ID   CA12A_CONIM             Reviewed;          62 AA.
AC   Q9U619; A0A125S9D7;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Alpha-conotoxin-like ImIIA;
DE   AltName: Full=Conopeptide im003 {ECO:0000303|PubMed:30893765, ECO:0000312|EMBL:AAF12824.1};
DE   Flags: Precursor;
OS   Conus imperialis (Imperial cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=35631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhao D., Huang P.;
RT   "Conus imperialis conotoxin ImIIA precursor mRNA.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=30893765; DOI=10.3390/md17030177;
RA   Jin A.H., Dutertre S., Dutt M., Lavergne V., Jones A., Lewis R.J.,
RA   Alewood P.F.;
RT   "Transcriptomic-proteomic correlation in the predation-evoked venom of the
RT   cone snail, Conus imperialis.";
RL   Mar. Drugs 17:0-0(2019).
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 {ECO:0000269|PubMed:30893765}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30893765}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; AF200595; AAF12824.1; -; mRNA.
DR   EMBL; KT377397; AME17661.1; -; mRNA.
DR   AlphaFoldDB; Q9U619; -.
DR   ConoServer; 78; ImIIA 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..48
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000034879"
FT   PEPTIDE         49..61
FT                   /note="Alpha-conotoxin-like ImIIA"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000034880"
FT   MOD_RES         61
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
FT   DISULFID        52..61
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
SQ   SEQUENCE   62 AA;  6830 MW;  BF0D811758C3047D CRC64;
     MGMRMMFTVF LLVVLATAVL PVTLDRASDG RNAAANAKTP RLIAPFIRDY CCHRGPCMVW
     CG