ID   CA12_CONBN              Reviewed;          18 AA.
AC   P0CE74; P0C1Y1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Alpha-conotoxin-like Bn1.2;
DE   Flags: Precursor; Fragment;
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].
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: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). Has possibly a distinct nAChR binding mode from other
CC       alpha-conotoxins, due to a different three residue motif (lacks the
CC       Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:14701840}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:14701840}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CE74; -.
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   2: Evidence at transcript level;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PROPEP          <1..1
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000392690"
FT   PEPTIDE         2..17
FT                   /note="Alpha-conotoxin-like Bn1.2"
FT                   /id="PRO_0000392691"
FT   REGION          5..7
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         17
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..9
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        4..17
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   NON_TER         1
SQ   SEQUENCE   18 AA;  1951 MW;  7CC4B27B4C49A37F CRC64;
     KECCTHPACH VSHPELCG