ID NPY1R_MOUSE Reviewed; 382 AA. AC Q04573; Q61993; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 04-NOV-2026, entry version 191. DE RecName: Full=Neuropeptide Y receptor type 1; DE Short=NPY1-R; GN Name=Npy1r; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=1468559; DOI=10.1016/0014-5793(92)81490-d; RA Eva C., Oberto A., Sprengel R., Genazzani E.; RT "The murine NPY-1 receptor gene. Structure and delineation of tissue- RT specific expression."; RL FEBS Lett. 314:285-288(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=8530415; DOI=10.1074/jbc.270.50.30102; RA Nakamura M., Sakanaka C., Aoki Y., Ogasawara H., Tsuji T., Kodama H., RA Matsumoto T., Shimizu T., Noma M.; RT "Identification of two isoforms of mouse neuropeptide Y-Y1 receptor RT generated by alternative splicing. Isolation, genomic structure, and RT functional expression of the receptors."; RL J. Biol. Chem. 270:30102-30110(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NPY1-R ALPHA). RC TISSUE=Eye; 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 [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9623984; DOI=10.1038/nm0698-722; RA Pedrazzini T., Seydoux J., Kuenstner P., Aubert J.F., Grouzmann E., RA Beermann F., Brunner H.R.; RT "Cardiovascular response, feeding behavior and locomotor activity in mice RT lacking the NPY Y1 receptor."; RL Nat. Med. 4:722-726(1998). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION. RX PubMed=21457230; DOI=10.1111/j.1476-5381.2011.01401.x; RA Tough I.R., Forbes S., Tolhurst R., Ellis M., Herzog H., Bornstein J.C., RA Cox H.M.; RT "Endogenous peptide YY and neuropeptide Y inhibit colonic ion transport, RT contractility and transit differentially via Y(1) and Y(2) receptors."; RL Br. J. Pharmacol. 164:471-484(2011). CC -!- FUNCTION: Receptor for neuropeptide Y (NPY) and peptide YY (PYY). Can CC also bind with high affinity [Leu-31, Pro-34]NPY, an analog of NPY CC modified at residues 31 and 34 of the mature form, while having CC virtually no affinity for pancreatic polypeptide (PP/PPY) at CC physiological concentrations. NPY or PYY binding induces adenylate CC cyclase-inhibiting G protein-coupled receptor signaling, resulting in CC inhibition of cAMP production. Receptor activation by ligands also CC leads to an increase of intracellular Ca(2+) levels. As a receptor for CC NPY, it is involved in the regulation of eating behavior and NPY- CC induced stimulation of food intake (PubMed:9623984). Involved in the CC regulation of colonic antisecretory tone, and colonic contractility CC (PubMed:21457230). {ECO:0000250|UniProtKB:P25929, CC ECO:0000269|PubMed:21457230, ECO:0000269|PubMed:9623984}. CC -!- SUBUNIT: Interacts with GNAI1; the interaction stabilizes the receptor CC in the high affinity state for NPY. {ECO:0000250|UniProtKB:P25929}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25929}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P25929}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=NPY1-R alpha; CC IsoId=Q04573-1; Sequence=Displayed; CC Name=NPY1-R beta; CC IsoId=Q04573-2; Sequence=VSP_001912, VSP_001913; CC -!- TISSUE SPECIFICITY: The alpha form is highly expressed in the brain, CC heart, kidney, spleen, skeletal muscle, and lung, whereas the beta CC receptor mRNA was not detected in these tissues (PubMed:8530415). CC However, the beta form is expressed in mouse embryonic developmental CC stage (7 and 11 days), bone marrow cells and several hematopoietic cell CC lines (PubMed:8530415). {ECO:0000269|PubMed:8530415}. CC -!- DEVELOPMENTAL STAGE: The beta form is expressed in embryonic CC developmental stage (7 and 11 days). The beta form is an embryonic and CC a bone marrow form of NPY1-R, which decreases in the expression during CC development and differentiation. {ECO:0000269|PubMed:8530415}. CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit a lower daily food intake CC than wild-type animals, and a diminished refeeding response following a CC 24-hour period of fasting. {ECO:0000269|PubMed:9623984}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; Z18280; CAA79157.1; -; Genomic_DNA. DR EMBL; Z18281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D63818; BAA09887.1; -; mRNA. DR EMBL; D63819; BAA09888.1; -; mRNA. DR EMBL; BC051420; AAH51420.1; -; mRNA. DR CCDS; CCDS22336.1; -. [Q04573-1] DR PIR; S27388; S27388. DR RefSeq; NP_001345884.1; NM_001358955.1. [Q04573-1] DR RefSeq; NP_035064.1; NM_010934.4. [Q04573-1] DR RefSeq; XP_006509657.1; XM_006509594.5. [Q04573-1] DR RefSeq; XP_006509658.1; XM_006509595.5. [Q04573-1] DR RefSeq; XP_036009704.1; XM_036153811.1. [Q04573-1] DR RefSeq; XP_036009705.1; XM_036153812.1. [Q04573-1] DR AlphaFoldDB; Q04573; -. DR SMR; Q04573; -. DR CORUM; Q04573; -. DR FunCoup; Q04573; 760. DR STRING; 10090.ENSMUSP00000045530; -. DR BindingDB; Q04573; -. DR ChEMBL; CHEMBL4739851; -. DR GuidetoPHARMACOLOGY; 305; -. DR GlyCosmos; Q04573; 3 sites, No reported glycans. DR GlyGen; Q04573; 3 sites, 1 N-linked glycan (1 site). DR iPTMnet; Q04573; -. DR PhosphoSitePlus; Q04573; -. DR PaxDb; 10090-ENSMUSP00000045530; -. DR ProteomicsDB; 293883; -. [Q04573-1] DR Antibodypedia; 16963; 464 antibodies from 40 providers. DR DNASU; 18166; -. DR Ensembl; ENSMPUT00000001894; ENSMPUP00000001858; ENSMPUG00000001873. DR Ensembl; ENSMUST00000039303.7; ENSMUSP00000045530.6; ENSMUSG00000036437.7. [Q04573-1] DR Ensembl; ENSMUST00000212588.2; ENSMUSP00000148417.2; ENSMUSG00000036437.7. [Q04573-1] DR GeneID; 18166; -. DR KEGG; mmu:18166; -. DR UCSC; uc009lvt.2; mouse. [Q04573-1] DR AGR; MGI:104963; -. DR CTD; 4886; -. DR MGI; MGI:104963; Npy1r. DR VEuPathDB; HostDB:ENSMUSG00000036437; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000160268; -. DR HOGENOM; CLU_009579_6_1_1; -. DR InParanoid; Q04573; -. DR OMA; AENHSIY; -. DR OrthoDB; 9046662at2759; -. DR PhylomeDB; Q04573; -. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 18166; 3 hits in 76 CRISPR screens. DR PRO; PR:Q04573; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q04573; protein. DR Bgee; ENSMUSG00000036437; Expressed in ascending aorta and 107 other cell types or tissues. DR ExpressionAtlas; Q04573; baseline and differential. DR GO; GO:0030424; C:axon; ISO:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0098992; C:neuronal dense core vesicle; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0042734; C:presynaptic membrane; ISO:GO_Central. DR GO; GO:0008021; C:synaptic vesicle; ISO:GO_Central. DR GO; GO:0008188; F:neuropeptide receptor activity; ISO:GO_Central. DR GO; GO:0004983; F:neuropeptide Y receptor activity; IDA:MGI. DR GO; GO:0001602; F:pancreatic polypeptide receptor activity; IDA:MGI. DR GO; GO:0001601; F:peptide YY receptor activity; IDA:MGI. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:GO_Central. DR GO; GO:0007631; P:feeding behavior; IMP:MGI. DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISO:GO_Central. DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:GO_Central. DR GO; GO:0046888; P:negative regulation of hormone secretion; ISO:GO_Central. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:GO_Central. DR GO; GO:0030432; P:peristalsis; ISO:GO_Central. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:GO_Central. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:GO_Central. DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI. DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI. DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:GO_Central. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:GO_Central. DR GO; GO:0043278; P:response to morphine; ISO:GO_Central. DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI. DR GO; GO:0099538; P:synaptic signaling via neuropeptide; ISO:GO_Central. DR CDD; cd15395; 7tmA_NPY1R; 1. DR FunFam; 1.20.1070.10:FF:000062; Neuropeptide Y receptor type 1; 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; IPR000351; NPY1_rcpt. DR InterPro; IPR000611; NPY_rcpt. DR PANTHER; PTHR24235; NEUROPEPTIDE Y RECEPTOR; 1. DR PANTHER; PTHR24235:SF24; NEUROPEPTIDE Y RECEPTOR TYPE 1; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01013; NRPEPTIDEY1R. DR PRINTS; PR01012; NRPEPTIDEYR. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. 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 Alternative splicing; Cell membrane; Disulfide bond; KW G protein-coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..382 FT /note="Neuropeptide Y receptor type 1" FT /id="PRO_0000069921" FT TOPO_DOM 1..36 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 37..62 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 63..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 76..98 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 99..109 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 110..135 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 136..153 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 154..174 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 175..207 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 208..232 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 233..261 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 262..284 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 285..298 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 299..322 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P25929" FT TOPO_DOM 323..382 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21555" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT LIPID 337 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" 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 112..197 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 304..307 FT /note="CHLT -> LNMN (in isoform NPY1-R beta)" FT /evidence="ECO:0000305" FT /id="VSP_001912" FT VAR_SEQ 308..382 FT /note="Missing (in isoform NPY1-R beta)" FT /evidence="ECO:0000305" FT /id="VSP_001913" SQ SEQUENCE 382 AA; 44015 MW; CDCCF93E3ABB4D70 CRC64; MNSTLFSKVE NHSIHYNASE NSPLLAFEND DCHLPLAVIF TLALAYGAVI ILGVSGNLAL IIIILKQKEM RNVTNILIVN LSFSDLLVAV MCLPFTFVYT LMDHWVFGET MCKLNPFVQC VSITVSIFSL VLIAVERHQL IINPRGWRPN NRHAYIGITV IWVLAVASSL PFVIYQILTD EPFQNVSLAA FKDKYVCFDK FPSDSHRLSY TTLLLVLQYF GPLCFIFICY FKIYIRLKRR NNMMDKIRDS KYRSSETKRI NIMLLSIVVA FAVCWLPLTI FNTVFDWNHQ IIATCNHNLL FLLCHLTAMI STCVNPIFYG FLNKNFQRDL QFFFNFCDFR SRDDDYETIA MSTMHTDVSK TSLKQASPVA FKKISMNDNE KV //