P02699 · OPSD_BOVIN
- ProteinRhodopsin
- GeneRHO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids348 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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:11972040, PubMed:12044163, PubMed:16586416, PubMed:16908857, 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).
Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins (PubMed:10926528, PubMed:11972040, PubMed:12044163, PubMed:16586416, PubMed:16908857, 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).
Features
Showing features for site, binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameRhodopsin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP02699
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-36 | Extracellular | ||||
Sequence: MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQ | ||||||
Transmembrane | 37-61 | Helical; Name=1 | ||||
Sequence: FSMLAAYMFLLIMLGFPINFLTLYV | ||||||
Topological domain | 62-73 | Cytoplasmic | ||||
Sequence: TVQHKKLRTPLN | ||||||
Transmembrane | 74-96 | Helical; Name=2 | ||||
Sequence: YILLNLAVADLFMVFGGFTTTLY | ||||||
Topological domain | 97-110 | Extracellular | ||||
Sequence: TSLHGYFVFGPTGC | ||||||
Transmembrane | 111-133 | Helical; Name=3 | ||||
Sequence: NLEGFFATLGGEIALWSLVVLAI | ||||||
Topological domain | 134-152 | Cytoplasmic | ||||
Sequence: ERYVVVCKPMSNFRFGENH | ||||||
Transmembrane | 153-173 | Helical; Name=4 | ||||
Sequence: AIMGVAFTWVMALACAAPPLV | ||||||
Topological domain | 174-202 | Extracellular | ||||
Sequence: GWSRYIPEGMQCSCGIDYYTPHEETNNES | ||||||
Transmembrane | 203-224 | Helical; Name=5 | ||||
Sequence: FVIYMFVVHFIIPLIVIFFCYG | ||||||
Topological domain | 225-252 | Cytoplasmic | ||||
Sequence: QLVFTVKEAAAQQQESATTQKAEKEVTR | ||||||
Transmembrane | 253-274 | Helical; Name=6 | ||||
Sequence: MVIIMVIAFLICWLPYAGVAFY | ||||||
Topological domain | 275-286 | Extracellular | ||||
Sequence: IFTHQGSDFGPI | ||||||
Transmembrane | 287-308 | Helical; Name=7 | ||||
Sequence: FMTIPAFFAKTSAVYNPVIYIM | ||||||
Topological domain | 309-348 | Cytoplasmic | ||||
Sequence: MNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. | ||||
Sequence: N → C | ||||||
Mutagenesis | 15 | Normal light absorption; when associated with C-2 and C-282. | ||||
Sequence: N → D | ||||||
Mutagenesis | 90 | Increased thermal stability and decreased retinal uptake. Decreases stability of the inactive conformation. | ||||
Sequence: G → D | ||||||
Mutagenesis | 94 | Stabilizes the activated conformation and hinders hydrolysis of the covalent bond that retains all-trans-retinol. | ||||
Sequence: T → I | ||||||
Mutagenesis | 113 | Causes shift to the activated conformation. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 257 | Causes shift to the activated conformation. | ||||
Sequence: M → Y | ||||||
Mutagenesis | 282 | Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. | ||||
Sequence: D → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 55 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation, disulfide bond, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000197653 | 1-348 | Rhodopsin | |||
Sequence: MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA | ||||||
Glycosylation | 2 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 15 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 110↔187 | |||||
Sequence: CNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSC | ||||||
Modified residue | 296 | N6-(retinylidene)lysine | ||||
Sequence: K | ||||||
Lipidation | 322 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 323 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 335 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 336 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 338 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 340 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 342 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 343 | Phosphoserine; by RK and GRK7 | ||||
Sequence: S |
Post-translational modification
Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in rod-shaped photoreceptor cells in the retina that mediate vision in dim light (at protein level).
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:18563085, PubMed:23303210).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884).
Interacts with GRK1 (By similarity).
Interacts (phosphorylated form) with SAG (PubMed:15111114, PubMed:15351781, PubMed:23579341, PubMed:25205354, PubMed:26200343).
Interacts with GNAT1 (PubMed:18818650, PubMed:21389983, PubMed:23303210, PubMed:23579341, PubMed:26526852, PubMed:28655769).
Interacts with GNAT3 (PubMed:22198838, PubMed:27458239).
SAG and G-proteins compete for a common binding site (By similarity).
Interacts with PRCD; the interaction promotes PRCD stability (PubMed:27509380).
Forms a complex with ASAP1 and ARF4 (PubMed:25673879).
Forms a complex with ASAP1, RAB11A, Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia rhodopsin/RHO transport in photoreceptors (PubMed:25673879).
May form a complex composed of RHO, GRK1 and RCVRN in a Ca2+-dependent manner; RCVRN prevents the interaction between GRK1 and RHO (PubMed:17020884).
Interacts with GRK1 (By similarity).
Interacts (phosphorylated form) with SAG (PubMed:15111114, PubMed:15351781, PubMed:23579341, PubMed:25205354, PubMed:26200343).
Interacts with GNAT1 (PubMed:18818650, PubMed:21389983, PubMed:23303210, PubMed:23579341, PubMed:26526852, PubMed:28655769).
Interacts with GNAT3 (PubMed:22198838, PubMed:27458239).
SAG and G-proteins compete for a common binding site (By similarity).
Interacts with PRCD; the interaction promotes PRCD stability (PubMed:27509380).
Forms a complex with ASAP1 and ARF4 (PubMed:25673879).
Forms a complex with ASAP1, RAB11A, Rabin8/RAB3IP, ARF4 and RAB11FIP3; the complex regulates Golgi-to-cilia rhodopsin/RHO transport in photoreceptors (PubMed:25673879).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P02699 | GNAT1 P04695 | 3 | EBI-8592832, EBI-7052221 | |
BINARY | P02699 | RHO P02699 | 6 | EBI-8592832, EBI-8592832 | |
BINARY | P02699 | SAG P08168-1 | 23 | EBI-8592832, EBI-15575296 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 134-136 | 'Ionic lock' involved in activated form stabilization | ||||
Sequence: ERY | ||||||
Region | 330-348 | Interaction with SAG | ||||
Sequence: DDEASTTVSKTETSQVAPA |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Length348
- Mass (Da)39,008
- Last updated1986-07-21 v1
- Checksum33FDA196803E81F3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 281 | in Ref. 3; AAA30675 | ||||
Sequence: S → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
K00506 EMBL· GenBank· DDBJ | AAA30674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00502 EMBL· GenBank· DDBJ | AAA30674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00503 EMBL· GenBank· DDBJ | AAA30674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00504 EMBL· GenBank· DDBJ | AAA30674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K00505 EMBL· GenBank· DDBJ | AAA30674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21606 EMBL· GenBank· DDBJ | AAA30675.1 EMBL· GenBank· DDBJ | mRNA |