ID   CA11_CONLE              Reviewed;          68 AA.
AC   Q6PTD5; A0SE61;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Alpha-conotoxin Lp1.1 {ECO:0000303|PubMed:17400270};
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 [GENOMIC DNA / MRNA], AND AMIDATION AT GLY-65.
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).
RN   [2]
RP   SYNTHESIS OF 49-64, FUNCTION, AND BIOASSAY.
RX   PubMed=18588930; DOI=10.1016/j.peptides.2008.05.028;
RA   Peng C., Han Y.-H., Sanders T., Chew G., Liu J., Hawrot E., Chi C.-W.,
RA   Wang C.-G.;
RT   "Alpha4/7-conotoxin Lp1.1 is a novel antagonist of neuronal nicotinic
RT   acetylcholine receptors.";
RL   Peptides 29:1700-1707(2008).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       Synthetic peptide inhibits alpha-6/alpha-3/beta-2 and alpha-3/beta-2
CC       nicotinic acetylcholine receptors and causes uncoordinated movement
CC       when intramuscularly injected into goldfish (PubMed:18588930). Has a
CC       distinct nAChR binding mode from other alpha-conotoxins, due to a
CC       different three residue motif (Ala-Xaa-Ala instead of the conserved
CC       Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8,
CC       ECO:0000269|PubMed:18588930}.
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}.
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DR   EMBL; AY580321; AAS93424.1; -; mRNA.
DR   EMBL; DQ359141; ABD48792.1; -; mRNA.
DR   EMBL; DQ309776; ABC39769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6PTD5; -.
DR   ConoServer; 119; Lp1.1 precursor.
DR   ConoServer; 543; Lp1.1 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   1: Evidence at protein level;
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:0000305|PubMed:17400270"
FT                   /id="PRO_0000370647"
FT   PEPTIDE         49..65
FT                   /note="Alpha-conotoxin Lp1.1"
FT                   /evidence="ECO:0000305|PubMed:17400270"
FT                   /id="PRO_0000370648"
FT   PROPEP          66..68
FT                   /evidence="ECO:0000305|PubMed:17400270"
FT                   /id="PRO_0000370649"
FT   REGION          52..54
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:Q2I2R8"
FT   MOD_RES         65
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P85886,
FT                   ECO:0000305|PubMed:17400270"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000305|PubMed:18588930"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000305|PubMed:18588930"
FT   CONFLICT        20
FT                   /note="V -> D (in Ref. 1; ABC39769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="R -> H (in Ref. 1; ABC39769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="G -> R (in Ref. 1; ABC39769)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   68 AA;  7155 MW;  30B30442453B2F3D CRC64;
     MGMRMMFIMF MLVVLATTVV TFTSDRALDA MNAAASNKAS RLIALAVRGC CARAACAGIH
     QELCGGGR