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Protein

Rhodopsin

Gene

Rho

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).By similarity

Absorptioni

Abs(max)=495 nm

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi201ZincBy similarity1
Binding sitei265Retinal chromophoreBy similarity1
Metal bindingi279ZincBy similarity1

GO - Molecular functioni

  • G-protein coupled photoreceptor activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • retinal binding Source: RGD
  • spectrin binding Source: MGI

GO - Biological processi

  • absorption of visible light Source: AgBase
  • protein-chromophore linkage Source: UniProtKB-KW
  • red, far-red light phototransduction Source: RGD
  • rhodopsin mediated signaling pathway Source: RGD
  • visual perception Source: UniProtKB-KW
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, Metal-binding, Zinc

Names & Taxonomyi

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

Organism-specific databases

RGDi3573. Rho.

Subcellular locationi

  • Membrane; Multi-pass membrane protein

  • Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 36ExtracellularAdd BLAST36
Transmembranei37 – 61Helical; Name=1Sequence analysisAdd BLAST25
Topological domaini62 – 73CytoplasmicAdd BLAST12
Transmembranei74 – 98Helical; Name=2Sequence analysisAdd BLAST25
Topological domaini99 – 113ExtracellularAdd BLAST15
Transmembranei114 – 133Helical; Name=3Sequence analysisAdd BLAST20
Topological domaini134 – 152CytoplasmicAdd BLAST19
Transmembranei153 – 176Helical; Name=4Sequence analysisAdd BLAST24
Topological domaini177 – 202ExtracellularAdd BLAST26
Transmembranei203 – 230Helical; Name=5Sequence analysisAdd BLAST28
Topological domaini231 – 252CytoplasmicAdd BLAST22
Transmembranei253 – 276Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini277 – 284Extracellular8
Transmembranei285 – 309Helical; Name=7Sequence analysisAdd BLAST25
Topological domaini310 – 348CytoplasmicAdd BLAST39

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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...)By similarity1
Glycosylationi15N-linked (GlcNAc...)By similarity1
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.
Contains one covalently linked retinal chromophore.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP51489.
PRIDEiP51489.

PTM databases

iPTMnetiP51489.
PhosphoSitePlusiP51489.

Expressioni

Tissue specificityi

Rod shaped photoreceptor cells which mediates vision in dim light.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • spectrin binding Source: MGI

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061473.

Structurei

3D structure databases

ProteinModelPortaliP51489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 125Retinal chromophore bindingBy similarityAdd BLAST13
Regioni207 – 212Retinal chromophore bindingBy similarity6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi134 – 137'Ionic lock' involved in activated form stabilization4

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

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP51489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061473.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP51489.
PhosphoSitePlusiP51489.

Proteomic databases

PaxDbiP51489.
PRIDEiP51489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24717.
KEGGirno:24717.
UCSCiRGD:3573. rat.

Organism-specific databases

CTDi6010.
RGDi3573. Rho.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiP51489.
KOiK04250.
PhylomeDBiP51489.
TreeFamiTF324998.

Miscellaneous databases

PROiP51489.

Family and domain databases

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOPSD_RAT
AccessioniPrimary (citable) accession number: P51489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.