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Protein

Rhodopsin

Gene

Rho

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal.1 Publication

Absorptioni

Abs(max)=495 nm

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011ZincBy similarity
Binding sitei265 – 2651Retinal chromophoreBy similarity
Metal bindingi279 – 2791ZincBy similarity

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. photoreceptor activity Source: UniProtKB-KW
  4. retinal binding Source: Ensembl
  5. spectrin binding Source: MGI

GO - Biological processi

  1. cellular response to light stimulus Source: MGI
  2. detection of light stimulus Source: MGI
  3. phototransduction Source: MGI
  4. protein-chromophore linkage Source: UniProtKB-KW
  5. protein phosphorylation Source: MGI
  6. red, far-red light phototransduction Source: Ensembl
  7. response to light stimulus Source: MGI
  8. retina development in camera-type eye Source: MGI
  9. rhodopsin mediated signaling pathway Source: Ensembl
  10. sensory perception of light stimulus Source: MGI
  11. visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Chromophore, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_280597. The canonical retinoid cycle in rods (twilight vision).
REACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_315493. VxPx cargo-targeting to cilium.
REACT_326042. Activation of the phototransduction cascade.
REACT_331048. G alpha (i) signalling events.
REACT_332325. Opsins.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:Rho
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:97914. Rho.

Subcellular locationi

Membrane; Multi-pass membrane protein
Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to the rod outer segment (OS) photosensory cilia.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636ExtracellularAdd
BLAST
Transmembranei37 – 6125Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini62 – 7312CytoplasmicAdd
BLAST
Transmembranei74 – 9825Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini99 – 11315ExtracellularAdd
BLAST
Transmembranei114 – 13320Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini134 – 15219CytoplasmicAdd
BLAST
Transmembranei153 – 17624Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini177 – 20226ExtracellularAdd
BLAST
Transmembranei203 – 23028Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini231 – 25222CytoplasmicAdd
BLAST
Transmembranei253 – 27624Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini277 – 2848Extracellular
Transmembranei285 – 30925Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini310 – 34839CytoplasmicAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. Golgi apparatus Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. photoreceptor inner segment Source: UniProtKB
  5. photoreceptor inner segment membrane Source: UniProtKB
  6. photoreceptor outer segment Source: MGI
  7. photoreceptor outer segment membrane Source: UniProtKB
  8. plasma membrane Source: MGI
  9. rough endoplasmic reticulum membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348RhodopsinPRO_0000197687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi2 – 21N-linked (GlcNAc...)By similarity
Glycosylationi15 – 151N-linked (GlcNAc...)By similarity
Disulfide bondi110 ↔ 187PROSITE-ProRule annotation
Modified residuei296 – 2961N6-(retinylidene)lysineBy similarity
Lipidationi322 – 3221S-palmitoyl cysteineBy similarity
Lipidationi323 – 3231S-palmitoyl cysteineBy similarity
Modified residuei334 – 3341Phosphoserine1 Publication
Modified residuei336 – 3361PhosphothreonineBy similarity
Modified residuei338 – 3381Phosphoserine1 Publication
Modified residuei340 – 3401PhosphothreonineBy similarity
Modified residuei342 – 3421PhosphothreonineBy similarity
Modified residuei343 – 3431Phosphoserine1 Publication

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.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiP15409.
PRIDEiP15409.

PTM databases

PhosphoSiteiP15409.

Expressioni

Tissue specificityi

Rod-shaped photoreceptor cells which mediate vision in dim light.

Gene expression databases

BgeeiP15409.
CleanExiMM_RHO.
GenevestigatoriP15409.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi229339. 1 interaction.
IntActiP15409. 2 interactions.
MINTiMINT-1795197.
STRINGi10090.ENSMUSP00000032471.

Structurei

3D structure databases

ProteinModelPortaliP15409.
SMRiP15409. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 12513Retinal chromophore bindingBy similarityAdd
BLAST
Regioni207 – 2126Retinal chromophore bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi134 – 1374'Ionic lock' involved in activated form stabilization

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311294.
GeneTreeiENSGT00760000118977.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiP15409.
KOiK04250.
OMAiLAAYMFM.
OrthoDBiEOG72NRQJ.
TreeFamiTF324998.

Family and domain databases

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:iB336C04B699AFF75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201V → G in AAA39861 (PubMed:2844600).Curated
Sequence conflicti20 – 201V → G in AAA63392 (PubMed:1978723).Curated

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.

Genome annotation databases

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

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.
SMRiP15409. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229339. 1 interaction.
IntActiP15409. 2 interactions.
MINTiMINT-1795197.
STRINGi10090.ENSMUSP00000032471.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP15409.

Proteomic databases

MaxQBiP15409.
PRIDEiP15409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6010.
MGIiMGI:97914. Rho.

Phylogenomic databases

eggNOGiNOG311294.
GeneTreeiENSGT00760000118977.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiP15409.
KOiK04250.
OMAiLAAYMFM.
OrthoDBiEOG72NRQJ.
TreeFamiTF324998.

Enzyme and pathway databases

ReactomeiREACT_280597. The canonical retinoid cycle in rods (twilight vision).
REACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_315493. VxPx cargo-targeting to cilium.
REACT_326042. Activation of the phototransduction cascade.
REACT_331048. G alpha (i) signalling events.
REACT_332325. Opsins.

Miscellaneous databases

ChiTaRSiRho. mouse.
NextBioi373628.
PROiP15409.
SOURCEiSearch...

Gene expression databases

BgeeiP15409.
CleanExiMM_RHO.
GenevestigatoriP15409.

Family and domain databases

Gene3Di4.10.840.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mouse opsin. Gene structure and molecular basis of multiple transcripts."
    Al-Ubaidi M.R., Pittler S.J., Champagne M.S., Triantafyllos J.T., McGinnis J.F., Baehr W.
    J. Biol. Chem. 265:20563-20569(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation."
    Lee K.A., Craven K.B., Niemi G.A., Hurley J.B.
    Protein Sci. 11:862-874(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-334; SER-338 AND SER-343, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiOPSD_MOUSE
AccessioniPrimary (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: April 1, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.