ID   CA1S1_CONPL             Reviewed;          63 AA.
AC   P0C8U6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Alpha-conotoxin-like PuSG1.1;
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 [MRNA].
RC   TISSUE=Salivary gland;
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-conopeptides-like may act on postsynaptic membranes,
CC       they bind to the nicotinic acetylcholine receptors (nAChR) and thus
CC       inhibit them (By similarity). Has possibly a distinct nAChR binding
CC       mode from other alpha-conotoxins, due to a different three residue
CC       motif (lacks the Ser-Xaa-Pro motif) (By similarity).
CC       {ECO:0000250|UniProtKB:Q2I2R8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18625510}.
CC   -!- TISSUE SPECIFICITY: Expressed by the salivary gland.
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; P0C8U6; -.
DR   ConoServer; 2861; PuSG1.1 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; 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..43
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000366058"
FT   PEPTIDE         44..63
FT                   /note="Alpha-conotoxin-like PuSG1.1"
FT                   /id="PRO_0000366059"
FT   REGION          48..50
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   63 AA;  6556 MW;  1ED46E78BB45584B CRC64;
     MRCLAFLVVT LLLFTATATT GASNGMNAAA SGEAPDSISL AVRDDCCPDP ACRQNHPELC
     STR