ID   CA120_CONBU             Reviewed;          66 AA.
AC   P0CY88;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Conotoxin Bu1.4;
DE   AltName: Full=Bu1.3;
DE   AltName: Full=Conotoxin Bu20;
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 [GENOMIC DNA] OF 8-66.
RA   Watkins M., Olivera B.M., Hillyard D.R., McIntosh J.M., Jones R.M.;
RT   "Alpha-conotoxin peptides.";
RL   Patent number US6797808, 28-SEP-2004.
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 8-66.
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   [4]
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/4 pattern.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   -!- CAUTION: There is a discrepancy in nomenclature: was submitted as Bu1.4
CC       in PubMed:20143226 but is named Bu1.3 in ConoServer. {ECO:0000305}.
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DR   EMBL; AR584845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FB299974; CAR81558.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P0CY88; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409992"
FT   PEPTIDE         47..63
FT                   /note="Conotoxin Bu1.4"
FT                   /id="PRO_0000409993"
FT   REGION          25..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         63
FT                   /note="Threonine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000250|UniProtKB:P69657"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250|UniProtKB:P69657"
FT   CONFLICT        19
FT                   /note="N -> T (in Ref. 2; AR584845 and 3; CAR81558)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   66 AA;  7460 MW;  E3F5D8B3280C0C02 CRC64;
     MGMRMRMMFT VFLLVVLANT VVSFPSDRDS DGADAEASDE PVEFERDENG CCWNPSCPRP
     RCTGRR