NPY5R_HUMAN
ID NPY5R_HUMAN Reviewed; 445 AA.
AC Q15761; Q6GTR7; Q92916;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Neuropeptide Y receptor type 5;
DE Short=NPY5-R;
DE AltName: Full=NPY-Y5 receptor;
DE Short=NPYY5-R;
DE Short=Y5 receptor;
GN Name=NPY5R; Synonyms=NPYR5;
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].
RX PubMed=8824284; DOI=10.1074/jbc.271.42.26044;
RA Hu Y., Bloomquist B.T., Cornfield L.J., Decarr L.B., Flores-Riveros J.R.,
RA Friedman L., Jiang P., Lewis-Higgins L., Sadlowski Y., Schaefer J.,
RA Velazquez N., McCaleb M.L.;
RT "Identification of a novel hypothalamic neuropeptide Y receptor associated
RT with feeding behavior.";
RL J. Biol. Chem. 271:26315-26319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RX PubMed=8700207; DOI=10.1038/382168a0;
RA Gerald C., Walker M.W., Criscione L., Gustafson E.L., Batzl-Hartmann C.,
RA Smith K.E., Vaysse P., Durkin M.M., Laz T.M., Linemeyer D.L.,
RA Schaffhauser A.O., Whitebread S., Hofbauer K.G., Taber R.I., Branchek T.A.,
RA Weinshank R.L.;
RT "A receptor subtype involved in neuropeptide-Y-induced food intake.";
RL Nature 382:168-171(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9169127; DOI=10.1006/geno.1997.4684;
RA Herzog H., Darby K., Ball H., Hort Y., Beck-Sickinger A., Shine J.;
RT "Overlapping gene structure of the human neuropeptide Y receptor subtypes
RT Y1 and Y5 suggests coordinate transcriptional regulation.";
RL Genomics 41:315-319(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "Isolation of complete coding sequence for neuropeptide Y receptor Y5
RT (NPY5R).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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=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).
CC -!- FUNCTION: Receptor for neuropeptide Y and peptide YY. The activity of
CC this receptor is mediated by G proteins that inhibit adenylate cyclase
CC activity. Seems to be associated with food intake. Could be involved in
CC feeding disorders.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Brain; hypothalamus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U66275; AAC50741.1; -; mRNA.
DR EMBL; U56079; AAC50623.1; ALT_INIT; mRNA.
DR EMBL; U94320; AAC51295.1; -; mRNA.
DR EMBL; AY322538; AAP84351.1; -; Genomic_DNA.
DR EMBL; AC079238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04839.1; -; Genomic_DNA.
DR EMBL; BC042416; AAH42416.1; -; mRNA.
DR CCDS; CCDS3804.1; -.
DR RefSeq; NP_001304020.1; NM_001317091.1.
DR RefSeq; NP_001304021.1; NM_001317092.1.
DR RefSeq; NP_006165.1; NM_006174.3.
DR RefSeq; XP_005263095.1; XM_005263038.3.
DR RefSeq; XP_011530319.1; XM_011532017.2.
DR AlphaFoldDB; Q15761; -.
DR BMRB; Q15761; -.
DR SMR; Q15761; -.
DR BioGRID; 110949; 2.
DR IntAct; Q15761; 3.
DR STRING; 9606.ENSP00000423917; -.
DR BindingDB; Q15761; -.
DR ChEMBL; CHEMBL4561; -.
DR DrugBank; DB05004; Peptide YY (3-36).
DR GuidetoPHARMACOLOGY; 308; -.
DR GlyGen; Q15761; 2 sites.
DR iPTMnet; Q15761; -.
DR PhosphoSitePlus; Q15761; -.
DR BioMuta; NPY5R; -.
DR DMDM; 215274093; -.
DR PaxDb; Q15761; -.
DR PeptideAtlas; Q15761; -.
DR PRIDE; Q15761; -.
DR Antibodypedia; 2946; 276 antibodies from 33 providers.
DR DNASU; 4889; -.
DR Ensembl; ENST00000338566.8; ENSP00000339377.3; ENSG00000164129.12.
DR Ensembl; ENST00000506953.1; ENSP00000423474.1; ENSG00000164129.12.
DR Ensembl; ENST00000515560.1; ENSP00000423917.1; ENSG00000164129.12.
DR GeneID; 4889; -.
DR KEGG; hsa:4889; -.
DR MANE-Select; ENST00000338566.8; ENSP00000339377.3; NM_006174.4; NP_006165.1.
DR UCSC; uc003iqn.3; human.
DR CTD; 4889; -.
DR DisGeNET; 4889; -.
DR GeneCards; NPY5R; -.
DR HGNC; HGNC:7958; NPY5R.
DR HPA; ENSG00000164129; Tissue enhanced (adipose tissue, lymphoid tissue).
DR MIM; 602001; gene.
DR neXtProt; NX_Q15761; -.
DR OpenTargets; ENSG00000164129; -.
DR PharmGKB; PA31742; -.
DR VEuPathDB; HostDB:ENSG00000164129; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161766; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q15761; -.
DR OMA; CHVMPFL; -.
DR OrthoDB; 609835at2759; -.
DR PhylomeDB; Q15761; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; Q15761; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q15761; -.
DR SIGNOR; Q15761; -.
DR BioGRID-ORCS; 4889; 8 hits in 1057 CRISPR screens.
DR GeneWiki; Neuropeptide_Y_receptor_Y5; -.
DR GenomeRNAi; 4889; -.
DR Pharos; Q15761; Tchem.
DR PRO; PR:Q15761; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q15761; protein.
DR Bgee; ENSG00000164129; Expressed in blood vessel layer and 99 other tissues.
DR Genevisible; Q15761; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0045202; C:synapse; IEA:GOC.
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; IBA:GO_Central.
DR GO; GO:0001601; F:peptide YY receptor activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060112; P:generation of ovulation cycle rhythm; IEA:Ensembl.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR CDD; cd15398; 7tmA_NPY5R; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000393; NPY5_rcpt.
DR InterPro; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01016; NRPEPTIDEY5R.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..445
FT /note="Neuropeptide Y receptor type 5"
FT /id="PRO_0000069939"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 442
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
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 114..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 445 AA; 50727 MW; A2B0F3169DBA66BE CRC64;
MDLELDEYYN KTLATENNTA ATRNSDFPVW DDYKSSVDDL QYFLIGLYTF VSLLGFMGNL
LILMALMKKR NQKTTVNFLI GNLAFSDILV VLFCSPFTLT SVLLDQWMFG KVMCHIMPFL
QCVSVLVSTL ILISIAIVRY HMIKHPISNN LTANHGYFLI ATVWTLGFAI CSPLPVFHSL
VELQETFGSA LLSSRYLCVE SWPSDSYRIA FTISLLLVQY ILPLVCLTVS HTSVCRSISC
GLSNKENRLE ENEMINLTLH PSKKSGPQVK LSGSHKWSYS FIKKHRRRYS KKTACVLPAP
ERPSQENHSR ILPENFGSVR SQLSSSSKFI PGVPTCFEIK PEENSDVHEL RVKRSVTRIK
KRSRSVFYRL TILILVFAVS WMPLHLFHVV TDFNDNLISN RHFKLVYCIC HLLGMMSCCL
NPILYGFLNN GIKADLVSLI HCLHM
