PYY_HUMAN
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 03-AUG-2022, entry version 192.
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="http://atlasgeneticsoncology.org/Genes/PYYID46182ch17q21.html";
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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 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 PDBsum; 2DEZ; -.
DR PDBsum; 2DF0; -.
DR PDBsum; 2L60; -.
DR PDBsum; 2NA5; -.
DR PDBsum; 7RT9; -.
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; P10082; -.
DR PeptideAtlas; P10082; -.
DR PRIDE; P10082; -.
DR ProteomicsDB; 52563; -. [P10082-1]
DR ProteomicsDB; 52564; -. [P10082-2]
DR Antibodypedia; 3390; 462 antibodies from 30 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 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; HAYPAKP; -.
DR OrthoDB; 1542445at2759; -.
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 1062 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 90 other tissues.
DR Genevisible; P10082; HS.
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; IBA:GO_Central.
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 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 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 41..59
FT /evidence="ECO:0007829|PDB:2DEZ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2L60"
SQ SEQUENCE 97 AA; 11145 MW; C166B73412E356B1 CRC64;
MVFVRRPWPA LTTVLLALLV CLGALVDAYP IKPEAPREDA SPEELNRYYA SLRHYLNLVT
RQRYGKRDGP DTLLSKTFFP DGEDRPVRSR SEGPDLW
