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Entry version 204 (17 Jun 2020)
Sequence version 1 (21 Jul 1986)
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Bos taurus (Bovine)
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei113Plays an important role in the conformation switch to the active conformation3 Publications1 Publication1
<p>This subsection of the <a href="">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi201ZincCombined sources2 Publications1
Metal bindingi279ZincCombined sources2 Publications1

<p>The <a href="">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

R-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

Protein family/group databases

Transport Classification Database

9.A.14.1.17 the g-protein-coupled receptor (gpcr) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
<p>This subsection of the <a href="">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
<p>This subsection of the <a href="">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Vertebrate Gene Nomenclature Database

VGNC:33942 RHO

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 36Extracellular20 PublicationsAdd BLAST36
<p>This subsection of the <a href="">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules


<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001976531 – 348RhodopsinAdd BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="">lipids</a>, <a href="">glycans</a> and <a href="">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine1 Publication1
<p>This subsection of the <a href="">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi2N-linked (GlcNAc...) asparagineCombined sources8 Publications1
Glycosylationi15N-linked (GlcNAc...) asparagineCombined sources13 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi110 ↔ 187PROSITE-ProRule annotationCombined sources12 Publications
Modified residuei296N6-(retinylidene)lysineCombined sources1 Publication13 Publications1
<p>This subsection of the <a href="">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>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

<p>This subsection of the <a href="">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life


PTM databases

GlyConnect protein glycosylation platform


iPTMnet integrated resource for PTMs in systems biology context


SwissPalm database of S-palmitoylation events


UniCarbKB; an annotated and curated database of glycan structures


<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="">P92958</a>, <a href="">Q8TDN4</a>, <a href="">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

ENSBTAG00000001310 Expressed in testis

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:23303210, PubMed:18563085). 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: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 (By similarity).

Interacts with PRCD; the interaction promotes PRCD stability (PubMed:27509380).

By similarity18 Publications

<p>This subsection of the '<a href="">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="">IntAct database</a>. It is updated at every <a href="">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

166570, 2 interactors

Database of interacting proteins


The Eukaryotic Linear Motif resource for Functional Sites in Proteins


Protein interaction database and analysis system

P02699, 5 interactors

Molecular INTeraction database


STRING: functional protein association networks


Chemistry databases

BindingDB database of measured binding affinities


<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models


Database of comparative protein structure models


Protein Data Bank in Europe - Knowledge Base


Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence


<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni330 – 348Interaction with SAG1 PublicationAdd BLAST19


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi134 – 136'Ionic lock' involved in activated form stabilization4 Publications