GPR52_HUMAN
ID GPR52_HUMAN Reviewed; 361 AA.
AC Q9Y2T5; O75654; Q4VBL6; Q6ISM0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=G-protein coupled receptor 52 {ECO:0000312|HGNC:HGNC:4508};
GN Name=GPR52 {ECO:0000303|PubMed:9931487, ECO:0000312|HGNC:HGNC:4508};
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].
RX PubMed=9931487; DOI=10.1016/s0169-328x(98)00277-0;
RA Sawzdargo M., Nguyen T., Lee D.K., Lynch K.R., Cheng R., Heng H.H.Q.,
RA George S.R., O'Dowd B.F.;
RT "Identification and cloning of three novel human G protein-coupled receptor
RT genes GPR52, PsiGPR53 and GPR55: GPR55 is extensively expressed in human
RT brain.";
RL Brain Res. Mol. Brain Res. 64:193-198(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24587241; DOI=10.1371/journal.pone.0090134;
RA Komatsu H., Maruyama M., Yao S., Shinohara T., Sakuma K., Imaichi S.,
RA Chikatsu T., Kuniyeda K., Siu F.K., Peng L.S., Zhuo K., Mun L.S., Han T.M.,
RA Matsumoto Y., Hashimoto T., Miyajima N., Itoh Y., Ogi K., Habata Y.,
RA Mori M.;
RT "Anatomical transcriptome of G protein-coupled receptors leads to the
RT identification of a novel therapeutic candidate GPR52 for psychiatric
RT disorders.";
RL PLoS ONE 9:E90134-E90134(2014).
RN [5]
RP FUNCTION.
RX PubMed=25738228; DOI=10.7554/elife.05449;
RA Yao Y., Cui X., Al-Ramahi I., Sun X., Li B., Hou J., Difiglia M.,
RA Palacino J., Wu Z.Y., Ma L., Botas J., Lu B.;
RT "A striatal-enriched intronic GPCR modulates huntingtin levels and
RT toxicity.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Gs-coupled receptor activated by antipsychotics reserpine
CC leading to an increase in intracellular cAMP and its internalization
CC (PubMed:24587241). May play a role in locomotor activity through
CC modulation of dopamine, NMDA and ADORA2A-induced locomotor activity.
CC These behavioral changes are accompanied by modulation of the dopamine
CC receptor signaling pathway in striatum (PubMed:24587241). Modulates HTT
CC level via cAMP-dependent but PKA independent mechanisms throught
CC activation of RAB39B that translocates HTT to the endoplasmic
CC reticulum, thus avoiding proteasome degradation (PubMed:25738228).
CC {ECO:0000269|PubMed:24587241, ECO:0000269|PubMed:25738228}.
CC -!- INTERACTION:
CC Q9Y2T5; Q86V38: ATN1; NbExp=3; IntAct=EBI-11305025, EBI-11954292;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in brain, especially in striatum.
CC {ECO:0000269|PubMed:24587241}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF096784; AAD22409.1; -; Genomic_DNA.
DR EMBL; AL022171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067456; AAH67456.1; -; mRNA.
DR EMBL; BC067457; AAH67457.1; -; mRNA.
DR EMBL; BC067458; AAH67458.1; -; mRNA.
DR EMBL; BC067459; AAH67459.1; -; mRNA.
DR EMBL; BC067460; AAH67460.1; -; mRNA.
DR EMBL; BC069460; AAH69460.1; -; mRNA.
DR EMBL; BC095532; AAH95532.1; -; mRNA.
DR CCDS; CCDS30941.1; -.
DR RefSeq; NP_005675.3; NM_005684.4.
DR PDB; 6LI0; X-ray; 2.20 A; A=17-236, A=261-340.
DR PDB; 6LI1; X-ray; 2.90 A; A=17-236, A=265-341.
DR PDB; 6LI2; X-ray; 2.80 A; A=17-235, A=265-340.
DR PDB; 6LI3; EM; 3.32 A; R=1-340.
DR PDBsum; 6LI0; -.
DR PDBsum; 6LI1; -.
DR PDBsum; 6LI2; -.
DR PDBsum; 6LI3; -.
DR AlphaFoldDB; Q9Y2T5; -.
DR SMR; Q9Y2T5; -.
DR BioGRID; 114707; 34.
DR IntAct; Q9Y2T5; 15.
DR STRING; 9606.ENSP00000356658; -.
DR BindingDB; Q9Y2T5; -.
DR ChEMBL; CHEMBL3297639; -.
DR GuidetoPHARMACOLOGY; 108; -.
DR GlyGen; Q9Y2T5; 3 sites.
DR iPTMnet; Q9Y2T5; -.
DR PhosphoSitePlus; Q9Y2T5; -.
DR BioMuta; GPR52; -.
DR DMDM; 76803659; -.
DR MassIVE; Q9Y2T5; -.
DR PaxDb; Q9Y2T5; -.
DR PeptideAtlas; Q9Y2T5; -.
DR PRIDE; Q9Y2T5; -.
DR Antibodypedia; 34403; 296 antibodies from 29 providers.
DR DNASU; 9293; -.
DR Ensembl; ENST00000367685.5; ENSP00000356658.2; ENSG00000203737.5.
DR GeneID; 9293; -.
DR KEGG; hsa:9293; -.
DR MANE-Select; ENST00000367685.5; ENSP00000356658.2; NM_005684.5; NP_005675.3.
DR UCSC; uc001gka.2; human.
DR CTD; 9293; -.
DR DisGeNET; 9293; -.
DR GeneCards; GPR52; -.
DR HGNC; HGNC:4508; GPR52.
DR HPA; ENSG00000203737; Tissue enriched (brain).
DR MIM; 604106; gene.
DR neXtProt; NX_Q9Y2T5; -.
DR OpenTargets; ENSG00000203737; -.
DR PharmGKB; PA28897; -.
DR VEuPathDB; HostDB:ENSG00000203737; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000163422; -.
DR HOGENOM; CLU_009579_3_3_1; -.
DR InParanoid; Q9Y2T5; -.
DR OMA; PITCQVF; -.
DR OrthoDB; 1099557at2759; -.
DR PhylomeDB; Q9Y2T5; -.
DR TreeFam; TF332372; -.
DR PathwayCommons; Q9Y2T5; -.
DR SignaLink; Q9Y2T5; -.
DR BioGRID-ORCS; 9293; 8 hits in 1058 CRISPR screens.
DR GenomeRNAi; 9293; -.
DR Pharos; Q9Y2T5; Tchem.
DR PRO; PR:Q9Y2T5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2T5; protein.
DR Bgee; ENSG00000203737; Expressed in bone marrow cell and 47 other tissues.
DR ExpressionAtlas; Q9Y2T5; baseline and differential.
DR Genevisible; Q9Y2T5; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; 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; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="G-protein coupled receptor 52"
FT /id="PRO_0000069576"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 18
FT /note="I -> V (in Ref. 3; AAH95532)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="V -> A (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="V -> A (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> R (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> T (in Ref. 3; AAH95532)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="I -> V (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="S -> G (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> F (in Ref. 1; AAD22409)"
FT /evidence="ECO:0000305"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6LI0"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:6LI2"
FT HELIX 41..66
FT /evidence="ECO:0007829|PDB:6LI0"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6LI0"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 111..144
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 155..172
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 261..289
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:6LI0"
FT HELIX 322..337
FT /evidence="ECO:0007829|PDB:6LI0"
SQ SEQUENCE 361 AA; 41354 MW; 4888D58CEBB2D725 CRC64;
MNESRWTEWR ILNMSSGIVN VSERHSCPLG FGHYSVVDVC IFETVVIVLL TFLIIAGNLT
VIFVFHCAPL LHHYTTSYFI QTMAYADLFV GVSCLVPTLS LLHYSTGVHE SLTCQVFGYI
ISVLKSVSMA CLACISVDRY LAITKPLSYN QLVTPCRLRI CIILIWIYSC LIFLPSFFGW
GKPGYHGDIF EWCATSWLTS AYFTGFIVCL LYAPAAFVVC FTYFHIFKIC RQHTKEINDR
RARFPSHEVD SSRETGHSPD RRYAMVLFRI TSVFYMLWLP YIIYFLLESS RVLDNPTLSF
LTTWLAISNS FCNCVIYSLS NSVFRLGLRR LSETMCTSCM CVKDQEAQEP KPRKRANSCS
I
