ID   CA11_CONBU              Reviewed;          63 AA.
AC   P0CY86;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Alpha-conotoxin-like Bu1.1 {ECO:0000303|PubMed:20143226, ECO:0000303|PubMed:26948522, ECO:0000303|Ref.2};
DE   AltName: Full=Bu18 {ECO:0000303|PubMed:21266071};
DE   Flags: Precursor;
OS   Conus bullatus (Bubble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Textilia.
OX   NCBI_TaxID=89438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=21266071; DOI=10.1186/1471-2164-12-60;
RA   Hu H., Bandyopadhyay P.K., Olivera B.M., Yandell M.;
RT   "Characterization of the Conus bullatus genome and its venom-duct
RT   transcriptome.";
RL   BMC Genomics 12:60-60(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 6-63.
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   NOMENCLATURE.
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   [4]
RP   SYNTHESIS OF 48-62.
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|PubMed:26948522}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:26948522}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/4 pattern.
CC   -!- MISCELLANEOUS: Does not inhibits 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 shows the
CC       toxin without C-terminal amidation. {ECO:0000269|PubMed:26948522}.
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DR   EMBL; FB299970; CAR81556.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P0CY86; -.
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   Pfam; PF07365; Toxin_8; 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..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..47
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT                   /id="PRO_0000409988"
FT   PEPTIDE         48..62
FT                   /note="Alpha-conotoxin-like Bu1.1"
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT                   /id="PRO_0000409989"
FT   REGION          23..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000250|UniProtKB:P69657"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250|UniProtKB:P69657"
FT   CONFLICT        13
FT                   /note="I -> V (in Ref. 2; CAR81556)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   63 AA;  6789 MW;  9E4CFE75BE9FCA17 CRC64;
     MGMRMMFTVF LLIVLATTVV SFSTDDESDG SNEEPSADQT ARSSMNRAPG CCNNPACVKH
     RCG