RGR_BOVIN
ID RGR_BOVIN Reviewed; 291 AA.
AC P47803; Q148K9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RPE-retinal G protein-coupled receptor;
GN Name=RGR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8258527;
RA Jiang M., Pandey S., Fong H.K.W.;
RT "An opsin homologue in the retina and pigment epithelium.";
RL Invest. Ophthalmol. Vis. Sci. 34:3669-3678(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Preferentially expressed at high levels in the
CC retinal pigment epithelium (RPE) and Mueller cells of the neural
CC retina.
CC -!- PTM: Covalently binds all-trans- and 11-cis-retinal.
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; S67535; AAB29270.1; -; mRNA.
DR EMBL; BC118188; AAI18189.1; -; mRNA.
DR PIR; I46965; I46965.
DR RefSeq; NP_786969.1; NM_175775.2.
DR AlphaFoldDB; P47803; -.
DR SMR; P47803; -.
DR STRING; 9913.ENSBTAP00000020822; -.
DR PaxDb; P47803; -.
DR Ensembl; ENSBTAT00000020822; ENSBTAP00000020822; ENSBTAG00000015681.
DR GeneID; 280911; -.
DR KEGG; bta:280911; -.
DR CTD; 5995; -.
DR VEuPathDB; HostDB:ENSBTAG00000015681; -.
DR VGNC; VGNC:33909; RGR.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244811; -.
DR HOGENOM; CLU_009579_3_2_1; -.
DR InParanoid; P47803; -.
DR OMA; CWGPYAL; -.
DR OrthoDB; 704940at2759; -.
DR TreeFam; TF324998; -.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-419771; Opsins.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000015681; Expressed in retina and 29 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; IPR027430; Retinal_BS.
DR InterPro; IPR001793; RPE_GPCR.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00667; RPERETINALR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..291
FT /note="RPE-retinal G protein-coupled receptor"
FT /id="PRO_0000197821"
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 CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 291 AA; 31961 MW; A25964BBDCA25E98 CRC64;
MAESGTLPTG FGELEVLAVG TVLLVEALSG LSLNILTILS FCKTPELRTP SHLLVLSLAL
ADSGISLNAL VAATSSLLRR WPYGSEGCQA HGFQGFVTAL ASICSSAAVA WGRYHHFCTR
SRLDWNTAVS LVFFVWLSSA FWAALPLLGW GHYDYEPLGT CCTLDYSRGD RNFTSFLFTM
AFFNFLLPLF ITVVSYRLME QKLGKTSRPP VNTVLPARTL LLGWGPYALL YLYATIADAT
SISPKLQMVP ALIAKAVPTV NAMNYALGSE MVHRGIWQCL SPQRREHSRE Q
