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P15409 (OPSD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhodopsin
Gene names
Name:Rho
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Homodimer By similarity.

Subcellular location

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.

Tissue specificity

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

Post-translational modification

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. Ref.7

Contains one covalently linked retinal chromophore By similarity.

Disruption phenotype

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. Ref.6

Sequence similarities

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

Biophysicochemical properties

Absorption:

Abs(max)=495 nm

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandChromophore
Metal-binding
Zinc
   Molecular functionG-protein coupled receptor
Photoreceptor protein
Receptor
Retinal protein
Transducer
   PTMAcetylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to light stimulus

Inferred from mutant phenotype PubMed 21052544. Source: MGI

detection of light stimulus

Inferred from mutant phenotype PubMed 11747369. Source: MGI

phototransduction

Inferred from mutant phenotype PubMed 16723493. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 10097103. Source: MGI

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

red, far-red light phototransduction

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from mutant phenotype PubMed 16723493. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

rhodopsin mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

sensory perception of light stimulus

Inferred from mutant phenotype PubMed 16723493. Source: MGI

visual perception

Inferred from mutant phenotype PubMed 22937111. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from sequence orthology PubMed 11773008. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

photoreceptor inner segment

Inferred from direct assay PubMed 10399916. Source: UniProtKB

photoreceptor inner segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay PubMed 12651948PubMed 19332056PubMed 20592197PubMed 22869374. Source: MGI

photoreceptor outer segment membrane

Inferred from sequence or structural similarity. Source: UniProtKB

rough endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

photoreceptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

retinal binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Rhodopsin
PRO_0000197687

Regions

Topological domain1 – 3636Extracellular
Transmembrane37 – 6125Helical; Name=1; Potential
Topological domain62 – 7312Cytoplasmic
Transmembrane74 – 9825Helical; Name=2; Potential
Topological domain99 – 11315Extracellular
Transmembrane114 – 13320Helical; Name=3; Potential
Topological domain134 – 15219Cytoplasmic
Transmembrane153 – 17624Helical; Name=4; Potential
Topological domain177 – 20226Extracellular
Transmembrane203 – 23028Helical; Name=5; Potential
Topological domain231 – 25222Cytoplasmic
Transmembrane253 – 27624Helical; Name=6; Potential
Topological domain277 – 2848Extracellular
Transmembrane285 – 30925Helical; Name=7; Potential
Topological domain310 – 34839Cytoplasmic
Region113 – 12513Retinal chromophore binding By similarity
Region207 – 2126Retinal chromophore binding By similarity
Motif134 – 1374'Ionic lock' involved in activated form stabilization

Sites

Metal binding2011Zinc By similarity
Metal binding2791Zinc By similarity
Binding site2651Retinal chromophore By similarity
Binding site2961Retinal chromophore (covalent) By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2961N6-(retinylidene)lysine
Modified residue3341Phosphoserine Ref.7
Modified residue3361Phosphothreonine By similarity
Modified residue3381Phosphoserine Ref.7
Modified residue3401Phosphothreonine By similarity
Modified residue3421Phosphothreonine By similarity
Modified residue3431Phosphoserine Ref.7
Lipidation3221S-palmitoyl cysteine By similarity
Lipidation3231S-palmitoyl cysteine By similarity
Glycosylation21N-linked (GlcNAc...) By similarity
Glycosylation151N-linked (GlcNAc...) By similarity
Disulfide bond110 ↔ 187 By similarity

Experimental info

Sequence conflict201V → G in AAA39861. Ref.1
Sequence conflict201V → G in AAA63392. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15409 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B336C04B699AFF75

FASTA34839,070
        10         20         30         40         50         60 
MNGTEGPNFY VPFSNVTGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY 

        70         80         90        100        110        120 
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG 

       130        140        150        160        170        180 
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVVFT WIMALACAAP PLVGWSRYIP 

       190        200        210        220        230        240 
EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES 

       250        260        270        280        290        300 
ATTQKAEKEV TRMVIIMVIF FLICWLPYAS VAFYIFTHQG SNFGPIFMTL PAFFAKSSSI 

       310        320        330        340 
YNPVIYIMLN KQFRNCMLTT LCCGKNPLGD DDASATASKT ETSQVAPA 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and analysis of the mouse opsin gene."
Baehr W., Falk J.D., Bugra K., Triantafyllos J.T., McGinnis J.F.
FEBS Lett. 238:253-256(1988) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Retinopathy induced in mice by targeted disruption of the rhodopsin gene."
Humphries M.M., Rancourt D., Farrar G.J., Kenna P., Hazel M., Bush R.A., Sieving P.A., Sheils D.M., McNally N., Creighton P., Erven A., Boros A., Gulya K., Capecchi M.R., Humphries P.
Nat. Genet. 15:216-219(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36699 expand/collapse EMBL AC list , 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.
PIRA23665.
RefSeqNP_663358.1. NM_145383.1.
UniGeneMm.2965.
Mm.406156.

3D structure databases

ProteinModelPortalP15409.
SMRP15409. Positions 1-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229339. 1 interaction.
IntActP15409. 2 interactions.
MINTMINT-1795197.
STRING10090.ENSMUSP00000032471.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP15409.

Proteomic databases

PRIDEP15409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324.
GeneID212541.
KEGGmmu:212541.
UCSCuc009djk.1. mouse.

Organism-specific databases

CTD6010.
MGIMGI:97914. Rho.

Phylogenomic databases

eggNOGNOG311294.
GeneTreeENSGT00710000106574.
HOGENOMHOG000253932.
HOVERGENHBG107442.
InParanoidQ8K0D8.
KOK04250.
OMALAAYMFM.
OrthoDBEOG72NRQJ.
TreeFamTF324998.

Gene expression databases

BgeeP15409.
CleanExMM_RHO.
GenevestigatorP15409.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
4.10.840.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001760. Opsin.
IPR027430. Retinal_BS.
IPR000732. Rhodopsin.
IPR019477. Rhodopsin_N.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF10413. Rhodopsin_N. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00238. OPSIN.
PR00579. RHODOPSIN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS00238. OPSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHO. mouse.
NextBio373628.
PROP15409.
SOURCESearch...

Entry information

Entry nameOPSD_MOUSE
AccessionPrimary (citable) accession number: P15409
Secondary accession number(s): Q8K0D8, Q96DZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries