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P51489 (OPSD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhodopsin
Gene names
Name:Rho
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer By similarity.

Subcellular location

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.

Tissue specificity

Rod shaped photoreceptor cells which mediates vision in dim light.

Post-translational modification

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.

Sequence similarities

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

Biophysicochemical properties

Absorption:

Abs(max)=495 nm

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandChromophore
Metal-binding
Zinc
   Molecular functionG-protein coupled receptor
Photoreceptor protein
Receptor
Retinal protein
Transducer
   PTMAcetylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

red, far-red light phototransduction

Inferred from direct assay PubMed 2525480. Source: RGD

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

rhodopsin mediated signaling pathway

Inferred from direct assay PubMed 8814134. Source: RGD

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

photoreceptor inner segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay PubMed 8814134. Source: RGD

photoreceptor outer segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

rough endoplasmic reticulum membrane

Inferred from direct assay PubMed 2525480. Source: RGD

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

photoreceptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

retinal binding

Inferred from direct assay PubMed 2525480PubMed 8814134. Source: RGD

spectrin binding

Inferred from direct assay PubMed 23704327. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Rhodopsin
PRO_0000197708

Regions

Topological domain1 – 3636Extracellular
Transmembrane37 – 6125Helical; Name=1; Potential
Topological domain62 – 7312Cytoplasmic
Transmembrane74 – 9825Helical; Name=2; Potential
Topological domain99 – 11315Extracellular
Transmembrane114 – 13320Helical; Name=3; Potential
Topological domain134 – 15219Cytoplasmic
Transmembrane153 – 17624Helical; Name=4; Potential
Topological domain177 – 20226Extracellular
Transmembrane203 – 23028Helical; Name=5; Potential
Topological domain231 – 25222Cytoplasmic
Transmembrane253 – 27624Helical; Name=6; Potential
Topological domain277 – 2848Extracellular
Transmembrane285 – 30925Helical; Name=7; Potential
Topological domain310 – 34839Cytoplasmic
Region113 – 12513Retinal chromophore binding By similarity
Region207 – 2126Retinal chromophore binding By similarity
Motif134 – 1374'Ionic lock' involved in activated form stabilization

Sites

Metal binding2011Zinc By similarity
Metal binding2791Zinc By similarity
Binding site2651Retinal chromophore By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2961N6-(retinylidene)lysine By similarity
Modified residue3341Phosphoserine By similarity
Modified residue3361Phosphothreonine By similarity
Modified residue3381Phosphoserine By similarity
Modified residue3401Phosphothreonine By similarity
Modified residue3421Phosphothreonine By similarity
Modified residue3431Phosphoserine By similarity
Lipidation3221S-palmitoyl cysteine By similarity
Lipidation3231S-palmitoyl cysteine By similarity
Glycosylation21N-linked (GlcNAc...) By similarity
Glycosylation151N-linked (GlcNAc...) By similarity
Disulfide bond110 ↔ 187 By similarity

Experimental info

Sequence conflict3201S → T in CAA87081. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51489 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DA0F3F90C30984BC

FASTA34839,042
        10         20         30         40         50         60 
MNGTEGPNFY VPFSNITGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY 

        70         80         90        100        110        120 
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG 

       130        140        150        160        170        180 
GEIGLWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP 

       190        200        210        220        230        240 
EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES 

       250        260        270        280        290        300 
ATTQKAEKEV TRMVIIMVIF FLICWLPYAS VAMYIFTHQG SNFGPIFMTL PAFFAKTASI 

       310        320        330        340 
YNPIIYIMMN KQFRNCMLTS LCCGKNPLGD DEASATASKT ETSQVAPA 

« Hide

References

[1]"Isolation and coding sequence of the rat rod opsin gene."
Barnstable C.J., Morabito M.A.
J. Mol. Neurosci. 5:207-209(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Retinal rod cell.
[2]Huber A., Baker B.B., Sander P., Gerdon G., Paulsen R., Williams T.P.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22180 Genomic DNA. Translation: AAA84439.1.
Z46957 mRNA. Translation: CAA87081.1.
PIRS51677.
RefSeqNP_254276.1. NM_033441.1.
UniGeneRn.92530.

3D structure databases

ProteinModelPortalP51489.
SMRP51489. Positions 1-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000061473.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP51489.

Proteomic databases

PaxDbP51489.
PRIDEP51489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000064603; ENSRNOP00000061473; ENSRNOG00000011144.
GeneID24717.
KEGGrno:24717.
UCSCRGD:3573. rat.

Organism-specific databases

CTD6010.
RGD3573. Rho.

Phylogenomic databases

eggNOGNOG311294.
GeneTreeENSGT00710000106574.
HOGENOMHOG000253932.
HOVERGENHBG107442.
InParanoidP51489.
KOK04250.
OrthoDBEOG72NRQJ.
PhylomeDBP51489.
TreeFamTF324998.

Gene expression databases

GenevestigatorP51489.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
4.10.840.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604217.
PROP51489.

Entry information

Entry nameOPSD_RAT
AccessionPrimary (citable) accession number: P51489
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries