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Protein

Rhodopsin

Gene

RHO

Organism
Bos taurus (Bovine)
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 similarity2 Publications

Absorptioni

Abs(max)=~495 nm

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi201ZincCombined sources2 Publications1
Binding sitei265Retinal chromophore3 Publications1
Metal bindingi279ZincCombined sources2 Publications1

GO - Molecular functioni

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiR-BTA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-418594. G alpha (i) signalling events.
R-BTA-419771. Opsins.
R-BTA-5620916. VxPx cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:RHO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

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 – 63Helical; Name=1Add BLAST27
Topological domaini64 – 73Cytoplasmic10
Transmembranei74 – 96Helical; Name=2Add BLAST23
Topological domaini97 – 110ExtracellularAdd BLAST14
Transmembranei111 – 133Helical; Name=3Add BLAST23
Topological domaini134 – 152CytoplasmicAdd BLAST19
Transmembranei153 – 173Helical; Name=4Add BLAST21
Topological domaini174 – 202ExtracellularAdd BLAST29
Transmembranei203 – 224Helical; Name=5Add BLAST22
Topological domaini225 – 249CytoplasmicAdd BLAST25
Transmembranei250 – 274Helical; Name=6Add BLAST25
Topological domaini275 – 286ExtracellularAdd BLAST12
Transmembranei287 – 308Helical; Name=7Add BLAST22
Topological domaini309 – 348CytoplasmicAdd BLAST40

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2N → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. 1 Publication1
Mutagenesisi15N → D: Normal light absorption; when associated with C-2 and C-282. 1 Publication1
Mutagenesisi282D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5739.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001976531 – 348RhodopsinAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Glycosylationi2N-linked (GlcNAc...)3 Publications1
Glycosylationi15N-linked (GlcNAc...)3 Publications1
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation1 Publication
Modified residuei296N6-(retinylidene)lysine1
Lipidationi322S-palmitoyl cysteine3 Publications1
Lipidationi323S-palmitoyl cysteine3 Publications1
Modified residuei334Phosphoserine2 Publications1
Modified residuei335Phosphothreonine2 Publications1
Modified residuei336Phosphothreonine2 Publications1
Modified residuei338Phosphoserine2 Publications1
Modified residuei340Phosphothreonine2 Publications1
Modified residuei342Phosphothreonine2 Publications1
Modified residuei343Phosphoserine; by RK and GRK73 Publications1

Post-translational modificationi

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.3 Publications
Contains one covalently linked retinal chromophore.

Keywords - PTMi

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

Proteomic databases

PaxDbiP02699.

PTM databases

iPTMnetiP02699.
SwissPalmiP02699.
UniCarbKBiP02699.

Expressioni

Tissue specificityi

Rod shaped photoreceptor cells which mediates vision in dim light.

Interactioni

Subunit structurei

Homodimer.5 Publications

Protein-protein interaction databases

BioGridi166570. 2 interactors.
DIPiDIP-29225N.
IntActiP02699. 4 interactors.
MINTiMINT-1507462.
STRINGi9913.ENSBTAP00000001730.

Chemistry databases

BindingDBiP02699.

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi10 – 13Combined sources4
Helixi15 – 17Combined sources3
Turni23 – 25Combined sources3
Turni29 – 31Combined sources3
Helixi34 – 64Combined sources31
Helixi66 – 68Combined sources3
Helixi71 – 89Combined sources19
Helixi91 – 100Combined sources10
Helixi103 – 105Combined sources3
Helixi106 – 139Combined sources34
Beta strandi143 – 145Combined sources3
Helixi150 – 168Combined sources19
Helixi170 – 172Combined sources3
Turni175 – 177Combined sources3
Beta strandi179 – 181Combined sources3
Turni182 – 185Combined sources4
Beta strandi186 – 188Combined sources3
Helixi192 – 195Combined sources4
Helixi196 – 198Combined sources3
Helixi200 – 210Combined sources11
Helixi213 – 223Combined sources11
Turni224 – 228Combined sources5
Turni229 – 231Combined sources3
Turni235 – 238Combined sources4
Beta strandi239 – 241Combined sources3
Helixi242 – 277Combined sources36
Turni278 – 280Combined sources3
Helixi285 – 294Combined sources10
Helixi295 – 299Combined sources5
Helixi301 – 308Combined sources8
Helixi311 – 321Combined sources11
Turni322 – 324Combined sources3
Turni328 – 330Combined sources3
Beta strandi332 – 334Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi339 – 342Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOJmodel-A1-348[»]
1BOKmodel-A1-348[»]
1EDSNMR-A93-123[»]
1EDVNMR-A172-205[»]
1EDWNMR-A268-293[»]
1EDXNMR-A1-40[»]
1F88X-ray2.80A/B1-348[»]
1FDFNMR-A291-315[»]
1GZMX-ray2.65A/B1-348[»]
1HZXX-ray2.80A/B1-348[»]
1JFPNMR-A1-348[»]
1L9HX-ray2.60A/B1-348[»]
1LN6NMR-A1-348[»]
1N3Mmodel-A/B/C/D/E/F1-348[»]
1NZSNMR-A330-348[»]
1OV0model-A1-348[»]
1OV1model-A1-348[»]
1U19X-ray2.20A/B1-348[»]
1VQXNMR-A330-348[»]
2G87X-ray2.60A/B1-348[»]
2HPYX-ray2.80A/B1-348[»]
2I35X-ray3.80A1-348[»]
2I36X-ray4.10A/B/C1-348[»]
2I37X-ray4.15A/B/C1-348[»]
2IQKmodel-A1-348[»]
2J4YX-ray3.40A/B1-348[»]
2PEDX-ray2.95A/B1-348[»]
2X72X-ray3.00A1-348[»]
3C9LX-ray2.65A1-348[»]
3C9MX-ray3.40A1-348[»]
3CAPX-ray2.90A/B1-348[»]
3DQBX-ray3.20A1-348[»]
3OAXX-ray2.60A/B1-348[»]
3PQRX-ray2.85A1-348[»]
3PXOX-ray3.00A1-348[»]
4A4MX-ray3.30A1-348[»]
4BEYX-ray2.90A1-348[»]
4BEZX-ray3.30A1-348[»]
4J4QX-ray2.65A1-348[»]
4PXFX-ray2.75A1-348[»]
4X1HX-ray2.29A1-348[»]
5DYSX-ray2.30A1-348[»]
5EN0X-ray2.81A1-348[»]
DisProtiDP00271.
ProteinModelPortaliP02699.
SMRiP02699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02699.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 125Retinal chromophore bindingAdd BLAST13
Regioni207 – 212Retinal chromophore binding6

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.
GeneTreeiENSGT00760000118977.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiP02699.
KOiK04250.
OMAiLAAYMFM.
OrthoDBiEOG091G0BDA.
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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
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.

P02699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML
60 70 80 90 100
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH
110 120 130 140 150
GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE
160 170 180 190 200
NHAIMGVAFT WVMALACAAP PLVGWSRYIP EGMQCSCGID YYTPHEETNN
210 220 230 240 250
ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
260 270 280 290 300
TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV
310 320 330 340
YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA
Length:348
Mass (Da):39,008
Last modified:July 21, 1986 - v1
Checksum:i33FDA196803E81F3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti281S → F in AAA30675 (PubMed:2950966).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00506
, K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.
PIRiA90840. OOBO.
RefSeqiNP_001014890.1. NM_001014890.2.
UniGeneiBt.12753.

Genome annotation databases

EnsembliENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneIDi509933.
KEGGibta:509933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00506
, K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.
PIRiA90840. OOBO.
RefSeqiNP_001014890.1. NM_001014890.2.
UniGeneiBt.12753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOJmodel-A1-348[»]
1BOKmodel-A1-348[»]
1EDSNMR-A93-123[»]
1EDVNMR-A172-205[»]
1EDWNMR-A268-293[»]
1EDXNMR-A1-40[»]
1F88X-ray2.80A/B1-348[»]
1FDFNMR-A291-315[»]
1GZMX-ray2.65A/B1-348[»]
1HZXX-ray2.80A/B1-348[»]
1JFPNMR-A1-348[»]
1L9HX-ray2.60A/B1-348[»]
1LN6NMR-A1-348[»]
1N3Mmodel-A/B/C/D/E/F1-348[»]
1NZSNMR-A330-348[»]
1OV0model-A1-348[»]
1OV1model-A1-348[»]
1U19X-ray2.20A/B1-348[»]
1VQXNMR-A330-348[»]
2G87X-ray2.60A/B1-348[»]
2HPYX-ray2.80A/B1-348[»]
2I35X-ray3.80A1-348[»]
2I36X-ray4.10A/B/C1-348[»]
2I37X-ray4.15A/B/C1-348[»]
2IQKmodel-A1-348[»]
2J4YX-ray3.40A/B1-348[»]
2PEDX-ray2.95A/B1-348[»]
2X72X-ray3.00A1-348[»]
3C9LX-ray2.65A1-348[»]
3C9MX-ray3.40A1-348[»]
3CAPX-ray2.90A/B1-348[»]
3DQBX-ray3.20A1-348[»]
3OAXX-ray2.60A/B1-348[»]
3PQRX-ray2.85A1-348[»]
3PXOX-ray3.00A1-348[»]
4A4MX-ray3.30A1-348[»]
4BEYX-ray2.90A1-348[»]
4BEZX-ray3.30A1-348[»]
4J4QX-ray2.65A1-348[»]
4PXFX-ray2.75A1-348[»]
4X1HX-ray2.29A1-348[»]
5DYSX-ray2.30A1-348[»]
5EN0X-ray2.81A1-348[»]
DisProtiDP00271.
ProteinModelPortaliP02699.
SMRiP02699.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi166570. 2 interactors.
DIPiDIP-29225N.
IntActiP02699. 4 interactors.
MINTiMINT-1507462.
STRINGi9913.ENSBTAP00000001730.

Chemistry databases

BindingDBiP02699.
ChEMBLiCHEMBL5739.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP02699.
SwissPalmiP02699.
UniCarbKBiP02699.

Proteomic databases

PaxDbiP02699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneIDi509933.
KEGGibta:509933.

Organism-specific databases

CTDi6010.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118977.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiP02699.
KOiK04250.
OMAiLAAYMFM.
OrthoDBiEOG091G0BDA.
TreeFamiTF324998.

Enzyme and pathway databases

ReactomeiR-BTA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-418594. G alpha (i) signalling events.
R-BTA-419771. Opsins.
R-BTA-5620916. VxPx cargo-targeting to cilium.

Miscellaneous databases

EvolutionaryTraceiP02699.
PROiP02699.

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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
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_BOVIN
AccessioniPrimary (citable) accession number: P02699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 176 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.