ID   CPY1_CONPO              Reviewed;          69 AA.
AC   B3SVF0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Conopeptide Y-Pl1;
DE   AltName: Full=CPY-Pl1;
DE   Flags: Precursor;
OS   Conus planorbis (Planorbis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Strategoconus.
OX   NCBI_TaxID=97183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-69, SYNTHESIS OF 40-69,
RP   FUNCTION, BIOASSAY, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=18505731; DOI=10.1074/jbc.m800084200;
RA   Imperial J.S., Chen P., Sporning A., Terlau H., Daly N.L., Craik D.J.,
RA   Alewood P.F., Olivera B.M.;
RT   "Tyrosine-rich conopeptides affect voltage-gated K+ channels.";
RL   J. Biol. Chem. 283:23026-23032(2008).
CC   -!- FUNCTION: Tyrosine-rich conopeptide that targets several
CC       channels/receptors that are expressed in Xenopus oocytes. These targets
CC       are the voltage-gated potassium channels Kv1.6/KCNA6 (IC(50) is 170 nM)
CC       and Kv1.2/KCNA2 (IC(50) is 2.0 uM), Nav1.2/SCN2A (30% of inhibition),
CC       and N-methyl-D-aspartate (NMDA) receptor (GRIN1/GRIN2A/GRIN3B and
CC       GRIN1/GRIN2B/GRIN3B) (15% of inhibition). In vivo, causes the marine
CC       worm N.virens to move very slowly in contrast to control worms, and
CC       causes seizures (at 5 nmol) and death (20 nmol) to mice when
CC       intracranially injected. {ECO:0000269|PubMed:18505731}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18505731}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4092.1; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:18505731};
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residues.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not target Kv1.3/KCNA3 (IC(50) is >50 uM),
CC       Kv1.4/KCNA4 (IC(50) is >50 uM), Kv1.5/KCNA5 (IC(50) is >5 uM).
CC       {ECO:0000305|PubMed:18505731}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. Conopeptide Y
CC       family. {ECO:0000305}.
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DR   EMBL; EU000528; ABV74049.1; -; mRNA.
DR   AlphaFoldDB; B3SVF0; -.
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:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ion channel impairing toxin;
KW   Ionotropic glutamate receptor inhibitor; Neurotoxin;
KW   Postsynaptic neurotoxin; Potassium channel impairing toxin; Secreted;
KW   Signal; Toxin; Voltage-gated potassium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..69
FT                   /id="PRO_5000379122"
FT   PEPTIDE         40..69
FT                   /note="Conopeptide Y-Pl1"
FT                   /id="PRO_5000379123"
SQ   SEQUENCE   69 AA;  8236 MW;  9D4F70CF0F83A1E0 CRC64;
     MSKLGVVLFV FLLLLPLAAP QPVGDQPADQ PADRNAEARA RFLHPFQYYT LYRYLTRFLH
     RYPIYYIRY