GPR62_HUMAN
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 03-AUG-2022, entry version 142.
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}.
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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 GlyGen; Q9BZJ7; 2 sites.
DR PhosphoSitePlus; Q9BZJ7; -.
DR BioMuta; GPR62; -.
DR DMDM; 296434526; -.
DR MassIVE; Q9BZJ7; -.
DR PaxDb; Q9BZJ7; -.
DR PeptideAtlas; Q9BZJ7; -.
DR PRIDE; Q9BZJ7; -.
DR Antibodypedia; 14225; 228 antibodies from 29 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 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; RPPRACT; -.
DR OrthoDB; 1373348at2759; -.
DR PhylomeDB; Q9BZJ7; -.
DR TreeFam; TF332667; -.
DR PathwayCommons; Q9BZJ7; -.
DR SignaLink; Q9BZJ7; -.
DR BioGRID-ORCS; 118442; 9 hits in 1065 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 tissues.
DR Genevisible; Q9BZJ7; HS.
DR GO; GO:0005768; C:endosome; IDA: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; 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:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IDA:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
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..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
