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 27-MAR-2024, entry version 164.
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 GlyCosmos; Q63634; 2 sites, No reported glycans.
DR GlyGen; Q63634; 2 sites.
DR PhosphoSitePlus; Q63634; -.
DR PaxDb; 10116-ENSRNOP00000018976; -.
DR Ensembl; ENSRNOT00000018976.4; ENSRNOP00000018976.2; ENSRNOG00000014172.5.
DR Ensembl; ENSRNOT00000099301.1; ENSRNOP00000089710.1; ENSRNOG00000014172.5.
DR Ensembl; ENSRNOT00000109751.1; ENSRNOP00000086593.1; ENSRNOG00000014172.5.
DR Ensembl; ENSRNOT00055006027; ENSRNOP00055004550; ENSRNOG00055003823.
DR Ensembl; ENSRNOT00055006030; ENSRNOP00055004553; ENSRNOG00055003823.
DR Ensembl; ENSRNOT00055006032; ENSRNOP00055004555; ENSRNOG00055003823.
DR Ensembl; ENSRNOT00060025345; ENSRNOP00060020205; ENSRNOG00060014829.
DR Ensembl; ENSRNOT00060025350; ENSRNOP00060020210; ENSRNOG00060014829.
DR Ensembl; ENSRNOT00060025358; ENSRNOP00060020219; ENSRNOG00060014829.
DR Ensembl; ENSRNOT00065007300; ENSRNOP00065005074; ENSRNOG00065004991.
DR Ensembl; ENSRNOT00065007304; ENSRNOP00065005076; ENSRNOG00065004991.
DR Ensembl; ENSRNOT00065007308; ENSRNOP00065005077; ENSRNOG00065004991.
DR GeneID; 25340; -.
DR KEGG; rno:25340; -.
DR UCSC; RGD:3199; rat.
DR AGR; RGD:3199; -.
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; VMCHVMP; -.
DR OrthoDB; 5361264at2759; -.
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 cell types or tissues.
DR Genevisible; Q63634; RN.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
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:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0042923; F:neuropeptide binding; 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: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 GO; GO:0099538; P:synaptic signaling via neuropeptide; ISO:RGD.
DR CDD; cd15398; 7tmA_NPY5R; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000393; NPY5_rcpt.
DR InterPro; IPR000611; NPY_rcpt.
DR PANTHER; PTHR24235; NEUROPEPTIDE Y RECEPTOR; 1.
DR PANTHER; PTHR24235:SF10; NEUROPEPTIDE Y RECEPTOR TYPE 5; 1.
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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//
