ID   GPR52_MOUSE             Reviewed;         361 AA.
AC   P0C5J4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=G-protein coupled receptor 52 {ECO:0000250|UniProtKB:Q9Y2T5};
GN   Name=Gpr52 {ECO:0000312|MGI:MGI:3643278};
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   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
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   [3]
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).
RN   [4]
RP   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=28583861; DOI=10.1016/j.brainres.2017.05.031;
RA   Nishiyama K., Suzuki H., Maruyama M., Yoshihara T., Ohta H.;
RT   "Genetic deletion of GPR52 enhances the locomotor-stimulating effect of an
RT   adenosine A2A receptor antagonist in mice: A potential role of GPR52 in the
RT   function of striatopallidal neurons.";
RL   Brain Res. 1670:24-31(2017).
CC   -!- FUNCTION: G- protein coupled receptor activated by antipsychotics
CC       reserpine leading to an increase in intracellular cAMP and its
CC       internalization (By similarity). May play a role in locomotor activity
CC       through modulation of dopamine, NMDA and ADORA2A-induced locomotor
CC       activity. These behavioral changes are accompanied by modulation of the
CC       dopamine receptor signaling pathway in striatum (PubMed:24587241,
CC       PubMed:28583861). Modulates HTT level via cAMP-dependent but PKA
CC       independent mechanisms throught activation of RAB39B that translocates
CC       HTT to the endoplasmic reticulum, thus avoiding proteasome degradation
CC       (PubMed:25738228). {ECO:0000250|UniProtKB:Q9Y2T5,
CC       ECO:0000269|PubMed:24587241, ECO:0000269|PubMed:25738228,
CC       ECO:0000269|PubMed:28583861}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, especially in striatum
CC       (PubMed:24587241). Expressed in the striatum, nucleus accumbens, and
CC       lateral globus pallidus (PubMed:28583861).
CC       {ECO:0000269|PubMed:24587241, ECO:0000269|PubMed:28583861}.
CC   -!- DISRUPTION PHENOTYPE: Gpr52 knockout mice are normal in body and brain
CC       weight. In the open field test, mice stay and move around the central
CC       zone significantly longer. The total distance traveled and brain
CC       morphology are normal. Mice are much more sensitive to the startle
CC       response following dizocilpine administration. Thus mice displayed
CC       psychosis-related behaviors (PubMed:24587241). Mice exhibit a
CC       significantly higher istradefylline-induced locomotor activity
CC       (PubMed:28583861). {ECO:0000269|PubMed:24587241,
CC       ECO:0000269|PubMed:28583861}.
CC   -!- MISCELLANEOUS: GPR52 is located within an intron of RABGAP1L gene,
CC       which exhibits epistatic effects on GPR52-mediated modulation of HTT
CC       levels by blocking this modulation. {ECO:0000269|PubMed:25738228}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AC117787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS87900.1; -.
DR   RefSeq; NP_001139802.1; NM_001146330.1.
DR   RefSeq; XP_017177375.1; XM_017321886.1.
DR   RefSeq; XP_017177377.1; XM_017321888.1.
DR   AlphaFoldDB; P0C5J4; -.
DR   SMR; P0C5J4; -.
DR   BindingDB; P0C5J4; -.
DR   ChEMBL; CHEMBL4105791; -.
DR   GlyGen; P0C5J4; 3 sites.
DR   PhosphoSitePlus; P0C5J4; -.
DR   SwissPalm; P0C5J4; -.
DR   PRIDE; P0C5J4; -.
DR   ProteomicsDB; 271070; -.
DR   Antibodypedia; 34403; 296 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000238289; ENSMUSP00000158769; ENSMUSG00000118401.
DR   GeneID; 620246; -.
DR   KEGG; mmu:620246; -.
DR   UCSC; uc011wum.1; mouse.
DR   CTD; 9293; -.
DR   MGI; MGI:3643278; Gpr52.
DR   VEuPathDB; HostDB:ENSMUSG00000118401; -.
DR   GeneTree; ENSGT00940000163422; -.
DR   InParanoid; P0C5J4; -.
DR   OMA; PITCQVF; -.
DR   OrthoDB; 191811at2759; -.
DR   PhylomeDB; P0C5J4; -.
DR   BioGRID-ORCS; 620246; 4 hits in 17 CRISPR screens.
DR   PRO; PR:P0C5J4; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P0C5J4; protein.
DR   Bgee; ENSMUSG00000118401; Expressed in striatum and 20 other tissues.
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; ISS: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; IMP:UniProtKB.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; 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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="G-protein coupled receptor 52"
FT                   /id="PRO_0000307680"
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..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..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..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..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"
SQ   SEQUENCE   361 AA;  41343 MW;  150F8A395B63290B CRC64;
     MNESRWTEWR ILNMSSSIVN VSEHHSCPLG FGHYSVEDVC IFETVVIVLL TFLIISGNLT
     VIFVFHCAPL LHHYTTSYFI QTMAYADLLV GVTCLVPTLS LLHYSTGVHE SLTCQVFGYI
     ISVLKSVSMA CLACISVDRY LAITKPLSYN QLVTPCRLRI CIIMIWIYSC LIFLPSFFGW
     GKPGYHGDIF EWCATSWLTS AYFTCFIVCL LYAPAALVVC FTYFHIFKIC RQHTKEINDR
     RARFPSHEVE ASREAGHSPD RRYAMVLFRI TSVFYMLWLP YIIYFLLESS RVLDNPTLSF
     LTTWLAISNS FCNCVIYSLS NSVFRLGLRR LSETMCTSCV CAKDQEAQDP KPRRRANSCS
     I