GPR88_RAT
ID GPR88_RAT Reviewed; 384 AA.
AC Q9ESP4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable G-protein coupled receptor 88;
DE AltName: Full=Striatum-specific G-protein coupled receptor;
GN Name=Gpr88; Synonyms=Strg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [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 FUNCTION.
RX PubMed=25155879; DOI=10.1038/mp.2014.92;
RA Ingallinesi M., Le Bouil L., Biguet N.F., Thi A.D., Mannoury la Cour C.,
RA Millan M.J., Ravassard P., Mallet J., Meloni R.;
RT "Local inactivation of Gpr88 in the nucleus accumbens attenuates behavioral
RT deficits elicited by the neonatal administration of phencyclidine in
RT rats.";
RL Mol. Psychiatry 20:951-958(2015).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26918661; DOI=10.1002/cne.23991;
RA Massart R., Mignon V., Stanic J., Munoz-Tello P., Becker J.A.,
RA Kieffer B.L., Darmon M., Sokoloff P., Diaz J.;
RT "Developmental and adult expression patterns of the G-protein-coupled
RT receptor GPR88 in the rat: Establishment of a dual nuclear-cytoplasmic
RT localization.";
RL J. Comp. Neurol. 524:2776-2802(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:Q9EPB7, ECO:0000269|PubMed:25155879}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26918661};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:26918661}. Nucleus {ECO:0000269|PubMed:26918661}.
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:0000269|PubMed:26918661}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the striatum
CC (PubMed:11056049). Expressed also in olfactory tubercle, nucleus
CC accumbens, amygdala, and neocortex. Spinal cord, pons, and medulla
CC expression remains discrete (PubMed:26918661). Also expressed in
CC peripheral tissues, including adrenal cortex (E16-E21) and cochlear
CC ganglia (E19-postnatal day 3(P3)) and also at moderate levels in retina
CC (E18-E19) and spleen (E21-P7) (PubMed:26918661).
CC {ECO:0000269|PubMed:11056049, ECO:0000269|PubMed:26918661}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic day 16 (E16) in the
CC striatum. From E16-E20 to adulthood, the highest expression levels of
CC protein is observed in the striatum, olfactory tubercle, nucleus
CC accumbens, amygdala, and neocortex. {ECO:0000269|PubMed:26918661}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB042407; BAB18244.1; -; mRNA.
DR RefSeq; NP_113884.1; NM_031696.1.
DR RefSeq; XP_006233282.1; XM_006233220.3.
DR RefSeq; XP_006233283.1; XM_006233221.3.
DR RefSeq; XP_006233284.1; XM_006233222.3.
DR AlphaFoldDB; Q9ESP4; -.
DR SMR; Q9ESP4; -.
DR STRING; 10116.ENSRNOP00000038233; -.
DR GlyGen; Q9ESP4; 1 site.
DR PhosphoSitePlus; Q9ESP4; -.
DR PaxDb; Q9ESP4; -.
DR Ensembl; ENSRNOT00000037068; ENSRNOP00000038233; ENSRNOG00000026953.
DR GeneID; 64443; -.
DR KEGG; rno:64443; -.
DR UCSC; RGD:61921; rat.
DR CTD; 54112; -.
DR RGD; 61921; Gpr88.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00390000009609; -.
DR HOGENOM; CLU_053532_0_0_1; -.
DR InParanoid; Q9ESP4; -.
DR OMA; LLYTWKN; -.
DR OrthoDB; 1258797at2759; -.
DR PhylomeDB; Q9ESP4; -.
DR TreeFam; TF336499; -.
DR PRO; PR:Q9ESP4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000026953; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; Q9ESP4; RN.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
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; ISO:RGD.
DR GO; GO:0061743; P:motor learning; ISS:UniProtKB.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
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_0000069599"
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; 40200 MW; 0334B64D0F3FD669 CRC64;
MTNSSSTSTS TTTGGSLLLL CEEEESWAGR RIPVSLLYSG LAIGGTLANG MVIYLVSSFR
KLQTTSNAFI VNGCAADLSV CALWMPQEAV LGLLPAGSAE PPGDWDSGGG SYRLLRGGLL
GLGLTVSLLS HCLVALNRYL LITRAPATYQ VLYQRRHTAG MLALSWALAL GLVLLLPPWA
PKPGAEPPQV HYPALLAAGA LLAQTALLLH CYLGIVRRVR VSVKRVSVLN FHLLHQLPGC
AAAAAAFPAA PHAPGAGGAA HPAQPQPLPA ALQPRRAQRR LSGLSVLLLC CVFLLATQPL
VWVSLASGFS LPVPWGVQAA SWLLCCALSA LNPLLYTWRN EEFRRSVRSV LPGVGDAAAA
AAAATAVPAM SQAQLGTRAA GQHW
