ID   CA1C_CONCT              Reviewed;          21 AA.
AC   P0DQQ5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=Alpha-conotoxin CIC {ECO:0000303|PubMed:33801301};
DE   AltName: Full=C1.1 {ECO:0000305};
DE   AltName: Full=Ca001 {ECO:0000303|PubMed:26322961};
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=26322961; DOI=10.1021/acs.jproteome.5b00630;
RA   Himaya S.W., Jin A.H., Dutertre S., Giacomotto J., Mohialdeen H.,
RA   Vetter I., Alewood P.F., Lewis R.J.;
RT   "Comparative venomics reveals the complex prey capture strategy of the
RT   piscivorous cone snail Conus catus.";
RL   J. Proteome Res. 14:4372-4381(2015).
RN   [2]
RP   FUNCTION, SYNTHESIS OF 1-21 AND 7-21, MUTAGENESIS OF 1-ALA--THR-16, AND
RP   STRUCTURE BY NMR.
RX   PubMed=33801301; DOI=10.3390/md19030141;
RA   Giribaldi J., Haufe Y., Evans E.R.J., Wilson D.T., Daly N.L., Enjalbal C.,
RA   Nicke A., Dutertre S.;
RT   "Synthesis, structural and pharmacological characterizations of CIC, a
RT   novel alpha-conotoxin with an extended N-terminal tail.";
RL   Mar. Drugs 19:0-0(2021).
CC   -!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
CC       receptors (nAChR) and inhibit them. This toxin selectively inhibits
CC       alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=3.51 uM) and alpha-6/alpha-3-beta-
CC       2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC(50)=0.94 uM) nAChRs.
CC       {ECO:0000269|PubMed:33801301}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26322961}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:26322961}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The 6 amino-acid N-terminal tail displays a well-defined
CC       structure and plays a role in stabilizing the peptide.
CC       {ECO:0000305|PubMed:33801301}.
CC   -!- MISCELLANEOUS: Does not show inhibition on rat alpha-7/CHRNA7, alpha-4-
CC       beta-2/CHRNA4-CHRNB2, alpha-4-beta-4/CHRNA4-CHRNB4, alpha-3-beta-
CC       4/CHRNA3-CHRNB4, alpha-2-beta-2/CHRNA2-CHRNB2, alpha-2-beta-4/CHRNA2-
CC       CHRNB4, and alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND
CC       acetylcholine receptors, as well as on human alpha-9-alpha-10/CHRNA9-
CC       CHRNA10 subtype. {ECO:0000269|PubMed:33801301}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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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   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..21
FT                   /note="Alpha-conotoxin CIC"
FT                   /evidence="ECO:0000269|PubMed:26322961"
FT                   /id="PRO_0000453219"
FT   REGION          9..11
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        7..13
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MUTAGEN         1..6
FT                   /note="Missing: No or small decrease in ability to inhibit
FT                   alpha-3-beta-2/CHRNA3-CHRNB2 and alpha-6/alpha-3-beta-2-
FT                   beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) nAChR."
FT                   /evidence="ECO:0000269|PubMed:33801301"
SQ   SEQUENCE   21 AA;  2110 MW;  BE6EDE3C20EC6F19 CRC64;
     ASGADTCCSN PACQVQHSDL C