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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

GO - Biological processi

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 Expressed in 1 organ(s), highest expression level in testis

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

GO - Molecular functioni

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

3D structure databases

DisProtiDP00271
ProteinModelPortaliP02699
SMRiP02699
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02699

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni330 – 348Interaction with SAG1 PublicationAdd BLAST19

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi134 – 136'Ionic lock' involved in activated form stabilization4 Publications3

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

InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR001760 Opsin
IPR027430 Retinal_BS
IPR000732 Rhodopsin
IPR019477 Rhodopsin_N
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PF10413 Rhodopsin_N, 1 hit
PRINTSiPR00237 GPCRRHODOPSN
PR00238 OPSIN
PR00579 RHODOPSIN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit
PS00238 OPSIN, 1 hit

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

Similar proteinsi

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[»]
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-ray2.63A1-348[»]
6FKAX-ray2.70A1-348[»]
6FKBX-ray3.03A1-328[»]
6FKCX-ray2.46A1-348[»]
6FKDX-ray2.49A1-348[»]
DisProtiDP00271
ProteinModelPortaliP02699
SMRiP02699
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi166570, 2 interactors
DIPiDIP-29225N
ELMiP02699
IntActiP02699, 5 interactors
MINTiP02699
STRINGi9913.ENSBTAP00000001730

Chemistry databases

BindingDBiP02699
ChEMBLiCHEMBL5739

Protein family/group databases

GPCRDBiSearch...

PTM databases

GlyConnecti523
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
VGNCiVGNC:33942 RHO

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
PROiPR:P02699