ID   CAE1_CONPL              Reviewed;          69 AA.
AC   C6ZJQ2;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Alpha-conotoxin Pu14.1 {ECO:0000303|PubMed:20691232};
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], FUNCTION, DISULFIDE BONDS, SYNTHESIS OF 50-68,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom duct;
RX   PubMed=20691232; DOI=10.1016/j.peptides.2010.07.011;
RA   Peng C., Ye M., Wang Y., Shao X., Yuan D., Liu J., Hawrot E., Wang C.,
RA   Chi C.;
RT   "A new subfamily of conotoxins belonging to the A-superfamily.";
RL   Peptides 31:2009-2016(2010).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. At
CC       1 uM, the synthetic peptide reversibly blocks mammalian nAChR alpha-
CC       1/beta-1/gamma/delta and, to a lesser degree, alpha-6/alpha-3/beta-2,
CC       but has no effect on alpha-7. At 10 uM, it reversibly blocks nAChR
CC       alpha-3/beta-2, but has no effect on nAChR alpha-3/beta-4, alpha-
CC       4/beta-2, alpha-4/beta-4 or alpha-6/alpha-3/beta-4. Intramuscular
CC       injection of 10-20 ug of the synthetic peptide in goldfish causes
CC       death. Intravenous injection of the same doses in Kunming male mice
CC       causes unconsciousness. Does not inhibit potassium channels.
CC       {ECO:0000269|PubMed:20691232}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86362}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:20691232}.
CC   -!- DOMAIN: The cysteine framework is XIV (C-C-C-C). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000255}.
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DR   EMBL; EU912017; ACL13206.1; -; mRNA.
DR   AlphaFoldDB; C6ZJQ2; -.
DR   BMRB; C6ZJQ2; -.
DR   ConoServer; 3761; Pu14.1 precursor.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044504; P:modulation of receptor activity in another organism; IDA:UniProtKB.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
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..49
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000405800"
FT   PEPTIDE         50..68
FT                   /note="Alpha-conotoxin Pu14.1"
FT                   /evidence="ECO:0000269|PubMed:20691232"
FT                   /id="PRO_0000405801"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250|UniProtKB:P86362"
FT   DISULFID        62..68
FT                   /evidence="ECO:0000250|UniProtKB:P86362"
SQ   SEQUENCE   69 AA;  7510 MW;  63884ED66A9DACDC CRC64;
     MGMRMMFAVF LLVVLATTVV SFNSDRASDG RNAAANVKAS DLMARVLEKD CPPHPVPGMH
     KCVCLKTCR