NPY1R_HUMAN
ID NPY1R_HUMAN Reviewed; 384 AA.
AC P25929; B2R6H5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Neuropeptide Y receptor type 1;
DE Short=NPY1-R;
GN Name=NPY1R; Synonyms=NPYR, NPYY1;
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].
RC TISSUE=Brain;
RX PubMed=1317848; DOI=10.1016/s0021-9258(19)49854-2;
RA Larhammar D., Blomqvist A.G., Yee F., Jazin E.E., Yoo H., Wahlestedt C.R.;
RT "Cloning and functional expression of a human neuropeptide Y/peptide YY
RT receptor of the Y1 type.";
RL J. Biol. Chem. 267:10935-10938(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=8095935; DOI=10.1016/s0021-9258(18)53306-8;
RA Herzog H., Baumgartner M., Vivero C., Selbie L.A., Auer B., Shine J.;
RT "Genomic organization, localization, and allelic differences in the gene
RT for the human neuropeptide Y Y1 receptor.";
RL J. Biol. Chem. 268:6703-6707(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Testis;
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).
CC -!- FUNCTION: Receptor for neuropeptide Y and peptide YY. The rank order of
CC affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34]
CC PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP
CC and PYY (3-36) > PP > NPY free acid.
CC -!- INTERACTION:
CC P25929; P10082: PYY; NbExp=2; IntAct=EBI-372227, EBI-6655667;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NPY1RID44260ch4q32.html";
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DR EMBL; M88461; AAA73215.1; -; mRNA.
DR EMBL; M84755; AAA59920.1; -; mRNA.
DR EMBL; L07614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L07615; AAA59947.1; -; mRNA.
DR EMBL; AY548168; AAS55647.1; -; mRNA.
DR EMBL; AK312578; BAG35472.1; -; mRNA.
DR EMBL; CH471056; EAX04841.1; -; Genomic_DNA.
DR EMBL; BC036657; AAH36657.1; -; mRNA.
DR EMBL; BC071720; AAH71720.1; -; mRNA.
DR CCDS; CCDS34089.1; -.
DR PIR; A45490; A45490.
DR RefSeq; NP_000900.1; NM_000909.5.
DR RefSeq; XP_005263088.1; XM_005263031.3.
DR RefSeq; XP_011530312.1; XM_011532010.2.
DR PDB; 5ZBQ; X-ray; 2.70 A; A=2-358.
DR PDB; 7VGX; EM; 3.20 A; R=1-384.
DR PDBsum; 5ZBQ; -.
DR PDBsum; 7VGX; -.
DR AlphaFoldDB; P25929; -.
DR BMRB; P25929; -.
DR SMR; P25929; -.
DR BioGRID; 110946; 3.
DR IntAct; P25929; 5.
DR STRING; 9606.ENSP00000354652; -.
DR BindingDB; P25929; -.
DR ChEMBL; CHEMBL4777; -.
DR DrugBank; DB05004; Peptide YY (3-36).
DR GuidetoPHARMACOLOGY; 305; -.
DR GlyGen; P25929; 3 sites.
DR iPTMnet; P25929; -.
DR PhosphoSitePlus; P25929; -.
DR BioMuta; NPY1R; -.
DR DMDM; 128997; -.
DR jPOST; P25929; -.
DR MassIVE; P25929; -.
DR PaxDb; P25929; -.
DR PeptideAtlas; P25929; -.
DR PRIDE; P25929; -.
DR ProteomicsDB; 54300; -.
DR Antibodypedia; 16963; 432 antibodies from 37 providers.
DR DNASU; 4886; -.
DR Ensembl; ENST00000296533.3; ENSP00000354652.2; ENSG00000164128.7.
DR GeneID; 4886; -.
DR KEGG; hsa:4886; -.
DR MANE-Select; ENST00000296533.3; ENSP00000354652.2; NM_000909.6; NP_000900.1.
DR UCSC; uc003iqm.3; human.
DR CTD; 4886; -.
DR DisGeNET; 4886; -.
DR GeneCards; NPY1R; -.
DR HGNC; HGNC:7956; NPY1R.
DR HPA; ENSG00000164128; Tissue enhanced (lymphoid).
DR MIM; 162641; gene.
DR neXtProt; NX_P25929; -.
DR OpenTargets; ENSG00000164128; -.
DR PharmGKB; PA258; -.
DR VEuPathDB; HostDB:ENSG00000164128; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160268; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; P25929; -.
DR OMA; KRNNMMD; -.
DR OrthoDB; 609835at2759; -.
DR PhylomeDB; P25929; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; P25929; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P25929; -.
DR SIGNOR; P25929; -.
DR BioGRID-ORCS; 4886; 13 hits in 1064 CRISPR screens.
DR ChiTaRS; NPY1R; human.
DR GeneWiki; Neuropeptide_Y_receptor_Y1; -.
DR GenomeRNAi; 4886; -.
DR Pharos; P25929; Tchem.
DR PRO; PR:P25929; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P25929; protein.
DR Bgee; ENSG00000164128; Expressed in blood vessel layer and 124 other tissues.
DR ExpressionAtlas; P25929; baseline and differential.
DR Genevisible; P25929; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; TAS:ProtInc.
DR GO; GO:0001602; F:pancreatic polypeptide receptor activity; IEA:Ensembl.
DR GO; GO:0001601; F:peptide YY receptor activity; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000351; NPY1_rcpt.
DR InterPro; IPR000611; NPY_rcpt.
DR PANTHER; PTHR24235:SF24; PTHR24235:SF24; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01013; NRPEPTIDEY1R.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Neuropeptide Y receptor type 1"
FT /id="PRO_0000069920"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21555"
FT LIPID 338
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 374
FT /note="K -> T (in dbSNP:rs5578)"
FT /id="VAR_014681"
FT CONFLICT 96
FT /note="F -> L (in Ref. 2; AAA59920)"
FT /evidence="ECO:0000305"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 37..67
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 74..92
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 110..142
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 152..176
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 221..240
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 259..288
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 296..321
FT /evidence="ECO:0007829|PDB:5ZBQ"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:5ZBQ"
SQ SEQUENCE 384 AA; 44392 MW; 582B0DDB04490316 CRC64;
MNSTLFSQVE NHSVHSNFSE KNAQLLAFEN DDCHLPLAMI FTLALAYGAV IILGVSGNLA
LIIIILKQKE MRNVTNILIV NLSFSDLLVA IMCLPFTFVY TLMDHWVFGE AMCKLNPFVQ
CVSITVSIFS LVLIAVERHQ LIINPRGWRP NNRHAYVGIA VIWVLAVASS LPFLIYQVMT
DEPFQNVTLD AYKDKYVCFD QFPSDSHRLS YTTLLLVLQY FGPLCFIFIC YFKIYIRLKR
RNNMMDKMRD NKYRSSETKR INIMLLSIVV AFAVCWLPLT IFNTVFDWNH QIIATCNHNL
LFLLCHLTAM ISTCVNPIFY GFLNKNFQRD LQFFFNFCDF RSRDDDYETI AMSTMHTDVS
KTSLKQASPV AFKKINNNDD NEKI
