ID   CA12_CONLE              Reviewed;          68 AA.
AC   Q6PTD4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Alpha-conotoxin-like Lp1.2 {ECO:0000312|EMBL:AAS93425.1};
DE   Flags: Precursor;
OS   Conus leopardus (Leopard cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lithoconus.
OX   NCBI_TaxID=101306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RA   Han Y.H., Wang Q., Jiang H., Chen J.S., Chi C.W.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       {ECO:0000250|UniProtKB:A0A068B0Z6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|Ref.1}.
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   EMBL; AY580322; AAS93425.1; -; mRNA.
DR   AlphaFoldDB; Q6PTD4; -.
DR   ConoServer; 120; Lp1.2 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; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..48
FT                   /evidence="ECO:0000250|UniProtKB:P85013"
FT                   /id="PRO_0000247845"
FT   PEPTIDE         49..64
FT                   /note="Alpha-conotoxin-like Lp1.2"
FT                   /evidence="ECO:0000250|UniProtKB:P85013"
FT                   /id="PRO_0000247846"
FT   PROPEP          65..68
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444874"
FT   REGION          52..54
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         64
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P85013"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   68 AA;  7266 MW;  EF271E9FF94C6CBE CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRAFDG RNAAASDKAS DLISLAVRGC CSHPACSVNN
     PYFCGGKR