ID   NPY5R_RAT               Reviewed;         445 AA.
AC   Q63634; P70586;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 155.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
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=Brain;
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].
RC   TISSUE=Brain;
RX   PubMed=9669502; DOI=10.1016/s0014-2999(98)00171-x;
RA   Parker E.M., Babij C.K., Balasubramaniam A., Burrier R.E., Guzzi M.,
RA   Hamud F., Mukhopadhyay G., Rudinski M.S., Tao Z., Tice M., Xia L.,
RA   Mullins D.E., Salisbury B.G.;
RT   "GR231118 (1229U91) and other analogues of the C-terminus of neuropeptide Y
RT   are potent neuropeptide Y Y1 receptor antagonists and neuropeptide Y Y4
RT   receptor agonists.";
RL   Eur. J. Pharmacol. 349:97-105(1998).
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=AAC52677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U66274; AAC52845.1; -; mRNA.
DR   EMBL; U56078; AAC52677.1; ALT_INIT; mRNA.
DR   EMBL; AF044264; AAC15670.1; -; mRNA.
DR   RefSeq; NP_037001.1; NM_012869.1.
DR   RefSeq; XP_006253075.1; XM_006253013.3.
DR   RefSeq; XP_006253076.1; XM_006253014.3.
DR   RefSeq; XP_017455484.1; XM_017599995.1.
DR   RefSeq; XP_017455485.1; XM_017599996.1.
DR   RefSeq; XP_017455486.1; XM_017599997.1.
DR   RefSeq; XP_017455487.1; XM_017599998.1.
DR   AlphaFoldDB; Q63634; -.
DR   SMR; Q63634; -.
DR   IntAct; Q63634; 1.
DR   STRING; 10116.ENSRNOP00000018976; -.
DR   BindingDB; Q63634; -.
DR   ChEMBL; CHEMBL2548; -.
DR   GuidetoPHARMACOLOGY; 308; -.
DR   GlyGen; Q63634; 2 sites.
DR   PhosphoSitePlus; Q63634; -.
DR   PaxDb; Q63634; -.
DR   Ensembl; ENSRNOT00000018976; ENSRNOP00000018976; ENSRNOG00000014172.
DR   Ensembl; ENSRNOT00000099301; ENSRNOP00000089710; ENSRNOG00000014172.
DR   Ensembl; ENSRNOT00000109751; ENSRNOP00000086593; ENSRNOG00000014172.
DR   GeneID; 25340; -.
DR   KEGG; rno:25340; -.
DR   UCSC; RGD:3199; rat.
DR   CTD; 4889; -.
DR   RGD; 3199; Npy5r.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161766; -.
DR   HOGENOM; CLU_009579_6_1_1; -.
DR   InParanoid; Q63634; -.
DR   OMA; CHVMPFL; -.
DR   OrthoDB; 609835at2759; -.
DR   PhylomeDB; Q63634; -.
DR   TreeFam; TF315303; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:Q63634; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000014172; Expressed in frontal cortex and 2 other tissues.
DR   Genevisible; Q63634; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
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; IDA:RGD.
DR   GO; GO:0001602; F:pancreatic polypeptide receptor activity; IDA:RGD.
DR   GO; GO:0001601; F:peptide YY receptor activity; IDA:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISO:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0042755; P:eating behavior; IMP:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0060112; P:generation of ovulation cycle rhythm; IMP:RGD.
DR   GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IDA:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0014050; P:negative regulation of glutamate secretion; IMP:RGD.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:RGD.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
DR   GO; GO:0002675; P:positive regulation of acute inflammatory response; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
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_0000069942"
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..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           441
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;  50408 MW;  D529EC04FF8DF62A CRC64;
     MEFKLEEHFN KTFVTENNTA AARNAAFPAW EDYRGSVDDL QYFLIGLYTF VSLLGFMGNL
     LILMAVMKKR NQKTTVNFLI GNLAFSDILV VLFCSPFTLT SVLLDQWMFG KAMCHIMPFL
     QCVSVLVSTL ILISIAIVRY HMIKHPISNN LTANHGYFLI ATVWTLGFAI CSPLPVFHSL
     VELKETFGSA LLSSKYLCVE SWPSDSYRIA FTISLLLVQY ILPLVCLTVS HTSVCRSISC
     GLSHKENRLE ENEMINLTLQ PSKKSRNQAK TPSTQKWSYS FIRKHRRRYS KKTACVLPAP
     AGPSQGKHLA VPENPASVRS QLSPSSKVIP GVPICFEVKP EESSDAHEMR VKRSITRIKK
     RSRSVFYRLT ILILVFAVSW MPLHVFHVVT DFNDNLISNR HFKLVYCICH LLGMMSCCLN
     PILYGFLNNG IKADLRALIH CLHMS