ID   CA12_CONCB              Reviewed;          68 AA.
AC   P0C1W0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Alpha-conotoxin-like Ca1.2;
DE   Flags: Precursor;
OS   Conus caracteristicus (Characteristic cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=89440;
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}.
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   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1W0; -.
DR   ConoServer; 13; Ca1.2 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   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; Sulfation; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000249785"
FT   PEPTIDE         49..64
FT                   /note="Alpha-conotoxin-like Ca1.2"
FT                   /id="PRO_0000249786"
FT   PROPEP          65..68
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000249787"
FT   REGION          52..54
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         63
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   68 AA;  7326 MW;  618E8912BC5BE7AF CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRASEG RNAAAKDKAS DLVALTVRGC CAIRECRLQN
     AAYCGGIY