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P47804

- RGR_HUMAN

UniProt

P47804 - RGR_HUMAN

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Protein

RPE-retinal G protein-coupled receptor

Gene

RGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. chemokine receptor activity Source: InterPro
  2. G-protein coupled receptor activity Source: ProtInc
  3. photoreceptor activity Source: UniProtKB-KW

GO - Biological processi

  1. chemotaxis Source: InterPro
  2. G-protein coupled receptor signaling pathway Source: ProtInc
  3. phototransduction Source: UniProtKB-KW
  4. protein-chromophore linkage Source: UniProtKB-KW
  5. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiREACT_18426. Opsins.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
RPE-retinal G protein-coupled receptor
Gene namesi
Name:RGR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9990. RGR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515ExtracellularSequence AnalysisAdd
BLAST
Transmembranei16 – 3621Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini37 – 5216CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei53 – 7321Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini74 – 9118ExtracellularSequence AnalysisAdd
BLAST
Transmembranei92 – 11221Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini113 – 13018CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei131 – 15121Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini152 – 17524ExtracellularSequence AnalysisAdd
BLAST
Transmembranei176 – 19621Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini197 – 21923CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei220 – 24021Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini241 – 2477ExtracellularSequence Analysis
Transmembranei248 – 26821Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini269 – 29123CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661S → R in RP44. 1 Publication
VAR_017034

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi613769. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA34360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291RPE-retinal G protein-coupled receptorPRO_0000197822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi88 ↔ 162PROSITE-ProRule annotation
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Modified residuei255 – 2551N6-(retinylidene)lysineBy similarity

Post-translational modificationi

Covalently binds all-trans- and 11-cis-retinal.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP47804.
PRIDEiP47804.

Expressioni

Tissue specificityi

Preferentially expressed at high levels in the retinal pigment epithelium (RPE) and Mueller cells of the neural retina.

Gene expression databases

BgeeiP47804.
CleanExiHS_RGR.
ExpressionAtlasiP47804. baseline and differential.
GenevestigatoriP47804.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KIAA1279Q96EK52EBI-745818,EBI-744150

Protein-protein interaction databases

BioGridi111927. 1 interaction.
IntActiP47804. 1 interaction.
MINTiMINT-1452896.
STRINGi9606.ENSP00000352427.

Structurei

3D structure databases

ProteinModelPortaliP47804.
SMRiP47804. Positions 13-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236124.
GeneTreeiENSGT00760000119394.
HOGENOMiHOG000293329.
HOVERGENiHBG017721.
InParanoidiP47804.
KOiK04254.
OMAiGICINAF.
OrthoDBiEOG75MVWJ.
PhylomeDBiP47804.
TreeFamiTF324998.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR027430. Retinal_BS.
IPR001793. RPE_GPCR.
[Graphical view]
PANTHERiPTHR24227. PTHR24227. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00667. RPERETINALR.
PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P47804-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAETSALPTG FGELEVLAVG MVLLVEALSG LSLNTLTIFS FCKTPELRTP
60 70 80 90 100
CHLLVLSLAL ADSGISLNAL VAATSSLLRR WPYGSDGCQA HGFQGFVTAL
110 120 130 140 150
ASICSSAAIA WGRYHHYCTR SQLAWNSAVS LVLFVWLSSA FWAALPLLGW
160 170 180 190 200
GHYDYEPLGT CCTLDYSKGD RNFTSFLFTM SFFNFAMPLF ITITSYSLME
210 220 230 240 250
QKLGKSGHLQ VNTTLPARTL LLGWGPYAIL YLYAVIADVT SISPKLQMVP
260 270 280 290
ALIAKMVPTI NAINYALGNE MVCRGIWQCL SPQKREKDRT K
Length:291
Mass (Da):31,874
Last modified:February 1, 1996 - v1
Checksum:i85AB087E09719E88
GO
Isoform 2 (identifier: P47804-2) [UniParc]FASTAAdd to Basket

Also known as: Long

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

Show »
Length:295
Mass (Da):32,354
Checksum:i4224150E95726B6D
GO
Isoform 3 (identifier: P47804-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:253
Mass (Da):27,728
Checksum:i4D610689536B5767
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661S → R in RP44. 1 Publication
VAR_017034
Natural varianti132 – 1321V → L.1 Publication
VAR_017055
Natural varianti152 – 1521H → N.1 Publication
Corresponds to variant rs150808273 [ dbSNP | Ensembl ].
VAR_017056
Natural varianti234 – 2341A → T.1 Publication
VAR_017058
Natural varianti241 – 2411S → F.1 Publication
VAR_017057

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 781L → LRVSH in isoform 2. 2 PublicationsVSP_003773
Alternative sequencei211 – 24838Missing in isoform 3. 1 PublicationVSP_038387Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41543.1. [P47804-3]
CCDS7374.1. [P47804-2]
PIRiA55980.
B55980.
RefSeqiNP_001012738.1. NM_001012720.1. [P47804-1]
NP_001012740.1. NM_001012722.1. [P47804-3]
NP_002912.2. NM_002921.3. [P47804-2]
UniGeneiHs.1544.

Genome annotation databases

EnsembliENST00000358110; ENSP00000350823; ENSG00000148604. [P47804-3]
ENST00000359452; ENSP00000352427; ENSG00000148604. [P47804-2]
GeneIDi5995.
KEGGihsa:5995.
UCSCiuc001kdc.1. human. [P47804-1]
uc001kdd.1. human. [P47804-2]
uc001kde.1. human. [P47804-3]

Polymorphism databases

DMDMi1350592.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the RGR gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41543.1. [P47804-3 ]
CCDS7374.1. [P47804-2 ]
PIRi A55980.
B55980.
RefSeqi NP_001012738.1. NM_001012720.1. [P47804-1 ]
NP_001012740.1. NM_001012722.1. [P47804-3 ]
NP_002912.2. NM_002921.3. [P47804-2 ]
UniGenei Hs.1544.

3D structure databases

ProteinModelPortali P47804.
SMRi P47804. Positions 13-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111927. 1 interaction.
IntActi P47804. 1 interaction.
MINTi MINT-1452896.
STRINGi 9606.ENSP00000352427.

Protein family/group databases

GPCRDBi Search...

Polymorphism databases

DMDMi 1350592.

Proteomic databases

PaxDbi P47804.
PRIDEi P47804.

Protocols and materials databases

DNASUi 5995.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358110 ; ENSP00000350823 ; ENSG00000148604 . [P47804-3 ]
ENST00000359452 ; ENSP00000352427 ; ENSG00000148604 . [P47804-2 ]
GeneIDi 5995.
KEGGi hsa:5995.
UCSCi uc001kdc.1. human. [P47804-1 ]
uc001kdd.1. human. [P47804-2 ]
uc001kde.1. human. [P47804-3 ]

Organism-specific databases

CTDi 5995.
GeneCardsi GC10P085994.
GeneReviewsi RGR.
HGNCi HGNC:9990. RGR.
MIMi 600342. gene.
613769. phenotype.
neXtProti NX_P47804.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA34360.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236124.
GeneTreei ENSGT00760000119394.
HOGENOMi HOG000293329.
HOVERGENi HBG017721.
InParanoidi P47804.
KOi K04254.
OMAi GICINAF.
OrthoDBi EOG75MVWJ.
PhylomeDBi P47804.
TreeFami TF324998.

Enzyme and pathway databases

Reactomei REACT_18426. Opsins.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikii Retinal_G_protein_coupled_receptor.
GenomeRNAii 5995.
NextBioi 23359.
PROi P47804.
SOURCEi Search...

Gene expression databases

Bgeei P47804.
CleanExi HS_RGR.
ExpressionAtlasi P47804. baseline and differential.
Genevestigatori P47804.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR027430. Retinal_BS.
IPR001793. RPE_GPCR.
[Graphical view ]
PANTHERi PTHR24227. PTHR24227. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00237. GPCRRHODOPSN.
PR00667. RPERETINALR.
PROSITEi PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRGR_HUMAN
AccessioniPrimary (citable) accession number: P47804
Secondary accession number(s): A6NKK7, Q96FC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3