GPR88_MOUSE
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 03-AUG-2022, entry version 130.
DE RecName: Full=Probable G-protein coupled receptor 88;
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: Probable G-protein coupled receptor implicated in a large
CC repertoire of behavioral responses that engage motor activities,
CC spatial learning, and emotional processing. May play a role in the
CC regulation of cognitive and motor function.
CC {ECO:0000250|UniProtKB:Q9ESP4, ECO:0000269|PubMed:26188600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ESP4};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ESP4}. Nucleus {ECO:0000250|UniProtKB:Q9ESP4}.
CC Note=During cortical lamination, subcellular location shifts, on the
CC day of birth, from expression at the plasma membrane and in the
CC cytoplasm to the nuclei of neurons. This intranuclear localization
CC remains throughout adulthood. {ECO:0000250|UniProtKB:Q9ESP4}.
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}.
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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 GlyGen; Q9EPB7; 1 site.
DR PhosphoSitePlus; Q9EPB7; -.
DR PaxDb; Q9EPB7; -.
DR PRIDE; Q9EPB7; -.
DR ProteomicsDB; 271072; -.
DR Antibodypedia; 19999; 206 antibodies from 26 providers.
DR DNASU; 64378; -.
DR Ensembl; ENSMUST00000090473; ENSMUSP00000087959; ENSMUSG00000068696.
DR GeneID; 64378; -.
DR KEGG; mmu:64378; -.
DR UCSC; uc008rbz.2; mouse.
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; 1258797at2759; -.
DR PhylomeDB; Q9EPB7; -.
DR TreeFam; TF336499; -.
DR BioGRID-ORCS; 64378; 2 hits in 71 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 tissues.
DR ExpressionAtlas; Q9EPB7; baseline and differential.
DR Genevisible; Q9EPB7; MM.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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: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: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 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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; G-protein coupled receptor; Glycoprotein;
KW Membrane; Nucleus; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..384
FT /note="Probable 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
