ID   CA1C_CONCN              Reviewed;          64 AA.
AC   P0C8U4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Alpha-conotoxin CnIC;
DE   Contains:
DE     RecName: Full=Alpha-conotoxin CnIF;
DE   Contains:
DE     RecName: Full=Alpha-conotoxin CnIH;
DE     AltName: Full=Alpha-conotoxin-like Cn1.1;
DE     AltName: Full=[Asp1]-CnIH;
DE   Flags: Precursor;
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEAMIDATION AT ASN-48, AMIDATION AT CYS-62,
RP   MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-64, AND REVIEW.
RC   TISSUE=Venom duct;
RX   PubMed=16905531; DOI=10.1074/jbc.r600020200;
RA   Olivera B.M.;
RT   "Conus peptides: biodiversity-based discovery and exogenomics.";
RL   J. Biol. Chem. 281:31173-31177(2006).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC   -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIC]: Mass=1286.48;
CC       Method=Electrospray; Note=CnIC.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIF]: Mass=1499.58;
CC       Method=Electrospray; Note=CnIF.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIH]: Mass=1613.64;
CC       Method=Electrospray; Note=CnIH.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIH]: Mass=1614.63;
CC       Method=Electrospray; Note=Deamidated CnIH.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C8U4; -.
DR   ConoServer; 3711; CnIH precursor.
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   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..47
FT                   /id="PRO_0000366054"
FT   PEPTIDE         48..62
FT                   /note="Alpha-conotoxin CnIH"
FT                   /id="PRO_0000366055"
FT   PEPTIDE         49..62
FT                   /note="Alpha-conotoxin CnIF"
FT                   /id="PRO_0000419826"
FT   PEPTIDE         51..62
FT                   /note="Alpha-conotoxin CnIC"
FT                   /id="PRO_0000419827"
FT   MOD_RES         48
FT                   /note="Deamidated asparagine; in CnIH; partial"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT   DISULFID        51..56
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   CONFLICT        10
FT                   /note="F -> G (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   64 AA;  7209 MW;  6EF718D09A422F7F CRC64;
     MGMRMMFTVF LLVVLTTTVV SFPSDSASDV RDDEAKDERS DMYKSKRNGR CCHPACGKHF
     SCGR