ID   CA12_CONAJ              Reviewed;          64 AA.
AC   P0CB08; P0CB13;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Alpha-conotoxin-like Ai1.2 {ECO:0000303|PubMed:26948522};
DE   AltName: Full=Alpha-conotoxin-like 291 {ECO:0000303|Ref.1, ECO:0000303|Ref.2};
DE   Flags: Precursor;
OS   Conus ammiralis (Admiral cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=97188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Watkins M., Olivera B.M., Hillyard D.R., McIntosh M.J., Jones R.M.;
RL   Patent number US6797808, 28-SEP-2004.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Watkins M., Hillyard D.R., McIntosh M.J., Jones R.M., Olivera B.M.;
RT   "Alpha-conotoxin peptides.";
RL   Patent number EP1852440, 07-NOV-2007.
RN   [3]
RP   FUNCTION, AND SYNTHESIS OF 44-60.
RX   PubMed=26948522; DOI=10.1002/anie.201600297;
RA   Carstens B.B., Berecki G., Daniel J.T., Lee H.S., Jackson K.A., Tae H.S.,
RA   Sadeghi M., Castro J., O'Donnell T., Deiteren A., Brierley S.M.,
RA   Craik D.J., Adams D.J., Clark R.J.;
RT   "Structure-activity studies of cysteine-rich alpha-conotoxins that inhibit
RT   high-voltage-activated calcium channels via GABA(B) receptor activation
RT   reveal a minimal functional motif.";
RL   Angew. Chem. Int. Ed. 55:4692-4696(2016).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). {ECO:0000250|UniProtKB:P0CE73}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not inhibit high voltage-activated (HVA) calcium
CC       channel currents in rat DRG neurons (at 1 uM toxin) (PubMed:26948522).
CC       {ECO:0000269|PubMed:26948522}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   -!- CAUTION: The synthetic peptide described in PubMed:26948522 is one
CC       residue shorter than the mature sequence shown in this entry (44-60)
CC       (the Gly-61 is removed) and the Cys-60 is amidated.
CC       {ECO:0000269|PubMed:26948522}.
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DR   EMBL; AR584879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FB300121; CAR81592.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P0CB08; -.
DR   ConoServer; 347; Ai1.2 patent.
DR   ConoServer; 2945; Ai1.2 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   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..43
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380618"
FT   PEPTIDE         44..61
FT                   /note="Alpha-conotoxin-like Ai1.2"
FT                   /id="PRO_0000380619"
FT   REGION          48..50
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         61
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P85886"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   64 AA;  6854 MW;  D0233029E24D3A4F CRC64;
     MFTVFLLVVL ATTVVSSTSG RRAFRGRNAA AKASGLVGLT DRRPECCSDP RCNSTHPELC
     GGRR