ID   CA18_CONLE              Reviewed;          64 AA.
AC   A1X8C2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Alpha-conotoxin-like Lp1.8 {ECO:0000303|PubMed:17400270};
DE   AltName: Full=Alpha-conotoxin-like Lp1.7 {ECO:0000312|EMBL:ABD33854.1};
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;
RX   PubMed=17400270; DOI=10.1016/j.toxicon.2007.02.011;
RA   Yuan D.-D., Han Y.-H., Wang C.-G., Chi C.-W.;
RT   "From the identification of gene organization of alpha conotoxins to the
RT   cloning of novel toxins.";
RL   Toxicon 49:1135-1149(2007).
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 (Lys-Xaa-Pro
CC       instead of the conserved Ser-Xaa-Pro motif) (By similarity).
CC       {ECO:0000250|UniProtKB:Q2I2R8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17400270}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:17400270}.
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}.
CC   -!- CAUTION: There is a discrepancy in nomenclature: was submitted as Lp1.7
CC       but is named Lp1.8 in PubMed:17400270. {ECO:0000305|PubMed:17400270}.
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DR   EMBL; DQ311062; ABD33854.1; -; mRNA.
DR   AlphaFoldDB; A1X8C2; -.
DR   SMR; A1X8C2; -.
DR   ConoServer; 552; Lp1.8 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; 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..41
FT                   /evidence="ECO:0000305|PubMed:17400270"
FT                   /id="PRO_0000370653"
FT   PEPTIDE         42..64
FT                   /note="Alpha-conotoxin-like Lp1.8"
FT                   /evidence="ECO:0000305|PubMed:17400270"
FT                   /id="PRO_0000370654"
FT   REGION          49..51
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   DISULFID        47..53
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        48..61
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   64 AA;  7577 MW;  304BA6FF341B9241 CRC64;
     MGMRMMFTMF LLVVLTTTVV SFNSDRESNH ENRRTSNQIT RGVWDECCKD PQCRQNHMQH
     CPAR