ID   PYY_MOUSE               Reviewed;          98 AA.
AC   Q9EPS2; Q91XD0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Peptide YY {ECO:0000250|UniProtKB:Q9TR93};
DE            Short=PYY {ECO:0000250|UniProtKB:Q9TR93};
DE   AltName: Full=Peptide tyrosine tyrosine;
DE   Contains:
DE     RecName: Full=Peptide YY(3-36) {ECO:0000250|UniProtKB:Q9TR93};
DE     AltName: Full=PYY-II {ECO:0000250|UniProtKB:Q9TR93};
DE   Flags: Precursor;
GN   Name=Pyy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RA   Brown G.J., James R., Eddie L.W.;
RT   "Mouse PYY promoter.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has
CC       a vasoconstrictory action and inhibitis jejunal and colonic mobility.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The peptide YY form is cleaved at Pro-30 by the prolyl
CC       endopeptidase FAP (seprase) activity (in vitro) to generate peptide
CC       YY(3-36). {ECO:0000250|UniProtKB:P10082}.
CC   -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR   EMBL; BC010821; AAH10821.1; -; mRNA.
DR   EMBL; AF325866; AAG42908.1; -; Genomic_DNA.
DR   CCDS; CCDS36339.1; -.
DR   RefSeq; NP_663410.1; NM_145435.1.
DR   AlphaFoldDB; Q9EPS2; -.
DR   BMRB; Q9EPS2; -.
DR   STRING; 10090.ENSMUSP00000135292; -.
DR   MaxQB; Q9EPS2; -.
DR   PaxDb; 10090-ENSMUSP00000017455; -.
DR   ProteomicsDB; 301856; -.
DR   Antibodypedia; 3390; 492 antibodies from 31 providers.
DR   DNASU; 217212; -.
DR   Ensembl; ENSMUST00000017455.15; ENSMUSP00000017455.9; ENSMUSG00000017311.16.
DR   GeneID; 217212; -.
DR   KEGG; mmu:217212; -.
DR   UCSC; uc007lqo.2; mouse.
DR   AGR; MGI:99924; -.
DR   CTD; 5697; -.
DR   MGI; MGI:99924; Pyy.
DR   VEuPathDB; HostDB:ENSMUSG00000017311; -.
DR   eggNOG; ENOG502S267; Eukaryota.
DR   GeneTree; ENSGT00940000160643; -.
DR   InParanoid; Q9EPS2; -.
DR   OrthoDB; 4180655at2759; -.
DR   PhylomeDB; Q9EPS2; -.
DR   TreeFam; TF332778; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 217212; 1 hit in 61 CRISPR screens.
DR   PRO; PR:Q9EPS2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9EPS2; Protein.
DR   Bgee; ENSMUSG00000017311; Expressed in dorsal pancreas and 49 other cell types or tissues.
DR   ExpressionAtlas; Q9EPS2; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IDA:MGI.
DR   GO; GO:0031841; F:neuropeptide Y receptor binding; IBA:GO_Central.
DR   GO; GO:0042755; P:eating behavior; IDA:MGI.
DR   GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR   GO; GO:0032096; P:negative regulation of response to food; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   CDD; cd00126; PAH; 1.
DR   Gene3D; 6.10.250.900; -; 1.
DR   InterPro; IPR001955; Pancreatic_hormone-like.
DR   InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR   PANTHER; PTHR10533; NEUROPEPTIDE Y/PANCREATIC HORMONE/PEPTIDE YY; 1.
DR   PANTHER; PTHR10533:SF14; PEPTIDE YY-RELATED; 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.
DR   Genevisible; Q9EPS2; MM.
PE   3: Inferred from homology;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         29..64
FT                   /note="Peptide YY"
FT                   /id="PRO_0000025387"
FT   PEPTIDE         31..64
FT                   /note="Peptide YY(3-36)"
FT                   /evidence="ECO:0000250|UniProtKB:P10082"
FT                   /id="PRO_0000430664"
FT   PROPEP          68..98
FT                   /id="PRO_0000025388"
FT   SITE            30..31
FT                   /note="Cleavage; by FAP"
FT                   /evidence="ECO:0000250|UniProtKB:P10082"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68005"
FT   MOD_RES         64
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        92..93
FT                   /note="PE -> SR (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   98 AA;  11064 MW;  7AF165A1052C3249 CRC64;
     MVAVRRPWPV TVAMLLILLA CLGALVDAYP AKPEAPGEDA SPEELSRYYA SLRHYLNLVT
     RQRYGKRDVP AALFSKLLFT DDSDSENLPF RPEGLDQW
//