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Protein

Rhodopsin

Gene

RHO

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins (PubMed:10926528, PubMed:12044163, PubMed:11972040, PubMed:16908857, PubMed:16586416, PubMed:17060607, PubMed:17449675, PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341, PubMed:25205354, PubMed:27458239). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:1396673, PubMed:15111114).By similarity5 Publications11 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei113Plays an important role in the conformation switch to the active conformation3 Publications1 Publication1
Metal bindingi201ZincCombined sources2 Publications1
Metal bindingi279ZincCombined sources2 Publications1

GO - Molecular functioni

  • 11-cis retinal binding Source: UniProtKB
  • arrestin family protein binding Source: CAFA
  • G-protein alpha-subunit binding Source: CAFA
  • G-protein coupled photoreceptor activity Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • opsin binding Source: CAFA
  • zinc ion binding Source: CAFA

GO - Biological processi

  • absorption of visible light Source: UniProtKB
  • photoreceptor cell maintenance Source: Ensembl
  • phototransduction, visible light Source: AgBase
  • protein-chromophore linkage Source: UniProtKB-KW
  • protein phosphorylation Source: Ensembl
  • response to light stimulus Source: CAFA
  • retina development in camera-type eye Source: Ensembl
  • rhodopsin mediated signaling pathway Source: UniProtKB
  • visual perception Source: UniProtKB-KW

Keywordsi

Molecular functionG-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer
Biological processSensory transduction, Vision
LigandChromophore, 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

Organism-specific databases

VGNCiVGNC:33942 RHO

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 36Extracellular20 PublicationsAdd BLAST36
Transmembranei37 – 61Helical; Name=120 PublicationsAdd BLAST25
Topological domaini62 – 73Cytoplasmic20 PublicationsAdd BLAST12
Transmembranei74 – 96Helical; Name=220 PublicationsAdd BLAST23
Topological domaini97 – 110Extracellular20 PublicationsAdd BLAST14
Transmembranei111 – 133Helical; Name=320 PublicationsAdd BLAST23
Topological domaini134 – 152Cytoplasmic20 PublicationsAdd BLAST19
Transmembranei153 – 173Helical; Name=420 PublicationsAdd BLAST21
Topological domaini174 – 202Extracellular20 PublicationsAdd BLAST29
Transmembranei203 – 224Helical; Name=520 PublicationsAdd BLAST22
Topological domaini225 – 252Cytoplasmic20 PublicationsAdd BLAST28
Transmembranei253 – 274Helical; Name=620 PublicationsAdd BLAST22
Topological domaini275 – 286Extracellular20 PublicationsAdd BLAST12
Transmembranei287 – 308Helical; Name=720 PublicationsAdd BLAST22
Topological domaini309 – 348Cytoplasmic20 PublicationsAdd BLAST40

Keywords - Cellular componenti

Cell projection, 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
Mutagenesisi90G → D: Increased thermal stability and decreased retinal uptake. Decreases stability of the inactive conformation. 1 Publication1
Mutagenesisi94T → I: Stabilizes the activated conformation and hinders hydrolysis of the covalent bond that retains all-trans-retinol. 1 Publication1
Mutagenesisi113E → Q: Causes shift to the activated conformation. 1 Publication1
Mutagenesisi257M → Y: Causes shift to the activated conformation. 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...) asparagineCombined sources8 Publications1
Glycosylationi15N-linked (GlcNAc...) asparagineCombined sources13 Publications1
Disulfide bondi110 ↔ 187PROSITE-ProRule annotationCombined sources12 Publications
Modified residuei296N6-(retinylidene)lysineCombined sources1 Publication13 Publications1
Lipidationi322S-palmitoyl cysteineCombined sources11 Publications1
Lipidationi323S-palmitoyl cysteineCombined sources13 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. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal.1 Publication14 Publications

Keywords - PTMi

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

Proteomic databases

PaxDbiP02699

PTM databases

GlyConnecti523
iPTMnetiP02699
SwissPalmiP02699
UniCarbKBiP02699

Expressioni

Tissue specificityi

Expressed in rod-shaped photoreceptor cells in the retina that mediate vision in dim light (at protein level).4 Publications

Gene expression databases

BgeeiENSBTAG00000001310

Interactioni

Subunit structurei

Homodimer (PubMed:23303210, PubMed:18563085). Interacts (phosphorylated form) with SAG (PubMed:26200343, PubMed:15111114, PubMed:15351781, PubMed:23579341, PubMed:25205354). Interacts with GNAT1 (PubMed:23303210, PubMed:28655769, PubMed:18818650, PubMed:21389983, PubMed:23579341, PubMed:26526852), Interacts with GNAT3 (PubMed:22198838, PubMed:27458239). SAG and G-proteins compete for a common binding site (PubMed:25205354). Interacts with GRK1 (By similarity).By similarity16 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • arrestin family protein binding Source: CAFA
  • G-protein alpha-subunit binding Source: CAFA
  • guanyl-nucleotide exchange factor activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • opsin binding Source: CAFA

Protein-protein interaction databases

BioGridi166570, 2 interactors
DIPiDIP-29225N
ELMiP02699
IntActiP02699, 5 interactors
MINTiP02699
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[»]
5TE3X-ray2.70A1-348[»]
5TE5X-ray4.01A1-348[»]
5WKTX-ray3.20A1-348[»]
6FK6X-ray2.36A1-326[»]
6FK7X-ray2.62A1-348[»]
6FK8X-ray2.87A1-348[»]
6FK9X-ray2.63A