ID   CA13_CONBN              Reviewed;          62 AA.
AC   P0C1Y2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Alpha-conotoxin-like Bn1.3 {ECO:0000303|PubMed:14701840};
DE   Flags: Precursor;
OS   Conus bandanus (Banded marble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX   NCBI_TaxID=72279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 49-61.
RC   TISSUE=Venom duct;
RX   PubMed=14701840; DOI=10.1074/jbc.m309654200;
RA   Santos A.D., McIntosh J.M., Hillyard D.R., Cruz L.J., Olivera B.M.;
RT   "The A-superfamily of conotoxins: structural and functional divergence.";
RL   J. Biol. Chem. 279:17596-17606(2004).
CC   -!- FUNCTION: Does not show activity on the acetylcholine receptors tested.
CC       {ECO:0000269|PubMed:14701840}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: The synthetic peptide does not detectably affect any of
CC       the nAChR subtypes tested (alpha-2-beta-2, alpha-2-beta-4, alpha-3-
CC       beta-2, alpha-3-beta-3, alpha-3-beta-4, alpha-4-beta-2, alpha-4-beta-4,
CC       alpha-6-beta-2 and alpha-6-beta-3). {ECO:0000269|PubMed:14701840}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1Y2; -.
DR   ConoServer; 20; Bn1.3 precursor.
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   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   Pfam; PF07365; Toxin_8; 1.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   3: Inferred from homology;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000251234"
FT   PEPTIDE         49..61
FT                   /note="Alpha-conotoxin-like Bn1.3"
FT                   /id="PRO_0000251235"
FT   MOD_RES         61
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
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