GPR61_MOUSE
ID GPR61_MOUSE Reviewed; 449 AA.
AC Q8C010; Q3UZR6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=G-protein coupled receptor 61;
GN Name=Gpr61;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Olfactory bulb;
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 [2]
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 [3]
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 [4]
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 [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21971119; DOI=10.1016/j.lfs.2011.09.002;
RA Nambu H., Fukushima M., Hikichi H., Inoue T., Nagano N., Tahara Y.,
RA Nambu T., Ito J., Ogawa Y., Ozaki S., Ohta H.;
RT "Characterization of metabolic phenotypes of mice lacking GPR61, an orphan
RT G-protein coupled receptor.";
RL Life Sci. 89:765-772(2011).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=28912303; DOI=10.1530/rep-17-0333;
RA Muroi T., Matsushima Y., Kanamori R., Inoue H., Fujii W., Yogo K.;
RT "GPR62 constitutively activates cAMP signaling but is dispensable for male
RT fertility in mice.";
RL Reproduction 154:755-764(2017).
CC -!- FUNCTION: Orphan G-protein coupled receptor. Constitutively activates
CC the G(s)-alpha/cAMP signaling pathway (By similarity). Shows a
CC reciprocal regulatory interaction with the melatonin receptor MTNR1B
CC most likely through receptor heteromerization (By similarity). May be
CC involved in the regulation of food intake and body weight
CC (PubMed:21971119). {ECO:0000250|UniProtKB:Q9BZJ8,
CC ECO:0000269|PubMed:21971119}.
CC -!- SUBUNIT: Forms heterodimer with MTNR1B. Interacts with ARRB1 and ARRB2
CC in a spontaneous and agonist-independent manner; leading to the
CC internalization of GPR61 in the endosomal compartment (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZJ8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BZJ8};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9BZJ8}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with ARRB2/beta-arrestin-2 in the
CC endosome (By similarity). {ECO:0000250|UniProtKB:Q9BZJ8}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain and testes,
CC with relatively lower expression observed in the eye, adrenal gland and
CC pituitary gland. {ECO:0000269|PubMed:21971119,
CC ECO:0000269|PubMed:28912303}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit obesity associated with
CC hyperphagia. {ECO:0000269|PubMed:21971119}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK032627; BAC27958.1; -; mRNA.
DR EMBL; AK133702; BAE21789.1; -; mRNA.
DR EMBL; AL671854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466607; EDL01951.1; -; Genomic_DNA.
DR EMBL; BC116333; AAI16334.1; -; mRNA.
DR EMBL; BC116334; AAI16335.1; -; mRNA.
DR CCDS; CCDS17752.1; -.
DR RefSeq; NP_001292390.1; NM_001305461.1.
DR RefSeq; XP_017175048.1; XM_017319559.1.
DR AlphaFoldDB; Q8C010; -.
DR SMR; Q8C010; -.
DR STRING; 10090.ENSMUSP00000055557; -.
DR GlyGen; Q8C010; 1 site.
DR PhosphoSitePlus; Q8C010; -.
DR PaxDb; Q8C010; -.
DR PRIDE; Q8C010; -.
DR Antibodypedia; 1935; 182 antibodies from 26 providers.
DR DNASU; 229714; -.
DR Ensembl; ENSMUST00000062028; ENSMUSP00000055557; ENSMUSG00000046793.
DR Ensembl; ENSMUST00000116284; ENSMUSP00000111988; ENSMUSG00000046793.
DR GeneID; 229714; -.
DR KEGG; mmu:229714; -.
DR UCSC; uc008qye.2; mouse.
DR CTD; 83873; -.
DR MGI; MGI:2441719; Gpr61.
DR VEuPathDB; HostDB:ENSMUSG00000046793; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182998; -.
DR HOGENOM; CLU_009579_3_1_1; -.
DR InParanoid; Q8C010; -.
DR OMA; GGQFLFC; -.
DR OrthoDB; 901432at2759; -.
DR PhylomeDB; Q8C010; -.
DR TreeFam; TF332667; -.
DR BioGRID-ORCS; 229714; 4 hits in 57 CRISPR screens.
DR PRO; PR:Q8C010; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C010; protein.
DR Bgee; ENSMUSG00000046793; Expressed in medial dorsal nucleus of thalamus and 81 other tissues.
DR Genevisible; Q8C010; MM.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:1990763; F:arrestin family protein binding; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..449
FT /note="G-protein coupled receptor 61"
FT /id="PRO_0000069579"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..310
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 218
FT /note="L -> V (in Ref. 1; BAC27958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49382 MW; 5514589B4EAB6F0B CRC64;
MESSPIPQSS GNSSTLGRAL QTPGPSTASG VPELGLRDVA SESVALFFML LLDLTAVAGN
AAVMAVIAKT PALRKFVFVF HLCLVDLLAA LTLMPLAMLS SSALFDHALF GEVACRLYLF
LSVCFVSLAI LSVSAINVER YYYVVHPMRY EVRMTLGLVA SVLVGVWVKA LAMASVPVLG
RVYWEEGAPS VNPGCSLQWS HSAYCQLFVV VFAVLYFLLP LILIFVVYCS MFRVARVAAM
QHGPLPTWME TPRQRSESLS SRSTMVTSSG AHQTTPHRTF GGGKAAVVLL AVGGQFLLCW
LPYFSFHLYV ALSAQPISAG QVENVVTWIG YFCFTSNPFF YGCLNRQIRG ELSKQFVCFF
KAAPEEELRL PSREGSIEEN FLQFLQGTSE NWVSRPLPSP KREPPPVVDF RIPGQIAEET
SEFLEQQLTS DIIMSDSYLR PAPSPRLES
