ID GPR62_HUMAN Reviewed; 368 AA. AC Q9BZJ7; F1DAM4; Q5KU27; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=G-protein coupled receptor 62 {ECO:0000305}; DE AltName: Full=G-protein coupled receptor GPCR8; DE Short=hGPCR8; DE AltName: Full=G-protein coupled receptor KPG_005; GN Name=GPR62; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-151 AND ARG-216, AND TISSUE RP SPECIFICITY. RX PubMed=11165367; DOI=10.1016/s0169-328x(00)00242-4; RA Lee D.K., George S.R., Cheng R., Nguyen T., Liu Y., Brown M., Lynch K.R., RA O'Dowd B.F.; RT "Identification of four novel human G protein-coupled receptors expressed RT in the brain."; RL Brain Res. Mol. Brain Res. 86:13-22(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-151 AND ARG-216. RA Urakawa I., Okazaki H.; RT "Probable G-protein coupled receptor."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-151 AND ARG-216. RC TISSUE=Brain; RA Sutterer S.M., Kaighin V.A., Martin A.L., Aronstam R.S.; RT "Isolation of cDNA coding for multiple human genes."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8; RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.; RT "Identification of G protein-coupled receptor genes from the human genome RT sequence."; RL FEBS Lett. 520:97-101(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS PRO-151 AND RP ARG-216. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, INTERACTION WITH MTNR1B, AND RP INTERACTION WITH ARRB1 AND ARRB2. RX PubMed=28827538; DOI=10.1038/s41598-017-08996-7; RA Oishi A., Karamitri A., Gerbier R., Lahuna O., Ahmad R., Jockers R.; RT "Orphan GPR61, GPR62 and GPR135 receptors and the melatonin MT2 receptor RT reciprocally modulate their signaling functions."; RL Sci. Rep. 7:8990-8990(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:28827538). Has spontaneous activity for beta-arrestin CC recruitment (PubMed:28827538). Shows a reciprocal modulation of CC signaling functions with the melatonin receptor MTNR1B most likely CC through receptor heteromerization (PubMed:28827538). CC {ECO:0000269|PubMed:28827538}. CC -!- SUBUNIT: Homodimers (By similarity). Forms heterodimer with MTNR1B CC (PubMed:28827538). Interacts with ARRB1 and ARRB2 in a spontaneous and CC agonist-independent manner; leading to the internalization of GPR62 in CC the endosomal compartment (PubMed:28827538). CC {ECO:0000250|UniProtKB:Q80UC6, ECO:0000269|PubMed:28827538}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28827538}; CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane CC {ECO:0000269|PubMed:28827538}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalizes with ARRB2 in the endosome CC (PubMed:28827538). {ECO:0000269|PubMed:28827538}. CC -!- TISSUE SPECIFICITY: Expressed in brain; detected in the basal CC forebrain, frontal cortex, caudate, putamen, thalamus and hippocampus. CC {ECO:0000269|PubMed:11165367}. CC -!- DOMAIN: Lacks the conserved DRY and BBXXB motifs. The restoration of CC these motifs affects its constitutive activity. CC {ECO:0000250|UniProtKB:Q80UC6}. 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; AF317653; AAK12638.1; -; Genomic_DNA. DR EMBL; AB032600; BAD83591.1; -; mRNA. DR EMBL; HQ709188; ADZ17395.1; -; mRNA. DR EMBL; AB083590; BAB89303.1; -; Genomic_DNA. DR EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65164.1; -; Genomic_DNA. DR CCDS; CCDS2838.1; -. DR RefSeq; NP_543141.3; NM_080865.3. DR AlphaFoldDB; Q9BZJ7; -. DR SMR; Q9BZJ7; -. DR IntAct; Q9BZJ7; 1. DR MINT; Q9BZJ7; -. DR STRING; 9606.ENSP00000319250; -. DR ChEMBL; CHEMBL4523917; -. DR GlyCosmos; Q9BZJ7; 2 sites, No reported glycans. DR GlyGen; Q9BZJ7; 2 sites. DR PhosphoSitePlus; Q9BZJ7; -. DR BioMuta; GPR62; -. DR DMDM; 296434526; -. DR MassIVE; Q9BZJ7; -. DR PaxDb; 9606-ENSP00000319250; -. DR PeptideAtlas; Q9BZJ7; -. DR Antibodypedia; 14225; 256 antibodies from 30 providers. DR DNASU; 118442; -. DR Ensembl; ENST00000322241.6; ENSP00000319250.4; ENSG00000180929.6. DR GeneID; 118442; -. DR KEGG; hsa:118442; -. DR MANE-Select; ENST00000322241.6; ENSP00000319250.4; NM_080865.4; NP_543141.3. DR UCSC; uc003dca.4; human. DR AGR; HGNC:13301; -. DR CTD; 118442; -. DR GeneCards; GPR62; -. DR HGNC; HGNC:13301; GPR62. DR HPA; ENSG00000180929; Tissue enriched (brain). DR MIM; 606917; gene. DR neXtProt; NX_Q9BZJ7; -. DR OpenTargets; ENSG00000180929; -. DR PharmGKB; PA28906; -. DR VEuPathDB; HostDB:ENSG00000180929; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00950000182998; -. DR HOGENOM; CLU_067115_0_0_1; -. DR InParanoid; Q9BZJ7; -. DR OMA; CTPRAWH; -. DR OrthoDB; 4640465at2759; -. DR PhylomeDB; Q9BZJ7; -. DR TreeFam; TF332667; -. DR PathwayCommons; Q9BZJ7; -. DR SignaLink; Q9BZJ7; -. DR BioGRID-ORCS; 118442; 10 hits in 1143 CRISPR screens. DR ChiTaRS; GPR62; human. DR GeneWiki; GPR62; -. DR GenomeRNAi; 118442; -. DR Pharos; Q9BZJ7; Tbio. DR PRO; PR:Q9BZJ7; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9BZJ7; Protein. DR Bgee; ENSG00000180929; Expressed in inferior vagus X ganglion and 85 other cell types or tissues. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:1990763; F:arrestin family protein binding; IDA:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0038035; P:G protein-coupled receptor signaling in absence of ligand; IDA:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:UniProtKB. DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB. DR CDD; cd15220; 7tmA_GPR61_GPR62-like; 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 PANTHER; PTHR22752; G PROTEIN-COUPLED RECEPTOR; 1. DR PANTHER; PTHR22752:SF11; G-PROTEIN COUPLED RECEPTOR 62; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; Q9BZJ7; HS. 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..368 FT /note="G-protein coupled receptor 62" FT /id="PRO_0000069580" FT TOPO_DOM 1..18 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 19..39 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 40..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..91 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 92..112 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 113..129 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 130..150 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 151..177 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 199..239 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 240..260 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 261..272 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 273..293 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 294..368 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 332..368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 3 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 8 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 151 FT /note="T -> P (in dbSNP:rs28587738)" FT /evidence="ECO:0000269|PubMed:11165367, ECO:0000269|Ref.2, FT ECO:0000269|Ref.3, ECO:0000269|Ref.6" FT /id="VAR_067702" FT VARIANT 216 FT /note="H -> R (in dbSNP:rs28651222)" FT /evidence="ECO:0000269|PubMed:11165367, ECO:0000269|Ref.2, FT ECO:0000269|Ref.3, ECO:0000269|Ref.6" FT /id="VAR_067703" FT VARIANT 313 FT /note="V -> L (in dbSNP:rs323871)" FT /id="VAR_055920" SQ SEQUENCE 368 AA; 37614 MW; B06F91BF4C51757A CRC64; MANSTGLNAS EVAGSLGLIL AAVVEVGALL GNGALLVVVL RTPGLRDALY LAHLCVVDLL AAASIMPLGL LAAPPPGLGR VRLGPAPCRA ARFLSAALLP ACTLGVAALG LARYRLIVHP LRPGSRPPPV LVLTAVWAAA GLLGALSLLG TPPAPPPAPA RCSVLAGGLG PFRPLWALLA FALPALLLLG AYGGIFVVAR RAALRPPRPA RGSRLHSDSL DSRLSILPPL RPRLPGGKAA LAPALAVGQF AACWLPYGCA CLAPAARAAE AEAAVTWVAY SAFAAHPFLY GLLQRPVRLA LGRLSRRALP GPVRACTPQA WHPRALLQCL QRPPEGPAVG PSEAPEQTPE LAGGRSPAYQ GPPESSLS //