disulfide bond; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /evidence="ECO:0000305|PubMed:34062129"
FT /id="PRO_0000454097"
FT PEPTIDE 50..64
FT /note="Alpha-conotoxin GIB"
FT /evidence="ECO:0000305|PubMed:34062129"
FT /id="PRO_5004957945"
FT MOD_RES 64
FT /note="Glycine amide"
FT /evidence="ECO:0000305|PubMed:34062129"
FT DISULFID 51..56
FT /evidence="ECO:0000250|UniProtKB:X5I9Y2"
FT DISULFID 52..62
FT /evidence="ECO:0000250|UniProtKB:X5I9Y2"
SQ SEQUENCE 66 AA; 7293 MW; 57C5AD26150E4BA6 CRC64;
MGMRMMFTVF LLVVLATTVV SFPSERASDG RDDTAKDEGS DMEKLVEKKE CCNPACGRHY
SCKGGR
