CA1A_CONCN
ID CA1A_CONCN Reviewed; 64 AA.
AC P56973;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Alpha-conotoxin CnIA;
DE Contains:
DE RecName: Full=Alpha-conotoxin CnIB;
DE Contains:
DE RecName: Full=Alpha-conotoxin CnIK;
DE AltName: Full=[Hyp7]-CnIK;
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], TISSUE SPECIFICITY, DOMAIN, HYDROXYLATION AT
RP PRO-54, AMIDATION AT CYS-62, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP 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 PROTEIN SEQUENCE OF 48-62, SYNTHESIS, CHARACTERIZATION, STRUCTURE BY NMR,
RP FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT CYS-62, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=10320362; DOI=10.1021/bi982817z;
RA Favreau P., Krimm I., le Gall F., Bobenrieth M.J., Lamthanh H., Bouet F.,
RA Servent D., Molgo J., Menez A., Letourneux Y., Lancelin J.-M.;
RT "Biochemical characterization and nuclear magnetic resonance structure of
RT novel alpha-conotoxins isolated from the venom of Conus consors.";
RL Biochemistry 38:6317-6326(1999).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28238803; DOI=10.1016/j.toxicon.2017.02.023;
RA Echterbille J., Gilles N., Araoz R., Mourier G., Amar M., Servent D.,
RA De Pauw E., Quinton L.;
RT "Discovery and characterization of EIIB, a new alpha-conotoxin from Conus
RT ermineus venom by nAChRs affinity capture monitored by MALDI-TOF/TOF mass
RT spectrometry.";
RL Toxicon 130:1-10(2017).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them
CC (PubMed:10320362, PubMed:28238803). CnIA and CnIB block muscular nAChR
CC alpha-1/gamma and alpha-1/delta subunits (PubMed:10320362).
CC {ECO:0000269|PubMed:10320362, ECO:0000269|PubMed:28238803}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10320362,
CC ECO:0000269|PubMed:22705119, ECO:0000269|PubMed:28238803}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:22705119}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIA]: Mass=1541.58;
CC Method=Electrospray; Note=CnIA.;
CC Evidence={ECO:0000269|PubMed:22705119};
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIB]: Mass=1328.47;
CC Method=Electrospray; Note=CnIB.;
CC Evidence={ECO:0000269|PubMed:22705119};
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIK]: Mass=1655.65;
CC Method=Electrospray; Note=CnIK.;
CC Evidence={ECO:0000269|PubMed:22705119};
CC -!- MASS SPECTROMETRY: [Alpha-conotoxin CnIK]: Mass=1671.63;
CC Method=Electrospray; Note=[Hyp]CnIK.;
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 PIR; A58963; A58963.
DR PDB; 1B45; NMR; -; A=49-62.
DR PDBsum; 1B45; -.
DR AlphaFoldDB; P56973; -.
DR SMR; P56973; -.
DR ConoServer; 1558; CnIA.
DR ConoServer; 594; CnIB.
DR EvolutionaryTrace; P56973; -.
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 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Direct protein sequencing; Disulfide bond; Hydroxylation;
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 /evidence="ECO:0000269|PubMed:10320362"
FT /id="PRO_0000419824"
FT PEPTIDE 48..62
FT /note="Alpha-conotoxin CnIK"
FT /id="PRO_0000419825"
FT PEPTIDE 49..62
FT /note="Alpha-conotoxin CnIA"
FT /id="PRO_0000034871"
FT PEPTIDE 51..62
FT /note="Alpha-conotoxin CnIB"
FT /id="PRO_0000034872"
FT MOD_RES 54
FT /note="4-hydroxyproline; in CnIK; partial"
FT /evidence="ECO:0000269|PubMed:22705119"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:10320362,
FT ECO:0000269|PubMed:22705119"
FT DISULFID 51..56
FT /evidence="ECO:0000269|PubMed:10320362"
FT DISULFID 52..62
FT /evidence="ECO:0000269|PubMed:10320362"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1B45"
SQ SEQUENCE 64 AA; 7192 MW; DAF703CA33783812 CRC64;
MGMRMMFTVF LLVVLTTTVV SFPSDSASDG RDDEAKDERS DIYESKRNGR CCHPACGKYY
SCGR
