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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011ZincCombined sources2 Publications
Binding sitei265 – 2651Retinal chromophore3 Publications
Metal bindingi279 – 2791ZincCombined sources2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636ExtracellularAdd
BLAST
Transmembranei37 – 6327Helical; Name=1Add
BLAST
Topological domaini64 – 7310Cytoplasmic
Transmembranei74 – 9623Helical; Name=2Add
BLAST
Topological domaini97 – 11014ExtracellularAdd
BLAST
Transmembranei111 – 13323Helical; Name=3Add
BLAST
Topological domaini134 – 15219CytoplasmicAdd
BLAST
Transmembranei153 – 17321Helical; Name=4Add
BLAST
Topological domaini174 – 20229ExtracellularAdd
BLAST
Transmembranei203 – 22422Helical; Name=5Add
BLAST
Topological domaini225 – 24925CytoplasmicAdd
BLAST
Transmembranei250 – 27425Helical; Name=6Add
BLAST
Topological domaini275 – 28612ExtracellularAdd
BLAST
Transmembranei287 – 30822Helical; Name=7Add
BLAST
Topological domaini309 – 34840CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21N → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. 1 Publication
Mutagenesisi15 – 151N → D: Normal light absorption; when associated with C-2 and C-282. 1 Publication
Mutagenesisi282 – 2821D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. 1 Publication

Chemistry

ChEMBLiCHEMBL5739.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348RhodopsinPRO_0000197653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Glycosylationi2 – 21N-linked (GlcNAc...)3 Publications
Glycosylationi15 – 151N-linked (GlcNAc...)3 Publications
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation1 Publication
Modified residuei296 – 2961N6-(retinylidene)lysine
Lipidationi322 – 3221S-palmitoyl cysteine3 Publications
Lipidationi323 – 3231S-palmitoyl cysteine3 Publications
Modified residuei334 – 3341Phosphoserine2 Publications
Modified residuei335 – 3351Phosphothreonine2 Publications
Modified residuei336 – 3361Phosphothreonine2 Publications
Modified residuei338 – 3381Phosphoserine2 Publications
Modified residuei340 – 3401Phosphothreonine2 Publications
Modified residuei342 – 3421Phosphothreonine2 Publications
Modified residuei343 – 3431Phosphoserine; by RK and GRK73 Publications

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 interactions.
DIPiDIP-29225N.
IntActiP02699. 4 interactions.
MINTiMINT-1507462.
STRINGi9913.ENSBTAP00000001730.

Chemistry

BindingDBiP02699.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi10 – 134Combined sources
Helixi15 – 173Combined sources
Turni23 – 253Combined sources
Turni29 – 313Combined sources
Helixi34 – 6431Combined sources
Helixi66 – 683Combined sources
Helixi71 – 8919Combined sources
Helixi91 – 10010Combined sources
Helixi103 – 1053Combined sources
Helixi106 – 13934Combined sources
Beta strandi143 – 1453Combined sources
Helixi150 – 16819Combined sources
Helixi170 – 1723Combined sources
Turni175 – 1773Combined sources
Beta strandi179 – 1813Combined sources
Turni182 – 1854Combined sources
Beta strandi186 – 1883Combined sources
Helixi192 – 1954Combined sources
Helixi196 – 1983Combined sources
Helixi200 – 21011Combined sources
Helixi213 – 22311Combined sources
Turni224 – 2285Combined sources
Turni229 – 2313Combined sources
Turni235 – 2384Combined sources
Beta strandi239 – 2413Combined sources
Helixi242 – 27736Combined sources
Turni278 – 2803Combined sources
Helixi285 – 29410Combined sources
Helixi295 – 2995Combined sources
Helixi301 – 3088Combined sources
Helixi311 – 32111Combined sources
Turni322 – 3243Combined sources
Turni328 – 3303Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi339 – 3424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00271.
ProteinModelPortaliP02699.
SMRiP02699. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02699.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 12513Retinal chromophore bindingAdd
BLAST
Regioni207 – 2126Retinal chromophore binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi134 – 1374'Ionic lock' involved in activated form stabilization

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811S → F in AAA30675 (PubMed:2950966).Curated

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
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[»]
DisProtiDP00271.
ProteinModelPortaliP02699.
SMRiP02699. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

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: September 7, 2016
This is version 174 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.