CA1C_CONGE
ID CA1C_CONGE Reviewed; 40 AA.
AC Q86RB2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Alpha-conotoxin GIC {ECO:0000303|PubMed:12114524, ECO:0000303|PubMed:14992691};
DE Flags: Precursor; Fragment;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SYNTHESIS OF 21-36, AMIDATION
RP AT CYS-36, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC TISSUE=Hepatopancreas;
RX PubMed=12114524; DOI=10.1074/jbc.m205102200;
RA McIntosh J.M., Dowell C., Watkins M., Garrett J.E., Yoshikami D.,
RA Olivera B.M.;
RT "Alpha-conotoxin GIC from Conus geographus, a novel peptide antagonist of
RT nicotinic acetylcholine receptors.";
RL J. Biol. Chem. 277:33610-33615(2002).
RN [2]
RP STRUCTURE BY NMR OF 21-36, SYNTHESIS OF 21-36, AMIDATION AT CYS-36, AND
RP DISULFIDE BONDS.
RX PubMed=14992691; DOI=10.1042/bj20031792;
RA Chi S.-W., Kim D.-H., Olivera B.M., McIntosh J.M., Han K.-H.;
RT "Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of
RT alpha3beta2 nicotinic acetylcholine receptors.";
RL Biochem. J. 380:347-352(2004).
CC -!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
CC receptors (nAChR) and inhibit them. This toxin reversibly blocks
CC neuronal nAChRs (alpha-3/beta-2 = alpha-6 or -3/beta-2 or -3 > alpha-
CC 3/beta-4 = alpha-4/beta-2). {ECO:0000269|PubMed:12114524}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1609.5; Method=LSI;
CC Evidence={ECO:0000269|PubMed:12114524};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; AF526267; AAO33169.1; -; Genomic_DNA.
DR PDB; 1UL2; NMR; -; A=21-36.
DR PDB; 5CO5; X-ray; 2.10 A; C/E/F/H/J=21-36.
DR PDBsum; 1UL2; -.
DR PDBsum; 5CO5; -.
DR AlphaFoldDB; Q86RB2; -.
DR SMR; Q86RB2; -.
DR TCDB; 8.B.32.1.7; the nicotinic acetylcholine receptor-targeting alpha-conotoxin (a-conotoxin) family.
DR ConoServer; 97; GIC precursor.
DR EvolutionaryTrace; Q86RB2; -.
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:0099106; F:ion channel regulator 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 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Toxin.
FT PROPEP <1..20
FT /id="PRO_0000034875"
FT PEPTIDE 21..36
FT /note="Alpha-conotoxin GIC"
FT /evidence="ECO:0000305|PubMed:12114524,
FT ECO:0000305|PubMed:14992691"
FT /id="PRO_0000034876"
FT REGION 24..26
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 36
FT /note="Cysteine amide"
FT /evidence="ECO:0000305|PubMed:12114524,
FT ECO:0000305|PubMed:14992691"
FT DISULFID 22..28
FT /evidence="ECO:0000305|PubMed:12114524,
FT ECO:0000305|PubMed:14992691"
FT DISULFID 23..36
FT /evidence="ECO:0000305|PubMed:12114524,
FT ECO:0000305|PubMed:14992691"
FT NON_TER 1
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5CO5"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:5CO5"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:5CO5"
SQ SEQUENCE 40 AA; 4246 MW; 14143320230CC89D CRC64;
SDGRNDAAKA FDLISSTVKK GCCSHPACAG NNQHICGRRR
