CA1A_CONTI
ID CA1A_CONTI Reviewed; 16 AA.
AC P0CI05;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Alpha-conotoxin CtIA {ECO:0000303|PubMed:20933537};
OS Conus tinianus (Variable cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Floraconus.
OX NCBI_TaxID=909294;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, SULFATION AT TYR-15,
RP AMIDATION AT CYS-16, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=20933537; DOI=10.1016/j.toxicon.2010.09.009;
RA Kauferstein S., Porth C., Kendel Y., Wunder C., Nicke A., Kordis D.,
RA Favreau P., Koua D., Stocklin R., Mebs D.;
RT "Venomic study on cone snails (Conus spp.) from South Africa.";
RL Toxicon 57:28-34(2011).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin is an antagonist of all rat neuronal alpha-3-beta-2/CHRNA3-
CC CHRNB2, alpha-4-beta-2/CHRNA4-CHRNB2 and alpha-7/CHRNA7 nAChR subtypes.
CC {ECO:0000269|PubMed:20933537}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20933537}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:20933537}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/6 pattern.
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1742.44; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20933537};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CI05; -.
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.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Amidation;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Sulfation; Toxin.
FT PEPTIDE 1..16
FT /note="Alpha-conotoxin CtIA"
FT /id="PRO_0000402137"
FT MOD_RES 15
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:20933537"
FT MOD_RES 16
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:20933537"
FT DISULFID 3..9
FT /evidence="ECO:0000250|UniProtKB:K8DWB5"
FT DISULFID 4..16
FT /evidence="ECO:0000250|UniProtKB:K8DWB5"
SQ SEQUENCE 16 AA; 1669 MW; 5DBB1199E9998E12 CRC64;
GGCCSHPACQ NNPDYC
