ID NPY_HUMAN Reviewed; 97 AA. AC P01303; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 226. DE RecName: Full=Pro-neuropeptide Y; DE Contains: DE RecName: Full=Neuropeptide Y {ECO:0000303|PubMed:2427515}; DE AltName: Full=Neuropeptide tyrosine {ECO:0000303|PubMed:6589611}; DE Short=NPY {ECO:0000303|PubMed:2427515}; DE Contains: DE RecName: Full=C-flanking peptide of NPY {ECO:0000303|PubMed:3839058}; DE Short=CPON {ECO:0000303|PubMed:3839058}; DE Flags: Precursor; GN Name=NPY {ECO:0000303|PubMed:2427515}; 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 [MRNA], AND AMIDATION AT TYR-64. RX PubMed=6589611; DOI=10.1073/pnas.81.14.4577; RA Minth C.D., Bloom S.R., Polak J.M., Dixon J.E.; RT "Cloning, characterization, and DNA sequence of a human cDNA encoding RT neuropeptide tyrosine."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4577-4581(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2427515; DOI=10.1016/s0021-9258(18)67189-3; RA Minth C.D., Andrews P.C., Dixon J.E.; RT "Characterization, sequence, and expression of the cloned human RT neuropeptide Y gene."; RL J. Biol. Chem. 261:11974-11979(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3753985; DOI=10.1172/jci112357; RA Takeuchi T., Gumucio D.L., Yamada T., Meisler M.H., Minth C.D., Dixon J.E., RA Eddy R.E., Shows T.B.; RT "Genes encoding pancreatic polypeptide and neuropeptide Y are on human RT chromosomes 17 and 7."; RL J. Clin. Invest. 77:1038-1041(1986). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 IDENTIFICATION OF CPON. RX PubMed=3839058; DOI=10.1016/0143-4179(85)90100-3; RA Allen J.M., Polak J.M., Bloom S.R.; RT "Presence of the predicted C-flanking peptide of neuropeptide Y (CPON) in RT tissue extracts."; RL Neuropeptides 6:95-100(1985). RN [7] RP FUNCTION, AND MUTAGENESIS OF ILE-59 AND GLN-62. RX PubMed=1321422; DOI=10.1073/pnas.89.13.5794; RA Herzog H., Hort Y.J., Ball H.J., Hayes G., Shine J., Selbie L.A.; RT "Cloned human neuropeptide Y receptor couples to two different second RT messenger systems."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5794-5798(1992). RN [8] RP FUNCTION. RX PubMed=7592910; DOI=10.1074/jbc.270.45.26758; RA Gerald C., Walker M.W., Vaysse P.J.-J., He C., Branchek T.A., RA Weinshank R.L.; RT "Expression cloning and pharmacological characterization of a human RT hippocampal neuropeptide Y/peptide YY Y2 receptor subtype."; RL J. Biol. Chem. 270:26758-26761(1995). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=7593641; DOI=10.1172/jci118310; RA deS Senanayake P., Denker J., Bravo E.L., Graham R.M.; RT "Production, characterization, and expression of neuropeptide Y by human RT pheochromocytoma."; RL J. Clin. Invest. 96:2503-2509(1995). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP STRUCTURE BY NMR OF 29-64. RX PubMed=1425680; DOI=10.1111/j.1432-1033.1992.tb17346.x; RA Darbon H., Bernassau J.-M., Deleuze C., Chenu J., Roussel A., Cambillau C.; RT "Solution conformation of human neuropeptide Y by 1H nuclear magnetic RT resonance and restrained molecular dynamics."; RL Eur. J. Biochem. 209:765-771(1992). RN [13] RP STRUCTURE BY NMR OF 29-64. RX PubMed=9008359; DOI=10.1007/bf00228141; RA Monks S.A., Karagianis G., Howlett G.J., Norton R.S.; RT "Solution structure of human neuropeptide Y."; RL J. Biomol. NMR 8:379-390(1996). RN [14] RP STRUCTURE BY NMR OF 52-64. RX PubMed=10561544; DOI=10.1016/s0167-4838(99)00214-9; RA Barnham K.J., Catalfamo F., Pallaghy P.K., Howlett G.J., Norton R.S.; RT "Helical structure and self-association in a 13 residue neuropeptide Y Y2 RT receptor agonist: relationship to biological activity."; RL Biochim. Biophys. Acta 1435:127-137(1999). RN [15] {ECO:0007744|PDB:7VGX} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 29-64 IN COMPLEX WITH RP NPY1R AND GNAI1, FUNCTION, AND MUTAGENESIS OF 1-MET--PRO-30 AND RP 29-TYR-PRO-30. RX PubMed=35165283; DOI=10.1038/s41467-022-28510-6; RA Park C., Kim J., Ko S.B., Choi Y.K., Jeong H., Woo H., Kang H., Bang I., RA Kim S.A., Yoon T.Y., Seok C., Im W., Choi H.J.; RT "Structural basis of neuropeptide Y signaling through Y1 receptor."; RL Nat. Commun. 13:853-853(2022). RN [16] RP ERRATUM OF PUBMED:35165283. RX PubMed=35217654; DOI=10.1038/s41467-022-28837-0; RA Park C., Kim J., Ko S.B., Choi Y.K., Jeong H., Woo H., Kang H., Bang I., RA Kim S.A., Yoon T.Y., Seok C., Im W., Choi H.J.; RL Nat. Commun. 13:1126-1126(2022). RN [17] {ECO:0007744|PDB:7RTA} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 29-64. RX PubMed=35180645; DOI=10.1016/j.npep.2022.102231; RA Langley D.B., Schofield P., Jackson J., Herzog H., Christ D.; RT "Crystal structures of human neuropeptide Y (NPY) and peptide YY (PYY)."; RL Neuropeptides 92:102231-102231(2022). RN [18] {ECO:0007744|PDB:7X9A, ECO:0007744|PDB:7X9B} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 29-64 IN COMPLEXES RP WITH NPY1R; NPY2R AND GNAI1, AND FUNCTION. RX PubMed=35507650; DOI=10.1126/sciadv.abm1232; RA Tang T., Tan Q., Han S., Diemar A., Lobner K., Wang H., Schuss C., Behr V., RA Morl K., Wang M., Chu X., Yi C., Keller M., Kofoed J., Reedtz-Runge S., RA Kaiser A., Beck-Sickinger A.G., Zhao Q., Wu B.; RT "Receptor-specific recognition of NPY peptides revealed by structures of RT NPY receptors."; RL Sci. Adv. 8:eabm1232-eabm1232(2022). RN [19] {ECO:0007744|PDB:7YOO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.11 ANGSTROMS) OF 29-64 IN COMPLEX WITH RP NPY2R AND GNAI1, AND FUNCTION. RX PubMed=36525977; DOI=10.1016/j.str.2022.11.010; RA Kang H., Park C., Choi Y.K., Bae J., Kwon S., Kim J., Choi C., Seok C., RA Im W., Choi H.J.; RT "Structural basis for Y2 receptor-mediated neuropeptide Y and peptide YY RT signaling."; RL Structure 31:44-57.e6(2023). RN [20] {ECO:0007744|PDB:8K6M, ECO:0007744|PDB:8K6N, ECO:0007744|PDB:8K6O} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 29-64 OF WILD TYPE AND RP MUTANT NPY IN COMPLEXES WITH NPY1R; NPY2R AND GNAI2, FUNCTION, AND RP MUTAGENESIS OF ILE-59 AND GLN-62. RX PubMed=38882210; DOI=10.1002/mco2.565; RA Shen S., Deng Y., Shen C., Chen H., Cheng L., Wu C., Zhao C., Yang Z., RA Hou H., Wang K., Shao Z., Deng C., Ye F., Yan W.; RT "Structural basis of neuropeptide Y signaling through Y1 and Y2 RT receptors."; RL MedComm 5:e565-e565(2024). CC -!- FUNCTION: [Neuropeptide Y]: Ligand for neuropeptide Y receptor type 1 CC (NPY1R) and neuropeptide Y receptor type 2 (NPY2R) (PubMed:1321422, CC PubMed:7592910, PubMed:35165283, PubMed:35507650, PubMed:36525977, CC PubMed:38882210). Receptor binding induces adenylate cyclase-inhibiting CC G protein-coupled receptor signaling, resulting in inhibition of cAMP CC production (PubMed:1321422, PubMed:7592910, PubMed:38882210). Receptor CC activation by NPY also leads to an increase of intracellular Ca(2+) CC levels (PubMed:1321422, PubMed:35165283, PubMed:7592910). Is involved CC in the regulation of eating behavior, acting as a stimulator of food CC intake (By similarity). Involved in the regulation of colonic CC antisecretory tone, and colonic contractility (By similarity). CC {ECO:0000250|UniProtKB:P07808, ECO:0000250|UniProtKB:P57774, CC ECO:0000269|PubMed:1321422, ECO:0000269|PubMed:35165283, CC ECO:0000269|PubMed:35507650, ECO:0000269|PubMed:36525977, CC ECO:0000269|PubMed:38882210, ECO:0000269|PubMed:7592910}. CC -!- INTERACTION: CC P01303; F1D8P7: NR1H2; NbExp=3; IntAct=EBI-3905877, EBI-10177172; CC P01303; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3905877, EBI-947187; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7593641}. CC Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle CC {ECO:0000250|UniProtKB:P07808}. CC -!- TISSUE SPECIFICITY: One of the most abundant peptides in the nervous CC system. Also found in some chromaffin cells of the adrenal medulla. CC -!- PTM: The neuropeptide Y form is cleaved at Pro-30 by the prolyl CC endopeptidase FAP (seprase) activity (in vitro). CC {ECO:0000269|PubMed:21314817}. CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Neuropeptide Y entry; CC URL="https://en.wikipedia.org/wiki/Neuropeptide_Y"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44438/NPY"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K01911; AAA59944.1; -; mRNA. DR EMBL; M14298; AAA59945.1; -; Genomic_DNA. DR EMBL; M14296; AAA59945.1; JOINED; Genomic_DNA. DR EMBL; M14297; AAA59945.1; JOINED; Genomic_DNA. DR EMBL; M15789; AAA59946.1; -; mRNA. DR EMBL; AC004485; AAQ96843.1; -; Genomic_DNA. DR EMBL; BC029497; AAH29497.1; -; mRNA. DR CCDS; CCDS5387.1; -. DR PIR; A25198; NYHUY. DR RefSeq; NP_000896.1; NM_000905.4. DR PDB; 1QFA; NMR; -; A=52-64. DR PDB; 1RON; NMR; -; A=29-64. DR PDB; 7RTA; X-ray; 2.60 A; N=29-64. DR PDB; 7VGX; EM; 3.20 A; L=29-64. DR PDB; 7X9A; EM; 3.20 A; P=29-64. DR PDB; 7X9B; EM; 3.40 A; P=29-64. DR PDB; 7YOO; EM; 3.11 A; L=29-64. DR PDB; 8K6M; EM; 3.30 A; E=29-64. DR PDB; 8K6N; EM; 3.20 A; D=29-64. DR PDB; 8K6O; EM; 3.30 A; E=29-64. DR AlphaFoldDB; P01303; -. DR BMRB; P01303; -. DR EMDB; EMD-31979; -. DR EMDB; EMD-33069; -. DR EMDB; EMD-33070; -. DR EMDB; EMD-33985; -. DR EMDB; EMD-36923; -. DR EMDB; EMD-36924; -. DR EMDB; EMD-36925; -. DR SMR; P01303; -. DR BioGRID; 110914; 8. DR FunCoup; P01303; 663. DR IntAct; P01303; 15. DR MINT; P01303; -. DR NDEx; IQUERY-CP-NPY; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000384364; -. DR BindingDB; P01303; -. DR DrugBank; DB02952; 2-aminoisobutyric acid. DR DrugBank; DB03380; L-tyrosinamide. DR DrugBank; DB00191; Phentermine. DR iPTMnet; P01303; -. DR PhosphoSitePlus; P01303; -. DR BioMuta; NPY; -. DR DMDM; 128117; -. DR CPTAC; CPTAC-1287; -. DR CPTAC; CPTAC-1288; -. DR CPTAC; CPTAC-1289; -. DR CPTAC; CPTAC-1290; -. DR CPTAC; CPTAC-1291; -. DR MassIVE; P01303; -. DR PaxDb; 9606-ENSP00000384364; -. DR PeptideAtlas; P01303; -. DR ProteomicsDB; 51373; -. DR ABCD; P01303; 2 sequenced antibodies. DR Antibodypedia; 12195; 595 antibodies from 42 providers. DR DNASU; 4852; -. DR Ensembl; ENST00000242152.7; ENSP00000242152.2; ENSG00000122585.9. DR Ensembl; ENST00000405982.1; ENSP00000385282.1; ENSG00000122585.9. DR Ensembl; ENST00000407573.5; ENSP00000384364.1; ENSG00000122585.9. DR Ensembl; ENST00000925261.1; ENSP00000595320.1; ENSG00000122585.9. DR GeneID; 4852; -. DR KEGG; hsa:4852; -. DR MANE-Select; ENST00000242152.7; ENSP00000242152.2; NM_000905.4; NP_000896.1. DR UCSC; uc003sww.3; human. DR AGR; HGNC:7955; -. DR ClinPGx; PA255; -. DR CTD; 4852; -. DR DisGeNET; 4852; -. DR GeneCards; NPY; -. DR HGNC; HGNC:7955; NPY. DR HPA; ENSG00000122585; Group enriched (adrenal gland, brain, prostate). DR MalaCards; NPY; -. DR MIM; 162640; gene. DR OpenTargets; ENSG00000122585; -. DR VEuPathDB; HostDB:ENSG00000122585; -. DR eggNOG; ENOG502S2BU; Eukaryota. DR GeneTree; ENSGT00940000156475; -. DR HOGENOM; CLU_162379_1_0_1; -. DR InParanoid; P01303; -. DR OMA; YEDPAMW; -. DR OrthoDB; 9852947at2759; -. DR PAN-GO; P01303; 5 GO annotations based on evolutionary models. DR PhylomeDB; P01303; -. DR PathwayCommons; P01303; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes. DR SignaLink; P01303; -. DR SIGNOR; P01303; -. DR Agora; ENSG00000122585; -. DR BioGRID-ORCS; 4852; 4 hits in 1143 CRISPR screens. DR ChiTaRS; NPY; human. DR EvolutionaryTrace; P01303; -. DR GeneWiki; Neuropeptide_Y; -. DR GenomeRNAi; 4852; -. DR Pharos; P01303; Tbio. DR PRO; PR:P01303; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P01303; protein. DR Bgee; ENSG00000122585; Expressed in ganglionic eminence and 146 other cell types or tissues. DR ExpressionAtlas; P01303; baseline and differential. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0005246; F:calcium channel regulator activity; TAS:ProtInc. DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc. DR GO; GO:0160041; F:neuropeptide activity; IDA:UniProtKB. 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:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL. DR GO; GO:0021954; P:central nervous system neuron development; IEP:DFLAT. DR GO; GO:0021987; P:cerebral cortex development; IEP:DFLAT. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0048589; P:developmental growth; IEA:Ensembl. DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl. DR GO; GO:0007631; P:feeding behavior; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProt. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc. DR GO; GO:0060575; P:intestinal epithelial cell differentiation; TAS:GO_Central. DR GO; GO:0042117; P:monocyte activation; IEA:Ensembl. DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IEA:Ensembl. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:0031175; P:neuron projection development; IEP:DFLAT. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl. DR GO; GO:1904000; P:positive regulation of eating behavior; ISS:UniProt. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0032903; P:regulation of nerve growth factor production; IEA:Ensembl. DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl. DR GO; GO:0048572; P:short-day photoperiodism; IEA:Ensembl. DR GO; GO:0099538; P:synaptic signaling via neuropeptide; IEA:Ensembl. 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:SF5; PRO-NEUROPEPTIDE Y; 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 PDBsum; 1QFA; -. DR PDBsum; 1RON; -. DR PDBsum; 7RTA; -. DR PDBsum; 7VGX; -. DR PDBsum; 7X9A; -. DR PDBsum; 7X9B; -. DR PDBsum; 7YOO; -. DR PDBsum; 8K6M; -. DR PDBsum; 8K6N; -. DR PDBsum; 8K6O; -. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Cleavage on pair of basic residues; KW Cytoplasmic vesicle; Neuropeptide; Phosphoprotein; KW Proteomics identification; Reference proteome; Secreted; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000269|PubMed:6589611" FT PEPTIDE 29..64 FT /note="Neuropeptide Y" FT /id="PRO_0000025321" FT PEPTIDE 68..97 FT /note="C-flanking peptide of NPY" FT /id="PRO_0000025322" FT SITE 30..31 FT /note="Cleavage; by FAP" FT /evidence="ECO:0000269|PubMed:21314817" FT MOD_RES 64 FT /note="Tyrosine amide" FT /evidence="ECO:0000269|PubMed:6589611" FT MOD_RES 83 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 7 FT /note="L -> P (in dbSNP:rs16139)" FT /id="VAR_014598" FT VARIANT 22 FT /note="L -> M (in dbSNP:rs5571)" FT /id="VAR_014599" FT MUTAGEN 1..30 FT /note="Missing: Decreased NPY1R activation and signaling." FT /evidence="ECO:0000269|PubMed:35165283" FT MUTAGEN 29..30 FT /note="YP->AA: Decreased NPY1R activation and signaling." FT /evidence="ECO:0000269|PubMed:35165283" FT MUTAGEN 59 FT /note="I->L: Has no effect on NPY1R activation and FT signaling; when associated in cis with P-62. Decreased FT NPY2R activation and signaling; when associated in cis with FT P-62." FT /evidence="ECO:0000269|PubMed:1321422, FT ECO:0000269|PubMed:38882210" FT MUTAGEN 62 FT /note="Q->P: Has no effect on NPY1R activation and FT signaling; when associated in cis with L-59. Decreased FT NPY2R activation and signaling; when associated in cis with FT L-59." FT /evidence="ECO:0000269|PubMed:1321422, FT ECO:0000269|PubMed:38882210" FT CONFLICT 53 FT /note="R -> G (in Ref. 2; AAA59945)" FT /evidence="ECO:0000305" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:7YOO" FT HELIX 42..61 FT /evidence="ECO:0007829|PDB:7RTA" SQ SEQUENCE 97 AA; 10851 MW; 832CF124321718F2 CRC64; MLGNKRLGLS GLTLALSLLV CLGALAEAYP SKPDNPGEDA PAEDMARYYS ALRHYINLIT RQRYGKRSSP ETLISDLLMR ESTENVPRTR LEDPAMW //