ID   PYY_RAT                 Reviewed;          98 AA.
AC   P10631; Q3C1E8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Peptide YY {ECO:0000303|PubMed:3413293};
DE            Short=PYY {ECO:0000303|PubMed:3413293};
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3654598; DOI=10.1016/s0021-9258(18)45154-x;
RA   Leiter A.B., Toder A., Wolfe H.J., Taylor I.L., Cooperman S., Mandel G.,
RA   Goodman R.H.;
RT   "Peptide YY. Structure of the precursor and expression in exocrine
RT   pancreas.";
RL   J. Biol. Chem. 262:12984-12988(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1890992; DOI=10.1210/mend-5-3-433;
RA   Krasinski S.D., Wheeler M.B., Leiter A.B.;
RT   "Isolation, characterization, and developmental expression of the rat
RT   peptide-YY gene.";
RL   Mol. Endocrinol. 5:433-440(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pandey J., Hamid Z., Vishwakarma N., Kumar A.;
RT   "Pyy gene for peptide synthesis in Rattus norvegicus.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 29-64.
RX   PubMed=3413293; DOI=10.1016/0167-0115(88)90008-0;
RA   Corder R., Gaillard R.C., Boehlen P.;
RT   "Isolation and sequence of rat peptide YY and neuropeptide Y.";
RL   Regul. Pept. 21:253-261(1988).
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; M17523; AAA41222.1; -; mRNA.
DR   EMBL; S57220; AAB19752.1; -; Genomic_DNA.
DR   EMBL; AB238226; BAE46747.1; -; mRNA.
DR   PIR; A37955; A29364.
DR   RefSeq; NP_001029252.1; NM_001034080.1.
DR   AlphaFoldDB; P10631; -.
DR   BMRB; P10631; -.
DR   STRING; 10116.ENSRNOP00000028323; -.
DR   PaxDb; P10631; -.
DR   GeneID; 287730; -.
DR   KEGG; rno:287730; -.
DR   UCSC; RGD:1593289; rat.
DR   CTD; 5697; -.
DR   RGD; 1593289; Pyy.
DR   eggNOG; ENOG502S267; Eukaryota.
DR   InParanoid; P10631; -.
DR   OrthoDB; 1542445at2759; -.
DR   PhylomeDB; P10631; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:P10631; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0005184; F:neuropeptide hormone activity; ISO:RGD.
DR   GO; GO:0031841; F:neuropeptide Y receptor binding; IBA:GO_Central.
DR   GO; GO:0042755; P:eating behavior; ISO:RGD.
DR   GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR   GO; GO:0032096; P:negative regulation of response to food; IDA:RGD.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:3413293"
FT   PEPTIDE         29..64
FT                   /note="Peptide YY"
FT                   /id="PRO_0000025391"
FT   PEPTIDE         31..64
FT                   /note="Peptide YY(3-36)"
FT                   /evidence="ECO:0000250|UniProtKB:P10082"
FT                   /id="PRO_0000430666"
FT   PROPEP          68..98
FT                   /id="PRO_0000025392"
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"
SQ   SEQUENCE   98 AA;  11121 MW;  994C0C3AD6A8A7DE CRC64;
     MVAVRRPWPV MVAMLLVLLA CLGALVDAYP AKPEAPGEDA SPEELSRYYA SLRHYLNLVT
     RQRYGKREVP AALFSKLLFT DDSENLPFRS RPEGVDQW