GPR62_MOUSE
ID GPR62_MOUSE Reviewed; 358 AA.
AC Q80UC6; Q8CEQ6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=G-protein coupled receptor 62;
GN Name=Gpr62;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-120.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-358.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS
RP OF ALA-111 AND 232-GLY--LEU-237, SUBUNIT, AND FUNCTION.
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(q/11)/inositol phosphate and the G(s)-alpha/cAMP signaling
CC pathways (PubMed:28912303). Has spontaneous activity for beta-arrestin
CC recruitment (By similarity). Shows a reciprocal regulatory interaction
CC with the melatonin receptor MTNR1B most likely through receptor
CC heteromerization (By similarity). {ECO:0000250|UniProtKB:Q9BZJ7,
CC ECO:0000269|PubMed:28912303}.
CC -!- SUBUNIT: Homodimer (PubMed:28912303). Forms heterodimer with MTNR1B (By
CC similarity). Interacts with ARRB1 and ARRB2 in a spontaneous and
CC agonist-independent manner; leading to the internalization of GPR62 in
CC the endosomal compartment (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZJ7, ECO:0000269|PubMed:28912303}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BZJ7};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9BZJ7}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with ARRB2 in the endosome.
CC {ECO:0000250|UniProtKB:Q9BZJ7}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and testes. Expressed
CC widely, in the brain, including the cerebral cortex, cerebellum,
CC hippocampus,thalamus and pituitary gland. In the testes, expressed
CC specifically in the germ cells. {ECO:0000269|PubMed:28912303}.
CC -!- DEVELOPMENTAL STAGE: Expression in the testes starts 25 days after
CC birth and continues thereafter. {ECO:0000269|PubMed:28912303}.
CC -!- DOMAIN: Lacks the conserved DRY and BBXXB motifs. The restoration of
CC these motifs affects its constitutive activity.
CC {ECO:0000269|PubMed:28912303}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice show any abnormality in growth and
CC behavior. Both male and female are fertile.
CC {ECO:0000269|PubMed:28912303}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AC151729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK016613; BAC25490.1; -; mRNA.
DR EMBL; AY255551; AAO85063.1; -; mRNA.
DR CCDS; CCDS52909.1; -.
DR RefSeq; NP_001153124.1; NM_001159652.1.
DR RefSeq; XP_006511830.1; XM_006511767.3.
DR AlphaFoldDB; Q80UC6; -.
DR SMR; Q80UC6; -.
DR STRING; 10090.ENSMUSP00000129055; -.
DR GlyGen; Q80UC6; 1 site.
DR iPTMnet; Q80UC6; -.
DR PhosphoSitePlus; Q80UC6; -.
DR SwissPalm; Q80UC6; -.
DR PaxDb; Q80UC6; -.
DR PRIDE; Q80UC6; -.
DR ProteomicsDB; 271071; -.
DR Antibodypedia; 14225; 228 antibodies from 29 providers.
DR Ensembl; ENSMUST00000164834; ENSMUSP00000129055; ENSMUSG00000091735.
DR GeneID; 436090; -.
DR KEGG; mmu:436090; -.
DR UCSC; uc012gzw.1; mouse.
DR CTD; 118442; -.
DR MGI; MGI:3525078; Gpr62.
DR VEuPathDB; HostDB:ENSMUSG00000091735; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182998; -.
DR HOGENOM; CLU_067115_0_0_1; -.
DR InParanoid; Q80UC6; -.
DR OMA; RPPRACT; -.
DR OrthoDB; 1373348at2759; -.
DR PhylomeDB; Q80UC6; -.
DR TreeFam; TF332667; -.
DR BioGRID-ORCS; 436090; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q80UC6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80UC6; protein.
DR Bgee; ENSMUSG00000091735; Expressed in lumbar subsegment of spinal cord and 78 other tissues.
DR Genevisible; Q80UC6; 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; ISS:UniProtKB.
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:0042802; F:identical protein binding; IMP:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISS:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="G-protein coupled receptor 62"
FT /id="PRO_0000305584"
FT TOPO_DOM 1..17
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 334..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 111
FT /note="A->D: No effect on constitutive activity; No effect
FT on protein level; Does not affect homooligomerization."
FT /evidence="ECO:0000269|PubMed:28912303"
FT MUTAGEN 232..237
FT /note="GGKAAL->KKAAKT: Strong decreases on constitutive
FT activity; No effect on protein level; Does not affect
FT homooligomerization."
FT /evidence="ECO:0000269|PubMed:28912303"
SQ SEQUENCE 358 AA; 37148 MW; 6FC222684565B5D6 CRC64;
MANGSGLSVT ELAGSVGFIL AVLVEVGAVL GNGTLLVVVL RTPDLQDAFY LAHLCVVDLL
AAASIMPLGL LAAPPGLGTV PLDPSSCRAA RFLSAALLPA CTLGVAALGL ARYRLIVHPL
RPGARPAPAL VLTAVWSAAA LLGALSLLGP PPAPPPAPAR CSVLAGGLGP FRPLWAMLAF
ALPALLLLAA YGSIFLVARR AALRPPRGTR PRSDSLDSRL SFLPPLRPRL LGGKAALAPA
LAVGQFAACW LPYGCACLAP AARAAAAEAT VTWVAYSAFA AHPFLYGLLQ RPVRLALGRL
TRRALPRAPK ACTSQAWHLQ TLLRRLQELR KDPVLGPSEA PEQARELARQ TPSVSEAT
