CA1A_CONCT
ID CA1A_CONCT Reviewed; 59 AA.
AC D4HPD6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Alpha-conotoxin CIA {ECO:0000303|PubMed:29857567};
DE AltName: Full=Cl {ECO:0000303|PubMed:20143226};
DE Flags: Precursor;
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 [GENOMIC DNA].
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, TOXIC DOSE, SYNTHESIS OF 43-57, AND STRUCTURE BY NMR OF
RP 43-57.
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 the rat muscle nAChRs alpha-1-beta-1-gamma-delta
CC (CHRNA1-CHRNB1-CHRNG-CHRND) (IC(50)=5.7 nM) and the rat neuronal nAChR
CC alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=2060 nM) (PubMed:29857567). In
CC vivo, intramuscular injection into zebrafish produces rapid flaccid
CC paralysis (PubMed:29857567). {ECO:0000269|PubMed:29857567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20143226}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:20143226}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC {ECO:0000305}.
CC -!- TOXIC DOSE: PD(50) is 110 ug/kg into zebrafish.
CC {ECO:0000269|PubMed:29857567}.
CC -!- MISCELLANEOUS: This toxin does not show effect on neuronal nAChR alpha-
CC 4-beta-2/CHRNA4-CHRNB2 and alpha-7/CHRNA7 (when tested at 10 uM).
CC {ECO:0000269|PubMed:29857567}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ868069; ACZ49755.1; -; Genomic_DNA.
DR AlphaFoldDB; D4HPD6; -.
DR ConoServer; 3926; C4.3 precursor.
DR ConoServer; 8016; CIA.
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;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..42
FT /evidence="ECO:0000250"
FT /id="PRO_0000420720"
FT PEPTIDE 43..57
FT /note="Alpha-conotoxin CIA"
FT /evidence="ECO:0000305|PubMed:29857567"
FT /id="PRO_0000420721"
FT MOD_RES 57
FT /note="Cysteine amide"
FT /evidence="ECO:0000250|UniProtKB:P0C8U4"
FT DISULFID 46..51
FT /evidence="ECO:0000250|UniProtKB:P56973"
FT DISULFID 47..57
FT /evidence="ECO:0000250|UniProtKB:P56973"
SQ SEQUENCE 59 AA; 6642 MW; D9579431C4ED69DA CRC64;
MFTVFLLVVL TITVVSFPSD RASDGRDDEA KDERSDMYKS KRNGRCCHPA CGKHFSCGR
