ID   PYY_HUMAN               Reviewed;          97 AA.
AC   P10082; Q5U5Q6; Q6FGH8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   24-JAN-2024, entry version 200.
DE   RecName: Full=Peptide YY {ECO:0000303|PubMed:2587421};
DE            Short=PYY {ECO:0000303|PubMed:2587421};
DE   AltName: Full=PYY-I {ECO:0000250|UniProtKB:Q9TR93};
DE   AltName: Full=Peptide tyrosine tyrosine;
DE   Contains:
DE     RecName: Full=Peptide YY(3-36) {ECO:0000303|PubMed:2587421};
DE     AltName: Full=PYY-II {ECO:0000250|UniProtKB:Q9TR93};
DE   Flags: Precursor;
GN   Name=PYY;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP   GLY-37 AND ARG-72.
RC   TISSUE=Colon mucosa;
RX   PubMed=8318545; DOI=10.1016/0167-4781(93)90136-2;
RA   Kohri K., Nata K., Yonekura H., Nagai A., Konno K., Okamoto H.;
RT   "Cloning and structural determination of human peptide YY cDNA and gene.";
RL   Biochim. Biophys. Acta 1173:345-349(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-37.
RA   Herzog H.;
RT   "Genomic organisation and localisation of the gene for the human peptide
RT   YY.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLY-37 AND
RP   ARG-72.
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-37 AND
RP   ARG-72.
RC   TISSUE=Brain;
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   [6]
RP   PROTEIN SEQUENCE OF 29-64, AMIDATION AT TYR-64, SYNTHESIS OF 29-64, AND
RP   VARIANT GLY-37.
RX   PubMed=3202875; DOI=10.1016/s0006-291x(88)80308-5;
RA   Tatemoto K., Nakano I., Makk G., Angwin P., Mann M., Schilling J.,
RA   Go V.L.W.;
RT   "Isolation and primary structure of human peptide YY.";
RL   Biochem. Biophys. Res. Commun. 157:713-717(1988).
RN   [7]
RP   PROTEIN SEQUENCE OF 29-64, AMIDATION AT TYR-64, AND VARIANT GLY-37.
RX   PubMed=2587421; DOI=10.1016/0196-9781(89)90116-2;
RA   Eberlein G.A., Eysselein V.E., Schaeffer M., Layer P., Grandt D.,
RA   Goebell H., Niebel W., Davis M., Lee T.D., Shively J.E., Reeve J.R. Jr.;
RT   "A new molecular form of PYY: structural characterization of human PYY(3-
RT   36) and PYY(1-36).";
RL   Peptides 10:797-803(1989).
RN   [8]
RP   CLEAVAGE BY FAP, AND CLEAVAGE SITE.
RX   PubMed=21314817; DOI=10.1111/j.1742-4658.2011.08051.x;
RA   Keane F.M., Nadvi N.A., Yao T.W., Gorrell M.D.;
RT   "Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are
RT   novel substrates of fibroblast activation protein-alpha.";
RL   FEBS J. 278:1316-1332(2011).
RN   [9]
RP   STRUCTURE BY NMR OF 29-64.
RX   PubMed=16819834; DOI=10.1021/bi060359l;
RA   Nygaard R., Nielbo S., Schwartz T.W., Poulsen F.M.;
RT   "The PP-fold solution structure of human polypeptide YY and human PYY3-36
RT   as determined by NMR.";
RL   Biochemistry 45:8350-8357(2006).
CC   -!- FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has
CC       a vasoconstrictory action and inhibitis jejunal and colonic mobility.
CC   -!- INTERACTION:
CC       P10082; P25929: NPY1R; NbExp=2; IntAct=EBI-6655667, EBI-372227;
CC       P10082; P49146: NPY2R; NbExp=2; IntAct=EBI-6655667, EBI-6655721;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P10082-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P10082-2; Sequence=VSP_005081;
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:0000269|PubMed:21314817}.
CC   -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/46182/PYY";
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DR   EMBL; D13897; BAA02997.1; -; Genomic_DNA.
DR   EMBL; D13897; BAA02998.1; -; Genomic_DNA.
DR   EMBL; D13899; BAA03000.1; -; mRNA.
DR   EMBL; D13902; BAA03002.1; -; mRNA.
DR   EMBL; L25648; AAA36433.1; -; Genomic_DNA.
DR   EMBL; CR542129; CAG46926.1; -; mRNA.
DR   EMBL; AC007993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041057; AAH41057.1; -; mRNA.
DR   CCDS; CCDS32662.1; -. [P10082-1]
DR   CCDS; CCDS92333.1; -. [P10082-2]
DR   PIR; A31358; A31358.
DR   PIR; S33795; S33795.
DR   PIR; S34568; S34568.
DR   PIR; S34569; S34569.
DR   RefSeq; NP_004151.3; NM_004160.5. [P10082-1]
DR   RefSeq; XP_011523337.1; XM_011525035.1.
DR   PDB; 2DEZ; NMR; -; A=29-64.
DR   PDB; 2DF0; NMR; -; A=31-64.
DR   PDB; 2L60; NMR; -; A=41-64.
DR   PDB; 2NA5; NMR; -; A=31-63.
DR   PDB; 7RT9; X-ray; 1.90 A; Y/Z=29-64.
DR   PDB; 7YON; EM; 2.95 A; L=31-64.
DR   PDBsum; 2DEZ; -.
DR   PDBsum; 2DF0; -.
DR   PDBsum; 2L60; -.
DR   PDBsum; 2NA5; -.
DR   PDBsum; 7RT9; -.
DR   PDBsum; 7YON; -.
DR   AlphaFoldDB; P10082; -.
DR   BMRB; P10082; -.
DR   SMR; P10082; -.
DR   BioGRID; 111670; 31.
DR   IntAct; P10082; 4.
DR   MINT; P10082; -.
DR   STRING; 9606.ENSP00000353198; -.
DR   BioMuta; PYY; -.
DR   DMDM; 317373516; -.
DR   jPOST; P10082; -.
DR   MassIVE; P10082; -.
DR   PaxDb; 9606-ENSP00000353198; -.
DR   PeptideAtlas; P10082; -.
DR   ProteomicsDB; 52563; -. [P10082-1]
DR   ProteomicsDB; 52564; -. [P10082-2]
DR   Antibodypedia; 3390; 492 antibodies from 31 providers.
DR   DNASU; 5697; -.
DR   Ensembl; ENST00000360085.6; ENSP00000353198.1; ENSG00000131096.11. [P10082-1]
DR   Ensembl; ENST00000592796.2; ENSP00000467310.1; ENSG00000131096.11. [P10082-2]
DR   Ensembl; ENST00000692052.1; ENSP00000509262.1; ENSG00000131096.11. [P10082-1]
DR   GeneID; 5697; -.
DR   KEGG; hsa:5697; -.
DR   MANE-Select; ENST00000692052.1; ENSP00000509262.1; NM_001394028.1; NP_001380957.1.
DR   UCSC; uc002ieq.4; human. [P10082-1]
DR   AGR; HGNC:9748; -.
DR   CTD; 5697; -.
DR   DisGeNET; 5697; -.
DR   GeneCards; PYY; -.
DR   HGNC; HGNC:9748; PYY.
DR   HPA; ENSG00000131096; Tissue enriched (intestine).
DR   MIM; 600781; gene.
DR   neXtProt; NX_P10082; -.
DR   OpenTargets; ENSG00000131096; -.
DR   PharmGKB; PA34090; -.
DR   VEuPathDB; HostDB:ENSG00000131096; -.
DR   eggNOG; ENOG502S267; Eukaryota.
DR   GeneTree; ENSGT00940000160643; -.
DR   HOGENOM; CLU_162379_1_0_1; -.
DR   InParanoid; P10082; -.
DR   OMA; SEGADQW; -.
DR   OrthoDB; 4180655at2759; -.
DR   PhylomeDB; P10082; -.
DR   TreeFam; TF332778; -.
DR   PathwayCommons; P10082; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P10082; -.
DR   SIGNOR; P10082; -.
DR   BioGRID-ORCS; 5697; 6 hits in 1140 CRISPR screens.
DR   ChiTaRS; PYY; human.
DR   EvolutionaryTrace; P10082; -.
DR   GeneWiki; Peptide_YY; -.
DR   GenomeRNAi; 5697; -.
DR   Pharos; P10082; Tbio.
DR   PRO; PR:P10082; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P10082; Protein.
DR   Bgee; ENSG00000131096; Expressed in mucosa of sigmoid colon and 92 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:GO_Central.
DR   GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR   GO; GO:0031841; F:neuropeptide Y receptor binding; IBA:GO_Central.
DR   GO; GO:0007631; P:feeding behavior; IBA:GO_Central.
DR   GO; GO:0060575; P:intestinal epithelial cell differentiation; TAS:GO_Central.
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; P10082; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amidation;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Hormone;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:2587421,
FT                   ECO:0000269|PubMed:3202875"
FT   PEPTIDE         29..64
FT                   /note="Peptide YY"
FT                   /id="PRO_0000025384"
FT   PEPTIDE         31..64
FT                   /note="Peptide YY(3-36)"
FT                   /id="PRO_0000025385"
FT   PROPEP          68..97
FT                   /id="PRO_0000025386"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            30..31
FT                   /note="Cleavage; by FAP"
FT                   /evidence="ECO:0000269|PubMed:21314817"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68005"
FT   MOD_RES         64
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:2587421,
FT                   ECO:0000269|PubMed:3202875"
FT   VAR_SEQ         91..97
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8318545, ECO:0000303|Ref.3"
FT                   /id="VSP_005081"
FT   VARIANT         37
FT                   /note="R -> G (in dbSNP:rs229969)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2587421, ECO:0000269|PubMed:3202875,
FT                   ECO:0000269|PubMed:8318545, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_047407"
FT   VARIANT         72
FT                   /note="T -> R (in dbSNP:rs1058046)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8318545, ECO:0000269|Ref.3"
FT                   /id="VAR_006382"
FT   VARIANT         95
FT                   /note="D -> H (in dbSNP:rs465407)"
FT                   /id="VAR_047408"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:2DEZ"
FT   HELIX           42..61
FT                   /evidence="ECO:0007829|PDB:7RT9"
SQ   SEQUENCE   97 AA;  11145 MW;  C166B73412E356B1 CRC64;
     MVFVRRPWPA LTTVLLALLV CLGALVDAYP IKPEAPREDA SPEELNRYYA SLRHYLNLVT
     RQRYGKRDGP DTLLSKTFFP DGEDRPVRSR SEGPDLW
//