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Protein

Rhodopsin

Gene

Rho

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei113Plays an important role in the conformation switch to the active conformationBy similarity1
Metal bindingi201ZincBy similarity1
Metal bindingi279ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionG-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer
Biological processSensory transduction, Vision
LigandChromophore, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:Rho
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3573 Rho

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 36ExtracellularCuratedAdd BLAST36
Transmembranei37 – 61Helical; Name=1By similarityAdd BLAST25
Topological domaini62 – 73CytoplasmicCuratedAdd BLAST12
Transmembranei74 – 96Helical; Name=2By similarityAdd BLAST23
Topological domaini97 – 110ExtracellularCuratedAdd BLAST14
Transmembranei111 – 133Helical; Name=3By similarityAdd BLAST23
Topological domaini134 – 152CytoplasmicCuratedAdd BLAST19
Transmembranei153 – 173Helical; Name=4By similarityAdd BLAST21
Topological domaini174 – 202ExtracellularCuratedAdd BLAST29
Transmembranei203 – 224Helical; Name=5By similarityAdd BLAST22
Topological domaini225 – 252CytoplasmicCuratedAdd BLAST28
Transmembranei253 – 274Helical; Name=6By similarityAdd BLAST22
Topological domaini275 – 286ExtracellularCuratedAdd BLAST12
Transmembranei287 – 308Helical; Name=7By similarityAdd BLAST22
Topological domaini309 – 348CytoplasmicCuratedAdd BLAST40

Keywords - Cellular componenti

Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001977081 – 348RhodopsinAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Glycosylationi2N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi15N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation
Modified residuei296N6-(retinylidene)lysineBy similarity1
Lipidationi322S-palmitoyl cysteineBy similarity1
Lipidationi323S-palmitoyl cysteineBy similarity1
Modified residuei334PhosphoserineBy similarity1
Modified residuei336PhosphothreonineBy similarity1
Modified residuei338PhosphoserineBy similarity1
Modified residuei340PhosphothreonineBy similarity1
Modified residuei342PhosphothreonineBy similarity1
Modified residuei343PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.By similarity
Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP51489
PRIDEiP51489

PTM databases

iPTMnetiP51489
PhosphoSitePlusiP51489

Interactioni

Subunit structurei

Homodimer. Interacts (phosphorylated form) with SAG. Interacts with GNAT1, Interacts with GNAT3. SAG and G-proteins compete for a common binding site. Interacts with GRK1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061473

Structurei

3D structure databases

ProteinModelPortaliP51489
SMRiP51489
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni330 – 348Interaction with SAGBy similarityAdd BLAST19

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi134 – 136'Ionic lock' involved in activated form stabilizationBy similarity3

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
HOGENOMiHOG000253932
HOVERGENiHBG107442
InParanoidiP51489
KOiK04250
PhylomeDBiP51489
TreeFamiTF324998

Family and domain databases

InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR001760 Opsin
IPR027430 Retinal_BS
IPR000732 Rhodopsin
IPR019477 Rhodopsin_N
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PF10413 Rhodopsin_N, 1 hit
PRINTSiPR00237 GPCRRHODOPSN
PR00238 OPSIN
PR00579 RHODOPSIN
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit
PS00238 OPSIN, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

P51489-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNGTEGPNFY VPFSNITGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL
60 70 80 90 100
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH
110 120 130 140 150
GYFVFGPTGC NLEGFFATLG GEIGLWSLVV LAIERYVVVC KPMSNFRFGE
160 170 180 190 200
NHAIMGVAFT WVMALACAAP PLVGWSRYIP EGMQCSCGID YYTLKPEVNN
210 220 230 240 250
ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
260 270 280 290 300
TRMVIIMVIF FLICWLPYAS VAMYIFTHQG SNFGPIFMTL PAFFAKTASI
310 320 330 340
YNPIIYIMMN KQFRNCMLTS LCCGKNPLGD DEASATASKT ETSQVAPA
Length:348
Mass (Da):39,042
Last modified:October 1, 1996 - v1
Checksum:iDA0F3F90C30984BC
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSY7A0A0G2JSY7_RAT
Rhodopsin
Rho rCG_29898
348Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti320S → T in CAA87081 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22180 Genomic DNA Translation: AAA84439.1
Z46957 mRNA Translation: CAA87081.1
PIRiS51677
RefSeqiNP_254276.1, NM_033441.1
UniGeneiRn.92530

Genome annotation databases

GeneIDi24717
KEGGirno:24717
UCSCiRGD:3573 rat

Similar proteinsi

Entry informationi

Entry nameiOPSD_RAT
AccessioniPrimary (citable) accession number: P51489
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 136 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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