Rho

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 key	Position(s)	DescriptionActions	Length
Siteⁱ	113	Plays an important role in the conformation switch to the active conformationBy similarity	1
Metal bindingⁱ	201	ZincBy similarity	1
Metal bindingⁱ	279	ZincBy similarity	1

GO - Molecular functionⁱ

11-cis retinal binding Source: UniProtKB
G-protein coupled photoreceptor activity Source: UniProtKB
metal ion binding Source: UniProtKB-KW
retinal binding Source: MGI
spectrin binding
Source: MGI
Inferred from sequence orthologyⁱ
- 23704327

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

absorption of visible light Source: AgBase
cellular response to light stimulus
Source: MGI
Inferred from mutant phenotypeⁱ
- 21052544
detection of light stimulus
Source: MGI
Inferred from mutant phenotypeⁱ
- 11747369
G-protein coupled receptor signaling pathway Source: MGI
photoreceptor cell maintenance
Source: MGI
Inferred from mutant phenotypeⁱ
- 22183357
phototransduction
Source: MGI
Inferred from mutant phenotypeⁱ
- 16723493
protein-chromophore linkage Source: UniProtKB-KW
protein phosphorylation
Source: MGI
Inferred from direct assayⁱ
- 10097103
red, far-red light phototransduction Source: MGI
response to light stimulus
Source: MGI
Inferred from mutant phenotypeⁱ
- 16723493
retina development in camera-type eye
Source: MGI
Inferred from mutant phenotypeⁱ
- 21052544
rhodopsin mediated signaling pathway Source: UniProtKB
sensory perception of light stimulus
Source: MGI
Inferred from mutant phenotypeⁱ
- 16723493
visual perception
Source: MGI
Inferred from mutant phenotypeⁱ
- 22937111

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer
Biological process	Sensory transduction, Vision
Ligand	Chromophore, Metal-binding, Zinc

Enzyme and pathway databases

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

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

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Rhodopsin
Gene namesⁱ	Name:Rho
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 6

Organism-specific databases

MGIⁱ	MGI:97914 Rho

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 36	ExtracellularCuratedAdd BLAST	36
Transmembraneⁱ	37 – 61	Helical; Name=1By similarityAdd BLAST	25
Topological domainⁱ	62 – 73	CytoplasmicCuratedAdd BLAST	12
Transmembraneⁱ	74 – 96	Helical; Name=2By similarityAdd BLAST	23
Topological domainⁱ	97 – 110	ExtracellularCuratedAdd BLAST	14
Transmembraneⁱ	111 – 133	Helical; Name=3By similarityAdd BLAST	23
Topological domainⁱ	134 – 152	CytoplasmicCuratedAdd BLAST	19
Transmembraneⁱ	153 – 173	Helical; Name=4By similarityAdd BLAST	21
Topological domainⁱ	174 – 202	ExtracellularCuratedAdd BLAST	29
Transmembraneⁱ	203 – 224	Helical; Name=5By similarityAdd BLAST	22
Topological domainⁱ	225 – 252	CytoplasmicCuratedAdd BLAST	28
Transmembraneⁱ	253 – 274	Helical; Name=6By similarityAdd BLAST	22
Topological domainⁱ	275 – 286	ExtracellularCuratedAdd BLAST	12
Transmembraneⁱ	287 – 308	Helical; Name=7By similarityAdd BLAST	22
Topological domainⁱ	309 – 348	CytoplasmicCuratedAdd BLAST	40

Keywords - Cellular componentⁱ

Cell projection, Membrane

Pathology & Biotechⁱ

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

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000197687	1 – 348	RhodopsinAdd BLAST		348

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineBy similarity	1
Glycosylationⁱ	2	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	15	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	110 ↔ 187	PROSITE-ProRule annotation
Modified residueⁱ	296	N6-(retinylidene)lysineBy similarity	1
Lipidationⁱ	322	S-palmitoyl cysteineBy similarity	1
Lipidationⁱ	323	S-palmitoyl cysteineBy similarity	1
Modified residueⁱ	334	Phosphoserine1 Publication	1
Modified residueⁱ	336	PhosphothreonineBy similarity	1
Modified residueⁱ	338	Phosphoserine1 Publication	1
Modified residueⁱ	340	PhosphothreonineBy similarity	1
Modified residueⁱ	342	PhosphothreonineBy similarity	1
Modified residueⁱ	343	Phosphoserine1 Publication	1

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
PaxDbⁱ	P15409
PRIDEⁱ	P15409

PTM databases

iPTMnetⁱ	P15409
PhosphoSitePlusⁱ	P15409
SwissPalmⁱ	P15409

Expressionⁱ

Tissue specificityⁱ

Rod-shaped photoreceptor cells in the retina (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000030324 Expressed in 56 organ(s), highest expression level in retina
CleanExⁱ	MM_RHO
ExpressionAtlasⁱ	P15409 baseline and differential
Genevisibleⁱ	P15409 MM

Interactionⁱ

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

spectrin binding
Source: MGI
Inferred from sequence orthologyⁱ
- 23704327

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActⁱ	P15409, 2 interactors
Molecular INTeraction database More...MINTⁱ	P15409
STRINGⁱ	10090.ENSMUSP00000032471

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P15409
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	330 – 348	Interaction with SAGBy similarityAdd BLAST		19

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	134 – 136	'Ionic lock' involved in activated form stabilizationBy similarity		3

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3656 Eukaryota ENOG410XRW9 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118977
HOGENOMⁱ	HOG000253932
HOVERGENⁱ	HBG107442
InParanoidⁱ	P15409
KEGG Orthology (KO) More...KOⁱ	K04250
OMAⁱ	LAAYMFM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0BDA
TreeFamⁱ	TF324998

Family and domain databases

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
PRINTSⁱ	PR00237 GPCRRHODOPSN PR00238 OPSIN PR00579 RHODOPSIN
SMARTⁱ	View protein in SMART SM01381 7TM_GPCR_Srsx, 1 hit
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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.ⁱShow all

P15409-1 [UniParc]FASTA Add 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

Checksum:ⁱB336C04B699AFF75

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
A0A0N4SUP8	A0A0N4SUP8_MOUSE	Rhodopsin Rhodopsin	Rho	203	Annotation score:
A0A0N4SV48	A0A0N4SV48_MOUSE	Rhodopsin Rhodopsin	Rho	189	Annotation score:
A0A0N4SWC6	A0A0N4SWC6_MOUSE	Rhodopsin Rhodopsin	Rho	54	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	20	V → G in AAA39861 (PubMed:2844600).Curated		1
Sequence conflictⁱ	20	V → G in AAA63392 (PubMed:1978723).Curated		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS20446.1
PIRⁱ	A23665
NCBI Reference Sequences More...RefSeqⁱ	NP_663358.1, NM_145383.1
UniGeneⁱ	Mm.2965 Mm.406156

Genome annotation databases

Ensemblⁱ	ENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324
GeneIDⁱ	212541
KEGGⁱ	mmu:212541
UCSC genome browser More...UCSCⁱ	uc009djk.1 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P15409	Rhodopsin (Fragment)		MOUSE		203	UniRef100_P15409
UPI0007EDE674		MOUSE		310

Protein	Similar proteins		Species	Score	Length	Source
P15409	Rhodopsin	)	HUMAN		348	UniRef90_P08100
Rhodopsin	)	BOVIN		348
Rhodopsin		SHEEP		348
Rhodopsin		SMICR		348
Rhodopsin		TRIMA		348
+343

Protein	Similar proteins		Species	Score	Length	Source
P15409	Rhodopsin	)	HUMAN		348	UniRef50_P08100
Rhodopsin		DELDE		348
Rhodopsin		SMICR		348
Rhodopsin		OTOCR		348
Rhodopsin	)	TURTR		348
+567

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
CCDSⁱ	CCDS20446.1
PIRⁱ	A23665
RefSeqⁱ	NP_663358.1, NM_145383.1
UniGeneⁱ	Mm.2965 Mm.406156

3D structure databases

ProteinModelPortalⁱ	P15409
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P15409, 2 interactors
MINTⁱ	P15409
STRINGⁱ	10090.ENSMUSP00000032471

Protein family/group databases

GPCRDBⁱ	Search...

GPCRDBⁱ

Search...

PTM databases

iPTMnetⁱ	P15409
PhosphoSitePlusⁱ	P15409
SwissPalmⁱ	P15409

Proteomic databases

MaxQBⁱ	P15409
PaxDbⁱ	P15409
PRIDEⁱ	P15409

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324
GeneIDⁱ	212541
KEGGⁱ	mmu:212541
UCSCⁱ	uc009djk.1 mouse

Organism-specific databases

CTDⁱ	6010
MGIⁱ	MGI:97914 Rho

Phylogenomic databases

eggNOGⁱ	KOG3656 Eukaryota ENOG410XRW9 LUCA
GeneTreeⁱ	ENSGT00760000118977
HOGENOMⁱ	HOG000253932
HOVERGENⁱ	HBG107442
InParanoidⁱ	P15409
KOⁱ	K04250
OMAⁱ	LAAYMFM
OrthoDBⁱ	EOG091G0BDA
TreeFamⁱ	TF324998

Enzyme and pathway databases

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

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

Miscellaneous databases

ChiTaRSⁱ	Rho mouse
Protein Ontology More...PROⁱ	PR:P15409
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000030324 Expressed in 56 organ(s), highest expression level in retina
CleanExⁱ	MM_RHO
ExpressionAtlasⁱ	P15409 baseline and differential
Genevisibleⁱ	P15409 MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR000276 GPCR_Rhodpsn IPR017452 GPCR_Rhodpsn_7TM IPR001760 Opsin IPR027430 Retinal_BS IPR000732 Rhodopsin IPR019477 Rhodopsin_N
Pfamⁱ	View protein in Pfam PF00001 7tm_1, 1 hit PF10413 Rhodopsin_N, 1 hit
PRINTSⁱ	PR00237 GPCRRHODOPSN PR00238 OPSIN PR00579 RHODOPSIN
SMARTⁱ	View protein in SMART SM01381 7TM_GPCR_Srsx, 1 hit
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	OPSD_MOUSE
Accessionⁱ	P15409Primary (citable) accession number: P15409 Secondary accession number(s): Q8K0D8, Q96DZ2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
	Last sequence update:	July 27, 2011
	Last modified:	September 12, 2018
	This is version 166 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

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UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P15409 (OPSD_MOUSE)

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Rhodopsin

Select a section on the left to see content.

<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

Sites

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Other locations

Endoplasmic reticulum

Golgi apparatus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<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 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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

<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

Motif

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ