CA1B_CONCT
ID CA1B_CONCT Reviewed; 41 AA.
AC P0DPT2;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Alpha-conotoxin CIB {ECO:0000303|PubMed:29857567};
DE AltName: Full=C1.2 {ECO:0000303|PubMed:20143226};
DE Flags: Precursor; Fragment;
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.
RX PubMed=20143226; DOI=10.1007/s00239-010-9321-7;
RA Puillandre N., Watkins M., Olivera B.M.;
RT "Evolution of conus peptide genes: duplication and positive selection in
RT the A-Superfamily.";
RL J. Mol. Evol. 70:190-202(2010).
RN [2]
RP FUNCTION, BIOASSAY, SYNTHESIS OF 22-37, AND STRUCTURE BY NMR OF 22-37.
RX PubMed=29857567; DOI=10.3390/toxins10060222;
RA Giribaldi J., Wilson D., Nicke A., El Hamdaoui Y., Laconde G.,
RA Faucherre A., Moha Ou Maati H., Daly N.L., Enjalbal C., Dutertre S.;
RT "Synthesis, structure and biological activity of CIA and CIB, two alpha-
RT conotoxins from the predation-evoked venom of Conus catus.";
RL Toxins 10:0-0(2018).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin blocks rat neuronal nAChR alpha-3-beta-2/CHRNA3-CHRNB2
CC (IC(50)=128.9 nM) and alpha-7/CHRNA7 (IC(50)=1511 nM)
CC (PubMed:29857567). In vivo, intramuscular injection into zebrafish does
CC not produce any effect on the locomotion of zebrafish
CC (PubMed:29857567). {ECO:0000269|PubMed:29857567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29857567}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:29857567}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: This toxin does not show effect on neuronal nAChR alpha-
CC 4-beta-2/CHRNA4-CHRNB2 and on muscular alpha-1-beta-1-gamma-delta
CC (CHRNA1-CHRNB1-CHRNG-CHRND) (when tested at 10 uM).
CC {ECO:0000269|PubMed:29857567}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; BD261484; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR AlphaFoldDB; P0DPT2; -.
DR ConoServer; 8017; CIB.
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 Pfam; PF07365; Toxin_8; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Toxin.
FT PROPEP <1..21
FT /evidence="ECO:0000305"
FT /id="PRO_0000446310"
FT PEPTIDE 22..37
FT /note="Alpha-conotoxin CIB"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT /id="PRO_0000446311"
FT REGION 25..27
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 37
FT /note="Cysteine amide"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 23..29
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 24..37
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT NON_TER 1
SQ SEQUENCE 41 AA; 4409 MW; 581BF338F33A3D8F CRC64;
SDGRNEAAND EASDVIELAL KGCCSNPVCH LEHPNACGRR R
