P47804 (RGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RPE-retinal G protein-coupled receptor

Gene names

Name:

RGR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for all-trans- and 11-cis-retinal. Binds preferentially to the former and may catalyze the isomerization of the chromophore by a retinochrome-like mechanism.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Preferentially expressed at high levels in the retinal pigment epithelium (RPE) and Mueller cells of the neural retina.
Post-translational modification	Covalently binds all-trans- and 11-cis-retinal.
Involvement in disease	Retinitis pigmentosa 44 (RP44) [MIM:613769]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Retinitis pigmentosa
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phototransduction Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement PubMed 8641686. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement PubMed 8641686. Source: ProtInc
Molecular_function	G-protein coupled receptor activity Traceable author statement PubMed 8641686. Source: ProtInc photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KIAA1279	Q96EK5	2	EBI-745818,EBI-744150

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P47804-1)

Also known as: Short;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P47804-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     78-78: L → LRVSH

Isoform 3 (identifier: P47804-3)

The sequence of this isoform differs from the canonical sequence as follows:
     211-248: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 291	291	RPE-retinal G protein-coupled receptor		PRO_0000197822
Regions
	Topological domain	1 – 15	15	Extracellular Potential
	Transmembrane	16 – 36	21	Helical; Name=1; Potential
	Topological domain	37 – 52	16	Cytoplasmic Potential
	Transmembrane	53 – 73	21	Helical; Name=2; Potential
	Topological domain	74 – 91	18	Extracellular Potential
	Transmembrane	92 – 112	21	Helical; Name=3; Potential
	Topological domain	113 – 130	18	Cytoplasmic Potential
	Transmembrane	131 – 151	21	Helical; Name=4; Potential
	Topological domain	152 – 175	24	Extracellular Potential
	Transmembrane	176 – 196	21	Helical; Name=5; Potential
	Topological domain	197 – 219	23	Cytoplasmic Potential
	Transmembrane	220 – 240	21	Helical; Name=6; Potential
	Topological domain	241 – 247	7	Extracellular Potential
	Transmembrane	248 – 268	21	Helical; Name=7; Potential
	Topological domain	269 – 291	23	Cytoplasmic Potential
Amino acid modifications
	Modified residue	255	1	N6-(retinylidene)lysine By similarity
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Disulfide bond	88 ↔ 162		Potential
Natural variations
	Alternative sequence	78	1	L → LRVSH in isoform 2.		VSP_003773
	Alternative sequence	211 – 248	38	Missing in isoform 3.		VSP_038387
	Natural variant	66	1	S → R in RP44. Ref.4		VAR_017034
	Natural variant	132	1	V → L. Ref.4		VAR_017055
	Natural variant	152	1	H → N. Ref.4		VAR_017056
	Natural variant	234	1	A → T. Ref.4		VAR_017058
	Natural variant	241	1	S → F. Ref.4		VAR_017057

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Short) [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 85AB087E09719E88	FASTA	291	31,874
	10 20 30 40 50 60 MAETSALPTG FGELEVLAVG MVLLVEALSG LSLNTLTIFS FCKTPELRTP CHLLVLSLAL 70 80 90 100 110 120 ADSGISLNAL VAATSSLLRR WPYGSDGCQA HGFQGFVTAL ASICSSAAIA WGRYHHYCTR 130 140 150 160 170 180 SQLAWNSAVS LVLFVWLSSA FWAALPLLGW GHYDYEPLGT CCTLDYSKGD RNFTSFLFTM 190 200 210 220 230 240 SFFNFAMPLF ITITSYSLME QKLGKSGHLQ VNTTLPARTL LLGWGPYAIL YLYAVIADVT 250 260 270 280 290 SISPKLQMVP ALIAKMVPTI NAINYALGNE MVCRGIWQCL SPQKREKDRT K
	Isoform 2 (Long) [UniParc]. Checksum: 4224150E95726B6D	FASTA	295	32,354
	10 20 30 40 50 60 MAETSALPTG FGELEVLAVG MVLLVEALSG LSLNTLTIFS FCKTPELRTP CHLLVLSLAL 70 80 90 100 110 120 ADSGISLNAL VAATSSLLRV SHRRWPYGSD GCQAHGFQGF VTALASICSS AAIAWGRYHH 130 140 150 160 170 180 YCTRSQLAWN SAVSLVLFVW LSSAFWAALP LLGWGHYDYE PLGTCCTLDY SKGDRNFTSF 190 200 210 220 230 240 LFTMSFFNFA MPLFITITSY SLMEQKLGKS GHLQVNTTLP ARTLLLGWGP YAILYLYAVI 250 260 270 280 290 ADVTSISPKL QMVPALIAKM VPTINAINYA LGNEMVCRGI WQCLSPQKRE KDRTK
	Isoform 3 [UniParc]. Checksum: 4D610689536B5767	FASTA	253	27,728
	10 20 30 40 50 60 MAETSALPTG FGELEVLAVG MVLLVEALSG LSLNTLTIFS FCKTPELRTP CHLLVLSLAL 70 80 90 100 110 120 ADSGISLNAL VAATSSLLRR WPYGSDGCQA HGFQGFVTAL ASICSSAAIA WGRYHHYCTR 130 140 150 160 170 180 SQLAWNSAVS LVLFVWLSSA FWAALPLLGW GHYDYEPLGT CCTLDYSKGD RNFTSFLFTM 190 200 210 220 230 240 SFFNFAMPLF ITITSYSLME QKLGKSGHLQ VPALIAKMVP TINAINYALG NEMVCRGIWQ 250 CLSPQKREKD RTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human opsin-related gene that encodes a retinaldehyde-binding protein." Shen D., Jiang M., Hao W., Tao L., Salazar M., Fong H.K.W. Biochemistry 33:13117-13125(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). Tissue: Retina.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-265 (ISOFORM 3). Tissue: Brain.
[4]	"Mutations in RGR, encoding a light-sensitive opsin homologue, in patients with retinitis pigmentosa." Morimura H., Saindelle-Ribeaudeau F., Berson E.L., Dryja T.P. Nat. Genet. 23:393-394(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP44 ARG-66, VARIANTS LEU-132; ASN-152; THR-234 AND PHE-241.
+	Additional computationally mapped references.

Web resources

Mutations of the RGR gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15790 , U14911, U15785, U15786, U15787, U15788, U15789 Genomic DNA. Translation: AAB92384.1. U14910 mRNA. Translation: AAA56748.1. AC022389 Genomic DNA. No translation available. BG912392 mRNA. No translation available. BC011349 mRNA. Translation: AAH11349.1.
IPI	IPI00026539. IPI00554654. IPI00843916.
PIR	A55980. B55980.
RefSeq	NP_001012738.1. NM_001012720.1. NP_001012740.1. NM_001012722.1. NP_002912.2. NM_002921.3.
UniGene	Hs.1544.
3D structure databases
ProteinModelPortal	P47804.
ModBase	Search...
Protein-protein interaction databases
IntAct	P47804. 1 interaction.
MINT	MINT-1452896.
STRING	9606.ENSP00000352427.
Protein family/group databases
GPCRDB	Search...
Polymorphism databases
DMDM	1350592.
Proteomic databases
PaxDb	P47804.
PRIDE	P47804.
Protocols and materials databases
DNASU	5995.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358110; ENSP00000350823; ENSG00000148604. ENST00000359452; ENSP00000352427; ENSG00000148604.
GeneID	5995.
KEGG	hsa:5995.
UCSC	uc001kdc.1. human. uc001kdd.1. human. uc001kde.1. human.
Organism-specific databases
CTD	5995.
GeneCards	GC10P085994.
HGNC	HGNC:9990. RGR.
MIM	600342. gene. 613769. phenotype.
neXtProt	NX_P47804.
Orphanet	791. Retinitis pigmentosa.
PharmGKB	PA34360.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236124.
HOGENOM	HOG000293329.
HOVERGEN	HBG017721.
KO	K04254.
OMA	RSQLAWN.
OrthoDB	EOG4GF3FP.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P47804.
Bgee	P47804.
CleanEx	HS_RGR.
Genevestigator	P47804.
GermOnline	ENSG00000148604. Homo sapiens.
Family and domain databases
InterPro	IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR001760. Opsin. IPR001793. RPE_GPCR. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00667. RPERETINALR.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. False negative. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. PS00238. OPSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5995.
NextBio	23359.
SOURCE	Search...

Entry information

Entry name

RGR_HUMAN

Accession

Primary (citable) accession number: P47804
Secondary accession number(s): A6NKK7, Q96FC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.