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UniProtKB - P15409 (OPSD_MOUSE)

Protein

Rhodopsin

Gene

Rho

Organism
Mus musculus (Mouse)
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. Required for photoreceptor cell viability after birth (PubMed:9020854). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:27353443).2 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 conformationBy similarity1
<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

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

<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
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:97914 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; 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 – 36ExtracellularCuratedAdd 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=1By similarityAdd BLAST25
Topological domaini62 – 73CytoplasmicCuratedAdd BLAST12
Transmembranei74 – 96Helical; Name=2By similarityAdd BLAST23
Topological domaini97 – 110ExtracellularCuratedAdd BLAST14
Transmembranei111 – 133Helical; Name=3By similarityAdd BLAST23
Topological domaini134 – 152CytoplasmicCuratedAdd BLAST19
Transmembranei153 – 173Helical; Name=4By similarityAdd BLAST21
Topological domaini174 – 202ExtracellularCuratedAdd BLAST29
Transmembranei203 – 224Helical; Name=5By similarityAdd BLAST22
Topological domaini225 – 252CytoplasmicCuratedAdd BLAST28
Transmembranei253 – 274Helical; Name=6By similarityAdd BLAST22
Topological domaini275 – 286ExtracellularCuratedAdd BLAST12
Transmembranei287 – 308Helical; Name=7By similarityAdd BLAST22
Topological domaini309 – 348CytoplasmicCuratedAdd 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice show no response in electroretinograms at low light intensity. They fail to form rod outer segments leading to degeneration of photoreceptor cells within 3 months of birth.1 Publication

<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_00001976871 – 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...) asparagineSequence analysis1
Glycosylationi15N-linked (GlcNAc...) asparagineSequence analysis1
<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 annotation
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 residuei336PhosphothreonineBy similarity1
Modified residuei338Phosphoserine1 Publication1
Modified residuei340PhosphothreonineBy similarity1
Modified residuei342PhosphothreonineBy similarity1
Modified residuei343Phosphoserine1 Publication1

<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.1 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.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15409

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

More...PaxDbi		P15409

PRoteomics IDEntifications database

More...PRIDEi		P15409

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15409

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

More...PhosphoSitePlusi		P15409

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P15409

<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 in the retina (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000030324 Expressed in 56 organ(s), highest expression level in retina

CleanEx database of gene expression profiles

More...CleanExi		MM_RHO

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P15409 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P15409 MM

<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. Interacts (phosphorylated form) with SAG. Interacts with GNAT1, Interacts with GNAT3. SAG and G-proteins compete for a common binding site. Interacts with GRK1 (By similarity).By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P15409, 2 interactors

Molecular INTeraction database

More...MINTi		P15409

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000032471

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P15409

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 SAGBy similarityAdd 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 stabilizationBy similarity3

<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		P15409

KEGG Orthology (KO)

More...KOi		K04250

Identification of Orthologs from Complete Genome Data

More...OMAi		LAAYMFM

Database of Orthologous Groups

More...OrthoDBi		EOG091G0BDA

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P15409-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNGTEGPNFY VPFSNVTGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL 
        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
NHAIMGVVFT WIMALACAAP PLVGWSRYIP EGMQCSCGID YYTLKPEVNN 
       210        220        230        240        250
ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV 
       260        270        280        290        300
TRMVIIMVIF FLICWLPYAS VAFYIFTHQG SNFGPIFMTL PAFFAKSSSI 
       310        320        330        340 
YNPVIYIMLN KQFRNCMLTT LCCGKNPLGD DDASATASKT ETSQVAPA
Length:348
Mass (Da):39,070
Last modified:July 27, 2011 - v2
<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:iB336C04B699AFF75
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0N4SUP8A0A0N4SUP8_MOUSE
Rhodopsin
Rho
203Annotation score:

Annotation score:3 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>
A0A0N4SV48A0A0N4SV48_MOUSE
Rhodopsin
Rho
189Annotation score:

Annotation score:3 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>
A0A0N4SWC6A0A0N4SWC6_MOUSE
Rhodopsin
Rho
54Annotation score:

Annotation score:2 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti20V → G in AAA39861 (PubMed:2844600).Curated1
Sequence conflicti20V → G in AAA63392 (PubMed:1978723).Curated1

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
M36699
, M36695, M36696, M36697, M36698 Genomic DNA Translation: AAA39861.1
M55171 Genomic DNA Translation: AAA63392.1
AK044333 mRNA Translation: BAC31871.1
AK044412 mRNA Translation: BAC31908.1
CH466523 Genomic DNA Translation: EDK99545.1
BC013125 mRNA Translation: AAH13125.1
BC031766 mRNA Translation: AAH31766.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS20446.1

Protein sequence database of the Protein Information Resource

More...PIRi		A23665

NCBI Reference Sequences

More...RefSeqi		NP_663358.1, NM_145383.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.2965
Mm.406156

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324

Database of genes from NCBI RefSeq genomes

More...GeneIDi		212541

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:212541

UCSC genome browser

More...UCSCi		uc009djk.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36699
, M36695, M36696, M36697, M36698 Genomic DNA Translation: AAA39861.1
M55171 Genomic DNA Translation: AAA63392.1
AK044333 mRNA Translation: BAC31871.1
AK044412 mRNA Translation: BAC31908.1
CH466523 Genomic DNA Translation: EDK99545.1
BC013125 mRNA Translation: AAH13125.1
BC031766 mRNA Translation: AAH31766.1
CCDSiCCDS20446.1
PIRiA23665
RefSeqiNP_663358.1, NM_145383.1
UniGeneiMm.2965
Mm.406156

3D structure databases

ProteinModelPortaliP15409
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15409, 2 interactors
MINTiP15409
STRINGi10090.ENSMUSP00000032471

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...GPCRDBi		Search...

PTM databases

iPTMnetiP15409
PhosphoSitePlusiP15409
SwissPalmiP15409

Proteomic databases

MaxQBiP15409
PaxDbiP15409
PRIDEiP15409

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324
GeneIDi212541
KEGGimmu:212541
UCSCiuc009djk.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6010
MGIiMGI:97914 Rho

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00940000154379
HOGENOMiHOG000253932
HOVERGENiHBG107442
InParanoidiP15409
KOiK04250
OMAiLAAYMFM
OrthoDBiEOG091G0BDA
TreeFamiTF324998

Enzyme and pathway databases

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

Miscellaneous databases

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

More...ChiTaRSi		Rho mouse

Protein Ontology

More...PROi		PR:P15409

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000030324 Expressed in 56 organ(s), highest expression level in retina
CleanExiMM_RHO
ExpressionAtlasiP15409 baseline and differential
GenevisibleiP15409 MM

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_MOUSE
<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: P15409
Secondary accession number(s): Q8K0D8, Q96DZ2
<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: April 1, 1990
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 168 of the entry and version 2 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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