ID   CA11_CONPL              Reviewed;          67 AA.
AC   A0SE60; A6M936;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Alpha-conotoxin-like Pu1.1;
DE   Flags: Precursor;
OS   Conus pulicarius (Flea-bitten cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=93154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD48793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ309775; ABC39768.1; -; Genomic_DNA.
DR   EMBL; DQ359142; ABD48793.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0SE60; -.
DR   ConoServer; 542; Pu1.1 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   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000370680"
FT   PEPTIDE         47..63
FT                   /note="Alpha-conotoxin-like Pu1.1"
FT                   /id="PRO_0000370681"
FT   REGION          51..53
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         47
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..55
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        50..63
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   67 AA;  7507 MW;  BE6CE72F20754F7C CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRTSDG RNAAFNAFDL IALTARQNCC NVPGCWAKYK
     HLCGRKR