Rhodopsin - Ovis aries (Sheep)

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P02700 (OPSD_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Rhodopsin

Gene names

Name:

RHO

Organism

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence 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	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 process	Sensory transduction Vision
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore Metal-binding Zinc
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Acetylation Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Direct protein sequencing
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 Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor inner segment membrane Inferred from sequence or structural similarity. Source: UniProtKB photoreceptor outer segment membrane Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	G-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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Rhodopsin

PRO_0000197719

Regions

Topological domain

1 – 36

Extracellular

Transmembrane

37 – 61

Helical; Name=1; Potential

Topological domain

62 – 73

Cytoplasmic

Transmembrane

74 – 98

Helical; Name=2; Potential

Topological domain

99 – 113

Extracellular

Transmembrane

114 – 133

Helical; Name=3; Potential

Topological domain

134 – 152

Cytoplasmic

Transmembrane

153 – 176

Helical; Name=4; Potential

Topological domain

177 – 202

Extracellular

Transmembrane

203 – 230

Helical; Name=5; Potential

Topological domain

231 – 252

Cytoplasmic

Transmembrane

253 – 276

Helical; Name=6; Potential

Topological domain

277 – 284

Extracellular

Transmembrane

285 – 309

Helical; Name=7; Potential

Topological domain

310 – 348

Cytoplasmic

Region

113 – 125

Retinal chromophore binding By similarity

Region

207 – 212

Retinal chromophore binding By similarity

Motif

134 – 137

'Ionic lock' involved in activated form stabilization

Sites

Metal binding

201

Zinc By similarity

Metal binding

279

Zinc By similarity

Binding site

265

Retinal chromophore By similarity

Binding site

296

Retinal chromophore (covalent) By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

296

N6-(retinylidene)lysine Ref.4

Modified residue

334

Phosphoserine Ref.5

Modified residue

334

Phosphoserine; by RK and GRK7 Ref.5

Modified residue

335

Phosphothreonine Ref.5

Modified residue

335

Phosphothreonine; by RK and GRK7 Ref.5

Modified residue

336

Phosphothreonine Ref.5

Modified residue

336

Phosphothreonine; by RK and GRK7 Ref.5

Modified residue

338

Phosphoserine; by RK and GRK7 Ref.5

Modified residue

340

Phosphothreonine By similarity

Modified residue

342

Phosphothreonine By similarity

Modified residue

343

Phosphoserine; by RK and GRK7 Ref.5

Lipidation

322

S-palmitoyl cysteine By similarity

Lipidation

323

S-palmitoyl cysteine By similarity

Glycosylation

N-linked (GlcNAc...) By similarity

Glycosylation

N-linked (GlcNAc...) By similarity

Disulfide bond

110 ↔ 187

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P02700 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: AAFD6F0D6A8BAEE5
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FASTA

348

38,892

        10         20         30         40         50         60 
MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY 

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

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

       190        200        210        220        230        240 
QGMQCSCGAL YFTLKPEINN ESFVIYMFVV HFSIPLIVIF FCYGQLVFTV KEAAAQQQES 

       250        260        270        280        290        300 
ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKSSSV 

       310        320        330        340 
YNPVIYIMMN KQFRNCMLTT LCCGKNPLGD DEASTTVSKT ETSQVAPA

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References

[1]	"A structural model for ovine rhodopsin." Pappin D.J.C., Elipoulos E., Brett M., Findlay J.B.C. Int. J. Biol. Macromol. 6:73-76(1984) Cited for: PROTEIN SEQUENCE.
[2]	"Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin." Brett M., Findlay J.B.C. Biochem. J. 211:661-670(1983) [PubMed: 6224479] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-111 AND 144-239.
[3]	"Primary structure of C-terminal functional sites in ovine rhodopsin." Findlay J.B.C., Brett M., Pappin D.J.C. Nature 293:314-316(1981) [PubMed: 7278988] [Abstract] Cited for: PROTEIN SEQUENCE OF 240-348.
[4]	"Sequence variability in the retinal-attachment domain of mammalian rhodopsins." Pappin D.J.C., Findlay J.B.C. Biochem. J. 217:605-613(1984) [PubMed: 6370231] [Abstract] Cited for: RETINAL-BINDING SITE.
[5]	"Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites." Thompson P., Findlay J.B.C. Biochem. J. 220:773-780(1984) [PubMed: 6466303] [Abstract] Cited for: PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338 AND SER-343.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	OOSH. A30407.
3D structure databases
ProteinModelPortal	P02700.
SMR	P02700. Positions 1-348.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG107442.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_supfam. IPR001760. Opsin. IPR000732. Rhodopsin. IPR019477. Rhodopsin_N. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. PF10413. Rhodopsin_N. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00238. OPSIN. PR00579. RHODOPSIN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. PS00238. OPSIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OPSD_SHEEP

Accession

Primary (citable) accession number: P02700

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1991
Last modified:	September 21, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents