RGR_MOUSE
ID RGR_MOUSE Reviewed; 291 AA.
AC Q9Z2B3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RPE-retinal G protein-coupled receptor;
GN Name=Rgr;
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 [MRNA].
RC TISSUE=Retina;
RX PubMed=9841934;
RA Tao L., Shen D., Pandey S., Hao W., Rich K.A., Fong H.K.W.;
RT "Structure and developmental expression of the mouse RGR opsin gene.";
RL Mol. Vis. 4:25-25(1998).
CC -!- FUNCTION: Receptor for all-trans- and 11-cis-retinal. Binds
CC preferentially to the former and may catalyze the isomerization of the
CC chromophore by a retinochrome-like mechanism (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Covalently binds all-trans- and 11-cis-retinal. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF076930; AAC69836.1; -; mRNA.
DR CCDS; CCDS26949.1; -.
DR RefSeq; NP_067315.1; NM_021340.4.
DR AlphaFoldDB; Q9Z2B3; -.
DR SMR; Q9Z2B3; -.
DR STRING; 10090.ENSMUSP00000022338; -.
DR PhosphoSitePlus; Q9Z2B3; -.
DR PaxDb; Q9Z2B3; -.
DR PRIDE; Q9Z2B3; -.
DR ProteomicsDB; 254948; -.
DR Antibodypedia; 15900; 223 antibodies from 28 providers.
DR DNASU; 57811; -.
DR Ensembl; ENSMUST00000022338; ENSMUSP00000022338; ENSMUSG00000021804.
DR GeneID; 57811; -.
DR KEGG; mmu:57811; -.
DR UCSC; uc007tbp.2; mouse.
DR CTD; 5995; -.
DR MGI; MGI:1929473; Rgr.
DR VEuPathDB; HostDB:ENSMUSG00000021804; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244811; -.
DR HOGENOM; CLU_009579_3_2_1; -.
DR InParanoid; Q9Z2B3; -.
DR OMA; CWGPYAL; -.
DR OrthoDB; 704940at2759; -.
DR PhylomeDB; Q9Z2B3; -.
DR TreeFam; TF324998; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419771; Opsins.
DR BioGRID-ORCS; 57811; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Rgr; mouse.
DR PRO; PR:Q9Z2B3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z2B3; protein.
DR Bgee; ENSMUSG00000021804; Expressed in pigmented layer of retina and 15 other tissues.
DR ExpressionAtlas; Q9Z2B3; baseline and differential.
DR Genevisible; Q9Z2B3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; 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: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:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001793; RPE_GPCR.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00667; RPERETINALR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Membrane;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..291
FT /note="RPE-retinal G protein-coupled receptor"
FT /id="PRO_0000197823"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 255
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT DISULFID 88..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 291 AA; 32127 MW; ED31E1F937810A7B CRC64;
MAATRALPAG LGELEVLAVG TVLLMEALSG ISLNGLTIFS FCKTPDLRTP SNLLVLSLAL
ADTGISLNAL VAAVSSLLRR WPHGSEGCQV HGFQGFATAL ASICGSAAVA WGRYHHYCTR
RQLAWDTAIP LVLFVWMSSA FWASLPLMGW GHYDYEPVGT CCTLDYSRGD RNFISFLFTM
AFFNFLVPLF ITHTSYRFME QKFSRSGHLP VNTTLPGRML LLGWGPYALL YLYAAIADVS
FISPKLQMVP ALIAKTMPTI NAINYALHRE MVCRGTWQCL SPQKSKKDRT Q