CA12A_CONER
ID CA12A_CONER Reviewed; 61 AA.
AC D4HRK4; D4HRK5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Alpha-conotoxin EIIA;
DE Flags: Precursor;
OS Conus ermineus (Agate cone) (Chelyconus ermineus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX NCBI_TaxID=55423;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Venom duct;
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 PROTEIN SEQUENCE OF 43-58, IDENTIFICATION BY MASS SPECTROMETRY, SYNTHESIS
RP OF 43-58, FUNCTION, SUBCELLULAR LOCATION, PYROGLUTAMATE FORMATION AT
RP GLN-43, HYDROXYLATION AT PRO-45, AND AMIDATION AT CYS-58.
RC TISSUE=Venom;
RX PubMed=23584713; DOI=10.1007/s00216-013-6926-x;
RA Quinton L., Servent D., Girard E., Molgo J., Le Caer J.P., Malosse C.,
RA Haidar E.A., Lecoq A., Gilles N., Chamot-Rooke J.;
RT "Identification and functional characterization of a novel alpha-conotoxin
RT (EIIA) from Conus ermineus.";
RL Anal. Bioanal. Chem. 405:5341-5351(2013).
RN [3]
RP PROTEIN SEQUENCE OF 43-58, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
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 bind to the nicotinic acetylcholine
CC receptors (nAChR) and inhibit them. This peptide potently blocks
CC muscular nicotinic acetylcholine receptor (CHRNA1-CHRNB1-CHRNG-CHRND),
CC and has no effect on neuronal receptors. It is able to totally displace
CC [125I]-Bgtx from the Torpedo receptor with a complete inhibition in the
CC high micromolar range. It produces a biphasic inhibition curve which
CC fits nicely with a two-site model (Ki of 0.46 and 105 nM).
CC {ECO:0000269|PubMed:23584713}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23584713,
CC ECO:0000269|PubMed:28238803}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:20143226}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/4 pattern.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Has no effect on chimeric alpha-7 (CHRNA7), alpha-3-
CC beta-2 (CHRNA3-CHRNB2) and alpha-4-beta-2 (CHRNA4-CHRNB2).
CC {ECO:0000305|PubMed:23584713}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; FJ937346; ACZ37197.1; -; Genomic_DNA.
DR EMBL; FJ937347; ACZ37198.1; -; Genomic_DNA.
DR AlphaFoldDB; D4HRK4; -.
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;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydroxylation; Neurotoxin; Postsynaptic neurotoxin;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..40
FT /evidence="ECO:0000305|PubMed:23584713,
FT ECO:0000305|PubMed:28238803"
FT /id="PRO_0000422880"
FT PEPTIDE 43..58
FT /note="Alpha-conotoxin EIIA"
FT /evidence="ECO:0000269|PubMed:23584713,
FT ECO:0000269|PubMed:28238803"
FT /id="PRO_0000422881"
FT MOD_RES 43
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:23584713"
FT MOD_RES 45
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:23584713"
FT MOD_RES 58
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:23584713"
FT DISULFID 47..53
FT /evidence="ECO:0000250|UniProtKB:P69657"
FT DISULFID 48..58
FT /evidence="ECO:0000250|UniProtKB:P69657"
FT VARIANT 29
FT /note="A -> K"
SQ SEQUENCE 61 AA; 6779 MW; 39D49248B0825395 CRC64;
MFIVFLLVVL ATTVGSFTLD RVLEGRNAAA IDNALDQRDP KRQTPGCCWN PACVKNRCGR
R
