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Protein

Rhodopsin

Gene

RHO

Organism
Homo sapiens (Human)
Status
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 (PubMed:8107847, PubMed:7846071). Required for photoreceptor cell viability after birth (PubMed:2215617, PubMed:12566452). Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins (PubMed:8107847, PubMed:28524165, PubMed:26200343, PubMed:28753425). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:28524165, PubMed:26200343).1 Publication6 Publications

Sites

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 conformation1 Publication1
<p>This subsection of the ‘Function’ 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 bindingi201ZincBy similarity1
Metal bindingi279ZincBy similarity1

<p>The <a href="http://www.geneontology.org/">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="http://www.uniprot.org/keywords">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

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Reactomei
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-2485179 Activation of the phototransduction cascade
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-418594 G alpha (i) signalling events
R-HSA-419771 Opsins
R-HSA-5620916 VxPx cargo-targeting to cilium

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P08100

SIGNOR Signaling Network Open Resource

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SIGNORi
P08100

Protein family/group databases

Transport Classification Database

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TCDBi
9.A.14.1.2 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="http://www.uniprot.org/help/names_and_taxonomy_section">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:
Rhodopsin
Alternative name(s):
Opsin-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Name:RHO
Synonyms:OPN2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000163914.4

Human Gene Nomenclature Database

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HGNCi
HGNC:10012 RHO

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180380 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P08100

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 36Extracellular2 PublicationsAdd BLAST36
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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=12 PublicationsAdd BLAST25
Topological domaini62 – 73Cytoplasmic2 PublicationsAdd BLAST12
Transmembranei74 – 96Helical; Name=22 PublicationsAdd BLAST23
Topological domaini97 – 110Extracellular2 PublicationsAdd BLAST14
Transmembranei111 – 133Helical; Name=32 PublicationsAdd BLAST23
Topological domaini134 – 152Cytoplasmic2 PublicationsAdd BLAST19
Transmembranei153 – 173Helical; Name=42 PublicationsAdd BLAST21
Topological domaini174 – 202Extracellular2 PublicationsAdd BLAST29
Transmembranei203 – 224Helical; Name=52 PublicationsAdd BLAST22
Topological domaini225 – 252Cytoplasmic2 PublicationsAdd BLAST28
Transmembranei253 – 274Helical; Name=62 PublicationsAdd BLAST22
Topological domaini275 – 284Extracellular2 Publications10
Transmembranei285 – 309Helical; Name=72 PublicationsAdd BLAST25
Topological domaini310 – 348Cytoplasmic2 PublicationsAdd BLAST39

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Retinitis pigmentosa 4 (RP4)26 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:613731
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0047654T → K in RP4. 1
Natural variantiVAR_00476615N → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893786EnsemblClinVar.1
Natural variantiVAR_00476717T → M in RP4. 2 PublicationsCorresponds to variant dbSNP:rs104893769EnsemblClinVar.1
Natural variantiVAR_00476823P → H in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system. 5 PublicationsCorresponds to variant dbSNP:rs104893768EnsemblClinVar.1
Natural variantiVAR_00476923P → L in RP4. 1
Natural variantiVAR_00477028Q → H in RP4. 1
Natural variantiVAR_00477140L → R in RP4. 1 Publication1
Natural variantiVAR_00477244M → T in RP4. 1 PublicationCorresponds to variant dbSNP:rs774336493Ensembl.1
Natural variantiVAR_00477345F → L in RP4. Corresponds to variant dbSNP:rs104893770EnsemblClinVar.1
Natural variantiVAR_00477446L → R in RP4. 1
Natural variantiVAR_00477651G → R in RP4. Corresponds to variant dbSNP:rs104893792EnsemblClinVar.1
Natural variantiVAR_00477751G → V in RP4. 1
Natural variantiVAR_00477853P → R in RP4. Corresponds to variant dbSNP:rs28933395EnsemblClinVar.1
Natural variantiVAR_00477958T → R in RP4. 2 PublicationsCorresponds to variant dbSNP:rs28933394EnsemblClinVar.1
Natural variantiVAR_00478068 – 71Missing in RP4. 4
Natural variantiVAR_00478187V → D in RP4. Corresponds to variant dbSNP:rs104893771EnsemblClinVar.1
Natural variantiVAR_00478289G → D in RP4. Corresponds to variant dbSNP:rs104893772EnsemblClinVar.1
Natural variantiVAR_004786106G → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893773EnsemblClinVar.1
Natural variantiVAR_004787106G → W in RP4. Corresponds to variant dbSNP:rs104893773EnsemblClinVar.1
Natural variantiVAR_004788109G → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs1415160298Ensembl.1
Natural variantiVAR_004789110C → F in RP4. 1 Publication1
Natural variantiVAR_004790110C → Y in RP4. Corresponds to variant dbSNP:rs104893787EnsemblClinVar.1
Natural variantiVAR_004791114G → D in RP4. Corresponds to variant dbSNP:rs104893788EnsemblClinVar.1
Natural variantiVAR_004792125L → R in RP4. 1
Natural variantiVAR_004793127S → F in RP4. 1 Publication1
Natural variantiVAR_004794131L → P in RP4. 2 Publications1
Natural variantiVAR_004795135R → G in RP4. 1 Publication1
Natural variantiVAR_004796135R → L in RP4. Corresponds to variant dbSNP:rs104893774EnsemblClinVar.1
Natural variantiVAR_004797135R → W in RP4. 2 PublicationsCorresponds to variant dbSNP:rs104893775EnsemblClinVar.1
Natural variantiVAR_004798140C → S in RP4. 1 Publication1
Natural variantiVAR_004799150E → K in RP4; autosomal recessive. 2 PublicationsCorresponds to variant dbSNP:rs104893791EnsemblClinVar.1
Natural variantiVAR_004800164A → E in RP4. Corresponds to variant dbSNP:rs104893793EnsemblClinVar.1
Natural variantiVAR_004801164A → V in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893793EnsemblClinVar.1
Natural variantiVAR_004802167C → R in RP4. 1
Natural variantiVAR_004803171P → L in RP4. 1
Natural variantiVAR_004804171P → Q in RP4. 1 Publication1
Natural variantiVAR_004805171P → S in RP4. Corresponds to variant dbSNP:rs104893794EnsemblClinVar.1
Natural variantiVAR_004806178Y → C in RP4. Corresponds to variant dbSNP:rs104893776EnsemblClinVar.1
Natural variantiVAR_004807178Y → N in RP4. 1 Publication1
Natural variantiVAR_068359180P → S in RP4. 1 Publication1
Natural variantiVAR_004808181E → K in RP4. Corresponds to variant dbSNP:rs775557680EnsemblClinVar.1
Natural variantiVAR_004809182G → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893780EnsemblClinVar.1
Natural variantiVAR_004810186S → P in RP4. 1
Natural variantiVAR_004811188G → E in RP4. 1 PublicationCorresponds to variant dbSNP:rs1424131846Ensembl.1
Natural variantiVAR_004812188G → R in RP4. Corresponds to variant dbSNP:rs527236100EnsemblClinVar.1
Natural variantiVAR_004814190D → G in RP4. Corresponds to variant dbSNP:rs104893777EnsemblClinVar.1
Natural variantiVAR_004813190D → N in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar.1
Natural variantiVAR_004815190D → Y in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar.1
Natural variantiVAR_004816207M → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893782EnsemblClinVar.1
Natural variantiVAR_004818211H → P in RP4. Corresponds to variant dbSNP:rs28933993EnsemblClinVar.1
Natural variantiVAR_004819211H → R in RP4. 1 Publication1
Natural variantiVAR_068360214I → N in RP4. 1 Publication1
Natural variantiVAR_004820216M → K in RP4. 1 Publication1
Natural variantiVAR_004821220F → C in RP4. Corresponds to variant dbSNP:rs766161322Ensembl.1
Natural variantiVAR_004822222C → R in RP4. 1
Natural variantiVAR_004823255Missing in RP4. 1 Publication1
Natural variantiVAR_004824264Missing in RP4. 1
Natural variantiVAR_004825267P → L in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893781EnsemblClinVar.1
Natural variantiVAR_004826267P → R in RP4. 1 Publication1
Natural variantiVAR_004828296K → E in RP4. Corresponds to variant dbSNP:rs29001653EnsemblClinVar.1
Natural variantiVAR_004829297S → R in RP4. 1 Publication1
Natural variantiVAR_004830342T → M in RP4. Corresponds to variant dbSNP:rs183318466Ensembl.1
Natural variantiVAR_004831345V → L in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893795EnsemblClinVar.1
Natural variantiVAR_004832345V → M in RP4. Corresponds to variant dbSNP:rs104893795EnsemblClinVar.1
Natural variantiVAR_004833347P → A in RP4. 1 Publication1
Natural variantiVAR_004834347P → L in RP4; common variant. 2 PublicationsCorresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004835347P → Q in RP4. Corresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004836347P → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004837347P → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs29001637EnsemblClinVar.1
Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia.
See also OMIM:610445
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00478390G → D in CSNBAD1; constitutive activity in the absence of bound retinal. 2 PublicationsCorresponds to variant dbSNP:rs104893790EnsemblClinVar.1
Natural variantiVAR_00478494T → I in CSNBAD1. 1 PublicationCorresponds to variant dbSNP:rs104893796EnsemblClinVar.1
Natural variantiVAR_004827292A → E in CSNBAD1. 1 PublicationCorresponds to variant dbSNP:rs104893789EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi113E → Q: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Y-257. 1 Publication1
Mutagenesisi257M → Y: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Q-113. 2 Publications1
Mutagenesisi336 – 340TVSKT → AVAKA: Loss of phosphorylation sites and decreased interaction with SAG. 1 Publication5
Mutagenesisi336 – 338TVS → AVA: Loss of phosphorylation sites and decreased interaction with SAG; when associated with A-343. 1 Publication3
Mutagenesisi343S → A: Loss of phosphorylation sites and decreased interaction with SAG; when associated with 336-A--A-338. 1 Publication1

Keywords - Diseasei

Congenital stationary night blindness, Disease mutation, Retinitis pigmentosa

Organism-specific databases

DisGeNET

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DisGeNETi
6010

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
RHO

MalaCards human disease database

More...
MalaCardsi
RHO
MIMi610445 phenotype
613731 phenotype

Open Targets

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OpenTargetsi
ENSG00000163914

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
215 Congenital stationary night blindness
791 Retinitis pigmentosa
52427 Retinitis punctata albescens

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34390

Chemistry databases

Drug and drug target database

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DrugBanki
DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane
DB03152 B-2-Octylglucoside
DB01159 Halothane
DB04450 Heptyl 1-Thiohexopyranoside
DB03381 Hexadecanal
DB04147 Lauryl Dimethylamine-N-Oxide
DB01646 N-Acetylmethionine
DB03796 Palmitic Acid
DB04522 Phosphonoserine
DB02482 Phosphonothreonine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RHO

Domain mapping of disease mutations (DMDM)

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DMDMi
129207

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001976771 – 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="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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...) asparagineBy similarity1
Glycosylationi15N-linked (GlcNAc...) asparagine1 Publication1
<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 annotation2 Publications
Modified residuei296N6-(retinylidene)lysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 cysteineBy similarity1
Lipidationi323S-palmitoyl cysteineBy similarity1
Modified residuei334Phosphoserine1 Publication1
Modified residuei336Phosphothreonine1 Publication1
Modified residuei338Phosphoserine1 Publication1
Modified residuei340PhosphothreonineBy similarity1
Modified residuei342PhosphothreonineBy similarity1
Modified residuei343PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 (By similarity). After activation by light, phosphorylated by GRK1 (in vitro) (PubMed:28524165).By similarity1 Publication
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(PubMed:12566452).1 Publication

Keywords - PTMi

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

Proteomic databases

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

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PaxDbi
P08100

PeptideAtlas

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PeptideAtlasi
P08100

PRoteomics IDEntifications database

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PRIDEi
P08100

ProteomicsDB human proteome resource

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ProteomicsDBi
52066

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
525

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08100

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P08100

SwissPalm database of S-palmitoylation events

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SwissPalmi
P08100

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P08100

<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="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Rod shaped photoreceptor cells which mediate vision in dim light.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000163914 Expressed in 87 organ(s), highest expression level in retina

CleanEx database of gene expression profiles

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CleanExi
HS_RHO

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08100 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022486
CAB034887
CAB034888
HPA013440

<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="http://www.uniprot.org/help/interaction_section">'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="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Interacts (phosphorylated form) with SAG (PubMed:28524165, PubMed:26200343, PubMed:28753425). Interacts with GNAT1 (PubMed:26200343). Interacts with GNAT3. SAG and G-proteins compete for a common binding site (By similarity). Interacts with GRK1 (PubMed:28524165).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ZFYVE9O954052EBI-1394177,EBI-296817

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111942, 11 interactors

Protein interaction database and analysis system

More...
IntActi
P08100, 4 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000296271

<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

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWJX-ray3.30A/B/C/D1-348[»]
5DGYX-ray7.70A/B/C/D1-348[»]
5W0PX-ray3.01A/B/C/D1-348[»]
6CMOelectron microscopy4.50R3-323[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P08100

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

More...
SMRi
P08100

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Region

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 SAG2 PublicationsAdd BLAST19

Motif

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 stabilization1 Publication3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3656 Eukaryota
ENOG410XRW9 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154379

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000253932

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG107442

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08100

KEGG Orthology (KO)

More...
KOi
K04250

Identification of Orthologs from Complete Genome Data

More...
OMAi
LAAYMFM

Database of Orthologous Groups

More...
OrthoDBi
541116at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P08100

TreeFam database of animal gene trees

More...
TreeFami
TF324998

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR001760 Opsin
IPR027430 Retinal_BS
IPR000732 Rhodopsin
IPR019477 Rhodopsin_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00001 7tm_1, 1 hit
PF10413 Rhodopsin_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00237 GPCRRHODOPSN
PR00238 OPSIN
PR00579 RHODOPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit
PS00238 OPSIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P08100-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL
60 70 80 90 100
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH
110 120 130 140 150
GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE
160 170 180 190 200
NHAIMGVAFT WVMALACAAP PLAGWSRYIP EGLQCSCGID YYTLKPEVNN
210 220 230 240 250
ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
260 270 280 290 300
TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
310 320 330 340
YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
Length:348
Mass (Da):38,893
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6F4F6FCBA34265B2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0047654T → K in RP4. 1
Natural variantiVAR_00476615N → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893786EnsemblClinVar.1
Natural variantiVAR_00476717T → M in RP4. 2 PublicationsCorresponds to variant dbSNP:rs104893769EnsemblClinVar.1
Natural variantiVAR_00476823P → H in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system. 5 PublicationsCorresponds to variant dbSNP:rs104893768EnsemblClinVar.1
Natural variantiVAR_00476923P → L in RP4. 1
Natural variantiVAR_00477028Q → H in RP4. 1
Natural variantiVAR_00477140L → R in RP4. 1 Publication1
Natural variantiVAR_00477244M → T in RP4. 1 PublicationCorresponds to variant dbSNP:rs774336493Ensembl.1
Natural variantiVAR_00477345F → L in RP4. Corresponds to variant dbSNP:rs104893770EnsemblClinVar.1
Natural variantiVAR_00477446L → R in RP4. 1
Natural variantiVAR_00477551G → A1 PublicationCorresponds to variant dbSNP:rs149079952EnsemblClinVar.1
Natural variantiVAR_00477651G → R in RP4. Corresponds to variant dbSNP:rs104893792EnsemblClinVar.1
Natural variantiVAR_00477751G → V in RP4. 1
Natural variantiVAR_00477853P → R in RP4. Corresponds to variant dbSNP:rs28933395EnsemblClinVar.1
Natural variantiVAR_00477958T → R in RP4. 2 PublicationsCorresponds to variant dbSNP:rs28933394EnsemblClinVar.1
Natural variantiVAR_00478068 – 71Missing in RP4. 4
Natural variantiVAR_00478187V → D in RP4. Corresponds to variant dbSNP:rs104893771EnsemblClinVar.1
Natural variantiVAR_00478289G → D in RP4. Corresponds to variant dbSNP:rs104893772EnsemblClinVar.1
Natural variantiVAR_00478390G → D in CSNBAD1; constitutive activity in the absence of bound retinal. 2 PublicationsCorresponds to variant dbSNP:rs104893790EnsemblClinVar.1
Natural variantiVAR_00478494T → I in CSNBAD1. 1 PublicationCorresponds to variant dbSNP:rs104893796EnsemblClinVar.1
Natural variantiVAR_004785104V → I Found in patients with pathologic myopia; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs144317206Ensembl.1
Natural variantiVAR_004786106G → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893773EnsemblClinVar.1
Natural variantiVAR_004787106G → W in RP4. Corresponds to variant dbSNP:rs104893773EnsemblClinVar.1
Natural variantiVAR_004788109G → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs1415160298Ensembl.1
Natural variantiVAR_004789110C → F in RP4. 1 Publication1
Natural variantiVAR_004790110C → Y in RP4. Corresponds to variant dbSNP:rs104893787EnsemblClinVar.1
Natural variantiVAR_004791114G → D in RP4. Corresponds to variant dbSNP:rs104893788EnsemblClinVar.1
Natural variantiVAR_004792125L → R in RP4. 1
Natural variantiVAR_004793127S → F in RP4. 1 Publication1
Natural variantiVAR_004794131L → P in RP4. 2 Publications1
Natural variantiVAR_004795135R → G in RP4. 1 Publication1
Natural variantiVAR_004796135R → L in RP4. Corresponds to variant dbSNP:rs104893774EnsemblClinVar.1
Natural variantiVAR_004797135R → W in RP4. 2 PublicationsCorresponds to variant dbSNP:rs104893775EnsemblClinVar.1
Natural variantiVAR_004798140C → S in RP4. 1 Publication1
Natural variantiVAR_004799150E → K in RP4; autosomal recessive. 2 PublicationsCorresponds to variant dbSNP:rs104893791EnsemblClinVar.1
Natural variantiVAR_004800164A → E in RP4. Corresponds to variant dbSNP:rs104893793EnsemblClinVar.1
Natural variantiVAR_004801164A → V in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893793EnsemblClinVar.1
Natural variantiVAR_004802167C → R in RP4. 1
Natural variantiVAR_004803171P → L in RP4. 1
Natural variantiVAR_004804171P → Q in RP4. 1 Publication1
Natural variantiVAR_004805171P → S in RP4. Corresponds to variant dbSNP:rs104893794EnsemblClinVar.1
Natural variantiVAR_004806178Y → C in RP4. Corresponds to variant dbSNP:rs104893776EnsemblClinVar.1
Natural variantiVAR_004807178Y → N in RP4. 1 Publication1
Natural variantiVAR_068359180P → S in RP4. 1 Publication1
Natural variantiVAR_004808181E → K in RP4. Corresponds to variant dbSNP:rs775557680EnsemblClinVar.1
Natural variantiVAR_004809182G → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893780EnsemblClinVar.1
Natural variantiVAR_004810186S → P in RP4. 1
Natural variantiVAR_004811188G → E in RP4. 1 PublicationCorresponds to variant dbSNP:rs1424131846Ensembl.1
Natural variantiVAR_004812188G → R in RP4. Corresponds to variant dbSNP:rs527236100EnsemblClinVar.1
Natural variantiVAR_004814190D → G in RP4. Corresponds to variant dbSNP:rs104893777EnsemblClinVar.1
Natural variantiVAR_004813190D → N in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar.1
Natural variantiVAR_004815190D → Y in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar.1
Natural variantiVAR_004816207M → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893782EnsemblClinVar.1
Natural variantiVAR_004817209V → M Found in a patient with retinitis pigmentosa; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs567288669Ensembl.1
Natural variantiVAR_004818211H → P in RP4. Corresponds to variant dbSNP:rs28933993EnsemblClinVar.1
Natural variantiVAR_004819211H → R in RP4. 1 Publication1
Natural variantiVAR_068360214I → N in RP4. 1 Publication1
Natural variantiVAR_004820216M → K in RP4. 1 Publication1
Natural variantiVAR_004821220F → C in RP4. Corresponds to variant dbSNP:rs766161322Ensembl.1
Natural variantiVAR_004822222C → R in RP4. 1
Natural variantiVAR_004823255Missing in RP4. 1 Publication1
Natural variantiVAR_004824264Missing in RP4. 1
Natural variantiVAR_004825267P → L in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893781EnsemblClinVar.1
Natural variantiVAR_004826267P → R in RP4. 1 Publication1
Natural variantiVAR_004827292A → E in CSNBAD1. 1 PublicationCorresponds to variant dbSNP:rs104893789EnsemblClinVar.1
Natural variantiVAR_004828296K → E in RP4. Corresponds to variant dbSNP:rs29001653EnsemblClinVar.1
Natural variantiVAR_004829297S → R in RP4. 1 Publication1
Natural variantiVAR_004830342T → M in RP4. Corresponds to variant dbSNP:rs183318466Ensembl.1
Natural variantiVAR_004831345V → L in RP4. 1 PublicationCorresponds to variant dbSNP:rs104893795EnsemblClinVar.1
Natural variantiVAR_004832345V → M in RP4. Corresponds to variant dbSNP:rs104893795EnsemblClinVar.1
Natural variantiVAR_004833347P → A in RP4. 1 Publication1
Natural variantiVAR_004834347P → L in RP4; common variant. 2 PublicationsCorresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004835347P → Q in RP4. Corresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004836347P → R in RP4. 1 PublicationCorresponds to variant dbSNP:rs29001566EnsemblClinVar.1
Natural variantiVAR_004837347P → S in RP4. 1 PublicationCorresponds to variant dbSNP:rs29001637EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U49742 Genomic DNA Translation: AAC31763.1
AB065668 Genomic DNA Translation: BAC05894.1
BX537381 mRNA Translation: CAD97623.1
BC112104 mRNA Translation: AAI12105.1
BC112106 mRNA Translation: AAI12107.1
U16824 Genomic DNA Translation: AAA97436.1
S81166 Genomic DNA Translation: AAB35906.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3063.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41200 OOHU

NCBI Reference Sequences

More...
RefSeqi
NP_000530.1, NM_000539.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.247565

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000296271; ENSP00000296271; ENSG00000163914

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6010

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6010

UCSC genome browser

More...
UCSCi
uc003emt.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Mutations of the RHO gene

Retina International's Scientific Newsletter

Wikipedia

Rhodopsin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49742 Genomic DNA Translation: AAC31763.1
AB065668 Genomic DNA Translation: BAC05894.1
BX537381 mRNA Translation: CAD97623.1
BC112104 mRNA Translation: AAI12105.1
BC112106 mRNA Translation: AAI12107.1
U16824 Genomic DNA Translation: AAA97436.1
S81166 Genomic DNA Translation: AAB35906.1
CCDSiCCDS3063.1
PIRiA41200 OOHU
RefSeqiNP_000530.1, NM_000539.3
UniGeneiHs.247565

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWJX-ray3.30A/B/C/D1-348[»]
5DGYX-ray7.70A/B/C/D1-348[»]
5W0PX-ray3.01A/B/C/D1-348[»]
6CMOelectron microscopy4.50R3-323[»]
ProteinModelPortaliP08100
SMRiP08100
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111942, 11 interactors
IntActiP08100, 4 interactors
STRINGi9606.ENSP00000296271

Chemistry databases

DrugBankiDB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane
DB03152 B-2-Octylglucoside
DB01159 Halothane
DB04450 Heptyl 1-Thiohexopyranoside
DB03381 Hexadecanal
DB04147 Lauryl Dimethylamine-N-Oxide
DB01646 N-Acetylmethionine
DB03796 Palmitic Acid
DB04522 Phosphonoserine
DB02482 Phosphonothreonine

Protein family/group databases

TCDBi9.A.14.1.2 the g-protein-coupled receptor (gpcr) family

Information system for G protein-coupled receptors (GPCRs)

More...
GPCRDBi
Search...

PTM databases

GlyConnecti525
iPTMnetiP08100
PhosphoSitePlusiP08100
SwissPalmiP08100
UniCarbKBiP08100

Polymorphism and mutation databases

BioMutaiRHO
DMDMi129207

Proteomic databases

PaxDbiP08100
PeptideAtlasiP08100
PRIDEiP08100
ProteomicsDBi52066

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6010
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296271; ENSP00000296271; ENSG00000163914
GeneIDi6010
KEGGihsa:6010
UCSCiuc003emt.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6010
DisGeNETi6010
EuPathDBiHostDB:ENSG00000163914.4

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RHO
GeneReviewsiRHO
HGNCiHGNC:10012 RHO
HPAiCAB022486
CAB034887
CAB034888
HPA013440
MalaCardsiRHO
MIMi180380 gene
610445 phenotype
613731 phenotype
neXtProtiNX_P08100
OpenTargetsiENSG00000163914
Orphaneti215 Congenital stationary night blindness
791 Retinitis pigmentosa
52427 Retinitis punctata albescens
PharmGKBiPA34390

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00940000154379
HOGENOMiHOG000253932
HOVERGENiHBG107442
InParanoidiP08100
KOiK04250
OMAiLAAYMFM
OrthoDBi541116at2759
PhylomeDBiP08100
TreeFamiTF324998

Enzyme and pathway databases

ReactomeiR-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-2485179 Activation of the phototransduction cascade
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-418594 G alpha (i) signalling events
R-HSA-419771 Opsins
R-HSA-5620916 VxPx cargo-targeting to cilium
SignaLinkiP08100
SIGNORiP08100

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RHO human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Rhodopsin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6010

Protein Ontology

More...
PROi
PR:P08100

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000163914 Expressed in 87 organ(s), highest expression level in retina
CleanExiHS_RHO
GenevisibleiP08100 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOPSD_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08100
Secondary accession number(s): Q16414, Q2M249
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 16, 2019
This is version 210 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  7. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
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