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P15409

- OPSD_MOUSE

UniProt

P15409 - OPSD_MOUSE

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Protein

Rhodopsin

Gene
Rho
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 2011Zinc By similarity
Binding sitei265 – 2651Retinal chromophore By similarity
Metal bindingi279 – 2791Zinc By 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. protein binding Source: MGI
  5. retinal binding Source: Ensembl
  6. 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_188252. Activation of the phototransduction cascade.
REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_188277. The canonical retinoid cycle in rods (twilight vision).

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:Rho
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: 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=1; Reviewed predictionAdd
BLAST
Topological domaini62 – 7312CytoplasmicAdd
BLAST
Transmembranei74 – 9825Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini99 – 11315ExtracellularAdd
BLAST
Transmembranei114 – 13320Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini134 – 15219CytoplasmicAdd
BLAST
Transmembranei153 – 17624Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini177 – 20226ExtracellularAdd
BLAST
Transmembranei203 – 23028Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini231 – 25222CytoplasmicAdd
BLAST
Transmembranei253 – 27624Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini277 – 2848Extracellular
Transmembranei285 – 30925Helical; Name=7; Reviewed predictionAdd
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. 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-acetylmethionine By similarity
Glycosylationi2 – 21N-linked (GlcNAc...) By similarity
Glycosylationi15 – 151N-linked (GlcNAc...) By similarity
Disulfide bondi110 ↔ 187 By similarity
Modified residuei296 – 2961N6-(retinylidene)lysine By similarity
Lipidationi322 – 3221S-palmitoyl cysteine By similarity
Lipidationi323 – 3231S-palmitoyl cysteine By similarity
Modified residuei334 – 3341Phosphoserine1 Publication
Modified residuei336 – 3361Phosphothreonine By similarity
Modified residuei338 – 3381Phosphoserine1 Publication
Modified residuei340 – 3401Phosphothreonine By similarity
Modified residuei342 – 3421Phosphothreonine By 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.

Family & Domainsi

Region

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

Motif

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311294.
GeneTreeiENSGT00710000106574.
HOGENOMiHOG000253932.
HOVERGENiHBG107442.
InParanoidiQ8K0D8.
KOiK04250.
OMAiLAAYMFM.
OrthoDBiEOG72NRQJ.
TreeFamiTF324998.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
4.10.840.10. 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

MNGTEGPNFY VPFSNVTGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL    50
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH 100
GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE 150
NHAIMGVVFT WIMALACAAP PLVGWSRYIP EGMQCSCGID YYTLKPEVNN 200
ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV 250
TRMVIIMVIF FLICWLPYAS VAFYIFTHQG SNFGPIFMTL PAFFAKSSSI 300
YNPVIYIMLN KQFRNCMLTT LCCGKNPLGD DDASATASKT ETSQVAPA 348
Length:348
Mass (Da):39,070
Last modified:July 27, 2011 - v2
Checksum:iB336C04B699AFF75
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201V → G in AAA39861. 1 Publication
Sequence conflicti20 – 201V → G in AAA63392. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
SMRi P15409. Positions 1-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229339. 1 interaction.
IntActi P15409. 2 interactions.
MINTi MINT-1795197.
STRINGi 10090.ENSMUSP00000032471.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P15409.

Proteomic databases

MaxQBi P15409.
PRIDEi P15409.

Protocols and materials databases

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 NOG311294.
GeneTreei ENSGT00710000106574.
HOGENOMi HOG000253932.
HOVERGENi HBG107442.
InParanoidi Q8K0D8.
KOi K04250.
OMAi LAAYMFM.
OrthoDBi EOG72NRQJ.
TreeFami TF324998.

Enzyme and pathway databases

Reactomei REACT_188252. Activation of the phototransduction cascade.
REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_188277. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

ChiTaRSi RHO. mouse.
NextBioi 373628.
PROi P15409.
SOURCEi Search...

Gene expression databases

Bgeei P15409.
CleanExi MM_RHO.
Genevestigatori P15409.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
4.10.840.10. 1 hit.
InterProi IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view ]
Pfami PF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view ]
PRINTSi PR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1990) [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(2005) [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 (JUL-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(2004) [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(2002) [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: September 3, 2014
This is version 135 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

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