ID   NPY2R_MOUSE             Reviewed;         381 AA.
AC   P97295; F7C6W7; Q8BWV1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 2.
DT   02-SEP-2026, entry version 181.
DE   RecName: Full=Neuropeptide Y receptor type 2 {ECO:0000303|PubMed:8914576};
DE            Short=NPY2-R;
DE   AltName: Full=NPY-Y2 receptor {ECO:0000303|PubMed:8914576};
DE            Short=Y2 receptor;
GN   Name=Npy2r;
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 [MRNA], AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=8914576; DOI=10.1016/s0005-2736(96)00166-6;
RA   Nakamura M., Aoki Y., Hirano D.;
RT   "Cloning and functional expression of a cDNA encoding a mouse type 2
RT   neuropeptide Y receptor.";
RL   Biochim. Biophys. Acta 1284:134-137(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=10436066; DOI=10.1523/jneurosci.19-16-07130.1999;
RA   Broberger C., Johansen J., Brismar H., Johansson C., Schalling M.,
RA   Hoekfelt T.;
RT   "Changes in neuropeptide Y receptors and pro-opiomelanocortin in the
RT   anorexia (anx/anx) mouse hypothalamus.";
RL   J. Neurosci. 19:7130-7139(1999).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12167864; DOI=10.1038/nature00887;
RA   Batterham R.L., Cowley M.A., Small C.J., Herzog H., Cohen M.A., Dakin C.L.,
RA   Wren A.M., Brynes A.E., Low M.J., Ghatei M.A., Cone R.D., Bloom S.R.;
RT   "Gut hormone PYY(3-36) physiologically inhibits food intake.";
RL   Nature 418:650-654(2002).
RN   [8]
RP   FUNCTION (PEPTIDE YY(3-36)).
RX   PubMed=16280589; DOI=10.1523/jneurosci.2552-05.2005;
RA   Acuna-Goycolea C., van den Pol A.N.;
RT   "Peptide YY(3-36) inhibits both anorexigenic proopiomelanocortin and
RT   orexigenic neuropeptide Y neurons: implications for hypothalamic regulation
RT   of energy homeostasis.";
RL   J. Neurosci. 25:10510-10519(2005).
RN   [9]
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)
CC       (PubMed:8914576). Can also bind with lower affinity pancreatic
CC       polypeptide (PP/PPY) and [Leu-31, Pro-34]NPY, an analog of NPY modified
CC       at residues 31 and 34 of the mature form (By similarity). NPY or PYY
CC       binding induces adenylate cyclase-inhibiting G protein-coupled receptor
CC       signaling, resulting in inhibition of cAMP production. Receptor
CC       activation by ligands also leads to an increase of intracellular Ca(2+)
CC       levels (PubMed:8914576). Involved in the regulation of colonic
CC       antisecretory tone, and colonic contractility (PubMed:21457230). As
CC       receptor for peptide PYY(3-36) in the arcuate nucleus of the
CC       hypothalamus, it is involved in the down-regulation of appetite and
CC       food intake (PubMed:12167864, PubMed:16280589).
CC       {ECO:0000250|UniProtKB:P49146, ECO:0000269|PubMed:21457230,
CC       ECO:0000269|PubMed:8914576}.
CC   -!- SUBUNIT: Interacts with GNAI1; the interaction stabilizes the receptor
CC       in the high affinity state for NPY. Upon activation by NPY or PYY,
CC       interacts with ARRB2. {ECO:0000250|UniProtKB:P49146}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P49146};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P49146}.
CC   -!- TISSUE SPECIFICITY: Expressed in the arcuate nucleus of hypothalamus.
CC       {ECO:0000269|PubMed:10436066}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice show no response to PYY(3-36), and
CC       the peptide does not reduce their food intake.
CC       {ECO:0000269|PubMed:12167864}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D86238; BAA13050.1; ALT_INIT; mRNA.
DR   EMBL; AK049892; BAC33975.1; -; mRNA.
DR   EMBL; AC091478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466547; EDL15430.1; -; Genomic_DNA.
DR   EMBL; CH466547; EDL15431.1; -; Genomic_DNA.
DR   EMBL; BC104490; AAI04491.1; -; mRNA.
DR   EMBL; BC104734; AAI04735.1; -; mRNA.
DR   CCDS; CCDS59646.1; -.
DR   RefSeq; NP_001397372.1; NM_001410443.1.
DR   RefSeq; NP_001397373.1; NM_001410444.1.
DR   RefSeq; NP_001397374.1; NM_001410445.1.
DR   RefSeq; NP_032757.2; NM_008731.4.
DR   AlphaFoldDB; P97295; -.
DR   SMR; P97295; -.
DR   CORUM; P97295; -.
DR   FunCoup; P97295; 627.
DR   STRING; 10090.ENSMUSP00000029633; -.
DR   BindingDB; P97295; -.
DR   ChEMBL; CHEMBL4739850; -.
DR   GlyCosmos; P97295; 1 site, No reported glycans.
DR   GlyGen; P97295; 2 sites.
DR   iPTMnet; P97295; -.
DR   PhosphoSitePlus; P97295; -.
DR   PaxDb; 10090-ENSMUSP00000029633; -.
DR   ProteomicsDB; 253100; -.
DR   Antibodypedia; 2964; 335 antibodies from 40 providers.
DR   DNASU; 18167; -.
DR   Ensembl; ENSMUST00000029633.5; ENSMUSP00000029633.5; ENSMUSG00000028004.13.
DR   Ensembl; ENSMUST00000098997.5; ENSMUSP00000096595.5; ENSMUSG00000028004.13.
DR   Ensembl; ENSMUST00000182831.2; ENSMUSP00000138282.2; ENSMUSG00000028004.13.
DR   GeneID; 18167; -.
DR   KEGG; mmu:18167; -.
DR   UCSC; uc008ppa.1; mouse.
DR   AGR; MGI:108418; -.
DR   CTD; 4887; -.
DR   MGI; MGI:108418; Npy2r.
DR   VEuPathDB; HostDB:ENSMUSG00000028004; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000155973; -.
DR   HOGENOM; CLU_009579_6_1_1; -.
DR   InParanoid; P97295; -.
DR   OMA; WPGKNTD; -.
DR   OrthoDB; 9046662at2759; -.
DR   PhylomeDB; P97295; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 18167; 2 hits in 78 CRISPR screens.
DR   PRO; PR:P97295; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P97295; protein.
DR   Bgee; ENSMUSG00000028004; Expressed in median eminence of neurohypophysis and 85 other cell types or tissues.
DR   ExpressionAtlas; P97295; baseline and differential.
DR   GO; GO:0097731; C:9+0 non-motile cilium; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:GO_Central.
DR   GO; GO:0008188; F:neuropeptide receptor activity; ISO:GO_Central.
DR   GO; GO:0004983; F:neuropeptide Y receptor activity; IDA:UniProtKB.
DR   GO; GO:0001601; F:peptide YY receptor activity; IDA:UniProtKB.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISO:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:1903999; P:negative regulation of eating behavior; IMP:UniProtKB.
DR   GO; GO:1904456; P:negative regulation of neuronal action potential; IDA:UniProtKB.
DR   GO; GO:0002792; P:negative regulation of peptide secretion; IDA:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISO:GO_Central.
DR   CDD; cd15399; 7tmA_NPY2R; 1.
DR   FunFam; 1.20.1070.10:FF:000158; Neuropeptide Y receptor type 2; 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; IPR001358; NPY2_rcpt.
DR   InterPro; IPR000611; NPY_rcpt.
DR   PANTHER; PTHR24235; NEUROPEPTIDE Y RECEPTOR; 1.
DR   PANTHER; PTHR24235:SF20; NEUROPEPTIDE Y RECEPTOR TYPE 2; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01014; NRPEPTIDEY2R.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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   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..381
FT                   /note="Neuropeptide Y receptor type 2"
FT                   /id="PRO_0000069930"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        46..73
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        74..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        87..113
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        114..119
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        120..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        147..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        164..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        187..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        214..240
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        241..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        268..292
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        293..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        302..326
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P49146"
FT   TOPO_DOM        327..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           342
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   381 AA;  42628 MW;  90787C051347884A CRC64;
     MGPVGAEADE NQTVEVKVEP YGPGHTTPRG ELPPDPEPEL IDSTKLVEVQ VILILAYCSI
     ILLGVVGNSL VIHVVIKFKS MRTVTNFFIA NLAVADLLVN TLCLPFTLTY TLMGEWKMGP
     VLCHLVPYAQ GLAVQVSTIT LTVIALDRHR CIVYHLESKI SKRISFLIIG LAWGISALLA
     SPLAIFREYS LIEIIPDFEI VACTEKWPGE EKSVYGTVYS LSTLLILYVL PLGIISFSYT
     RIWSKLRNHV SPGAASDHYH QRRHKMTKML VCVVVVFAVS WLPLHAFQLA VDIDSHVLDL
     KEYKLIFTVF HIIAMCSTFA NPLLYGWMNS NYRKAFLSAF RCEQRLDAIH SEVSMTFKAK
     KNLEVKKNNG PTDSFSEATN V
//