ID GPR88_MOUSE Reviewed; 384 AA. AC Q9EPB7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=G protein-coupled receptor 88 {ECO:0000305}; DE AltName: Full=Striatum-specific G-protein coupled receptor; GN Name=Gpr88; Synonyms=Strg; 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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY. RX PubMed=11056049; DOI=10.1006/geno.2000.6340; RA Mizushima K., Miyamoto Y., Tsukahara F., Hirai M., Sakaki Y., Ito T.; RT "A novel G-protein-coupled receptor gene expressed in striatum."; RL Genomics 69:314-321(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; 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 [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=26188600; DOI=10.1016/j.biopsych.2015.05.020; RA Meirsman A.C., Le Merrer J., Pellissier L.P., Diaz J., Clesse D., RA Kieffer B.L., Becker J.A.; RT "Mice lacking GPR88 show motor deficit, improved spatial learning, and low RT anxiety reversed by delta opioid antagonist."; RL Biol. Psychiatry 79:917-927(2016). CC -!- FUNCTION: Orphan G protein-coupled receptor implicated in a large CC repertoire of behavioral responses that engage motor activities, CC spatial learning, and emotional processing (By similarity). May play a CC role in the regulation of cognitive and motor function CC (PubMed:26188600). Couples with the heterotrimeric G protein complex of CC the G(i) subfamily, consisting of GNAI1, GNB1 and GNG2, thereby acting CC through a G(i)-mediated pathway (By similarity). Plays a role in the CC attenuation of D1 dopamine receptor (D1R)-mediated cAMP response in CC ciliated cells (By similarity). In on-ciliated cells, involved in the CC inhibition of the beta-2 adrenergic receptor (B2AR) response (By CC similarity). {ECO:0000250|UniProtKB:Q9ESP4, CC ECO:0000250|UniProtKB:Q9GZN0, ECO:0000269|PubMed:26188600}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ESP4}; CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium CC membrane {ECO:0000250|UniProtKB:Q9GZN0}; Multi-pass membrane protein CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9ESP4}. Nucleus CC {ECO:0000250|UniProtKB:Q9ESP4}. Note=Localized to cilia in ciliated CC cells; whereas in non-ciliated cells, distributed throughout the cell CC membrane (By similarity). During cortical lamination, subcellular CC location shifts, on the day of birth, from expression at the plasma CC membrane and in the cytoplasm to the nuclei of neurons. This CC intranuclear localization remains throughout adulthood. CC {ECO:0000250|UniProtKB:Q9ESP4, ECO:0000250|UniProtKB:Q9GZN0}. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the striatum. CC {ECO:0000269|PubMed:11056049}. CC -!- DISRUPTION PHENOTYPE: Mice have increased locomotion, increased motor CC stereotypical behavior, and impaired motor skill learning. Mutant mice CC also show facilitated hippocampal-mediated behaviors and decreased CC anxiety. Chronic blockade of delta opioid receptors and mu opioid, but CC not other Gi/o coupled receptors, using delta opioid receptor CC antagonist partially improved motor coordination and normalized spatial CC navigation and anxiety of mutant mice. {ECO:0000269|PubMed:26188600}. 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; AB042408; BAB18245.1; -; mRNA. DR EMBL; AB042409; BAB18246.1; -; Genomic_DNA. DR EMBL; BC051941; AAH51941.1; -; mRNA. DR CCDS; CCDS38610.1; -. DR RefSeq; NP_071872.1; NM_022427.2. DR RefSeq; XP_006501919.1; XM_006501856.1. DR RefSeq; XP_006501920.1; XM_006501857.1. DR AlphaFoldDB; Q9EPB7; -. DR SMR; Q9EPB7; -. DR STRING; 10090.ENSMUSP00000087959; -. DR BindingDB; Q9EPB7; -. DR ChEMBL; CHEMBL3879835; -. DR GlyCosmos; Q9EPB7; 1 site, No reported glycans. DR GlyGen; Q9EPB7; 1 site. DR PhosphoSitePlus; Q9EPB7; -. DR PaxDb; 10090-ENSMUSP00000087959; -. DR ProteomicsDB; 271072; -. DR Antibodypedia; 19999; 211 antibodies from 26 providers. DR DNASU; 64378; -. DR Ensembl; ENSMUST00000090473.7; ENSMUSP00000087959.6; ENSMUSG00000068696.7. DR GeneID; 64378; -. DR KEGG; mmu:64378; -. DR UCSC; uc008rbz.2; mouse. DR AGR; MGI:1927653; -. DR CTD; 54112; -. DR MGI; MGI:1927653; Gpr88. DR VEuPathDB; HostDB:ENSMUSG00000068696; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00390000009609; -. DR HOGENOM; CLU_053532_0_0_1; -. DR InParanoid; Q9EPB7; -. DR OMA; LLYTWKN; -. DR OrthoDB; 5362232at2759; -. DR PhylomeDB; Q9EPB7; -. DR TreeFam; TF336499; -. DR BioGRID-ORCS; 64378; 2 hits in 76 CRISPR screens. DR PRO; PR:Q9EPB7; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q9EPB7; Protein. DR Bgee; ENSMUSG00000068696; Expressed in caudate-putamen and 138 other cell types or tissues. DR ExpressionAtlas; Q9EPB7; baseline and differential. DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB. DR GO; GO:0005929; C:cilium; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004941; F:beta2-adrenergic receptor activity; ISS:UniProtKB. DR GO; GO:0003774; F:cytoskeletal motor activity; IMP:UniProtKB. DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central. DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:MGI. DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:MGI. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; 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; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; IMP:MGI. DR GO; GO:0061743; P:motor learning; IMP:UniProtKB. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0019228; P:neuronal action potential; IMP:MGI. DR GO; GO:0007602; P:phototransduction; IBA:GO_Central. 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; PTHR24240:SF165; G-PROTEIN COUPLED RECEPTOR 88-RELATED; 1. DR PANTHER; PTHR24240; OPSIN; 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; Q9EPB7; MM. PE 2: Evidence at transcript level; KW Cell membrane; Cell projection; Cytoplasm; G-protein coupled receptor; KW Glycoprotein; Membrane; Nucleus; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..384 FT /note="G protein-coupled receptor 88" FT /id="PRO_0000069598" FT TOPO_DOM 1..35 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 36..56 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 57..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 74..94 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 95..116 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 117..136 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 137..158 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 159..179 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 180..195 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 217..285 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 286..306 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 307..310 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 311..331 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 332..384 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 3 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 384 AA; 40240 MW; 1E5BB8A5B5B3B37D CRC64; MTNSSSTSTS TTTGGSLLLL CEEEESWAGR RIPVSLLYSG LAIGGTLANG MVIYLVSSFR KLQTTSNAFI VNGCAADLSV CALWMPQEAV LGLLPSGSAE PPGDWDGGGG SYRLLRGGLL GLGLTVSLLS HCLVALNRYL LITRAPATYQ VLYQRRHTVG MLALSWALAL GLVLLLPPWA PKPGAEPPQV HYPALLAAGA LLAQTALLLH CYLGIVRRVR VSVKRVSVLN FHLLHQLPGC AAAAAAFPAA PHAPGPGGAA HPAQPQPLPA ALQPRRAQRR LSGLSVLLLC CVFLLATQPL VWVSLASGFS LPVPWGVQAA SWLLCCALSA LNPLLYTWRN EEFRRSVRSV LPGVGDAAAA AAAATAVPAM SQAQLGTRAA GQHW //