ID   CA15_CONPL              Reviewed;          81 AA.
AC   P0C8U9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Alpha-conotoxin-like Pu1.5;
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 [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=18625510; DOI=10.1016/j.toxicon.2008.05.004;
RA   Biggs J.S., Olivera B.M., Kantor Y.I.;
RT   "Alpha-conopeptides specifically expressed in the salivary gland of Conus
RT   pulicarius.";
RL   Toxicon 52:101-105(2008).
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|PubMed:18625510}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:18625510}.
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; P0C8U9; -.
DR   ConoServer; 2865; Pu1.5 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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..35
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000366065"
FT   PEPTIDE         36..77
FT                   /note="Alpha-conotoxin-like Pu1.5"
FT                   /id="PRO_0000366066"
FT   PROPEP          78..81
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000366067"
FT   REGION          17..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..48
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   DISULFID        44..50
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        45..58
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   81 AA;  8937 MW;  DF46130834A92324 CRC64;
     MFTVFLLVIL ATTVVPFPSD RDPASNHENS KGSNRNAWLT PEECCAAPAC REMILEFCLA
     GEAFAAALDG FRRLPYRLSS E