ID   NPY_DICLA               Reviewed;          99 AA.
AC   Q9PTA0; Q9PT97;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Pro-neuropeptide Y;
DE   Contains:
DE     RecName: Full=Neuropeptide Y;
DE     AltName: Full=Neuropeptide tyrosine;
DE              Short=NPY;
DE   Contains:
DE     RecName: Full=C-flanking peptide of NPY;
DE              Short=CPON;
DE   Flags: Precursor;
GN   Name=npy;
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Cerda-Reverter J.M., Martinez-Rodriguez G., Zanuy S., Carrillo M.,
RA   Larhammar D.;
RT   "Neuropeptide Y, endocrine gut peptide YY and fish pancreatic peptide Y
RT   expression in the brain of a teleost fish (Dicentrarchus labrax): from
RT   cloning to evolutionary considerations.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-62.
RC   TISSUE=Blood;
RA   Cerda-Reverter J.M., Martinez-Rodriguez G., Zanuy S., Carrillo M.,
RA   Larhammar D.;
RT   "Deduced peptide sequence of neuropeptide Y exon 2 from sea bass
RT   (Dicentrarchus labrax).";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NPY is implicated in the control of feeding and in secretion
CC       of gonadotrophin-release hormone.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR   EMBL; AJ005378; CAB64932.1; -; mRNA.
DR   EMBL; AJ005381; CAB64935.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9PTA0; -.
DR   Ensembl; ENSDLAT00005019115; ENSDLAP00005017692; ENSDLAG00005008510.
DR   GeneTree; ENSGT00940000156475; -.
DR   Proteomes; UP000694389; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0031843; F:type 2 neuropeptide Y receptor binding; IEA:Ensembl.
DR   GO; GO:0071878; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
DR   GO; GO:2000253; P:positive regulation of feeding behavior; IEA:Ensembl.
DR   CDD; cd00126; PAH; 1.
DR   InterPro; IPR001955; Pancreatic_hormone-like.
DR   InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR   PANTHER; PTHR10533; PTHR10533; 1.
DR   Pfam; PF00159; Hormone_3; 1.
DR   PRINTS; PR00278; PANCHORMONE.
DR   SMART; SM00309; PAH; 1.
DR   PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
DR   PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
PE   3: Inferred from homology;
KW   Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         29..64
FT                   /note="Neuropeptide Y"
FT                   /id="PRO_0000025341"
FT   PEPTIDE         68..99
FT                   /note="C-flanking peptide of NPY"
FT                   /id="PRO_0000025342"
FT   MOD_RES         64
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   99 AA;  11260 MW;  4EEFAED164964184 CRC64;
     MHPNLVSWLG TLGFLLWALL CLGALTEGYP VKPENPGEDA PAEELAKYYS ALRHYINLIT
     RQRYGKRSSP EILDTLVSEL LLKESTDQLP QSRYDPSLW