P15409 (OPSD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rhodopsin

Gene names

Name:

Rho

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Sensory transduction Vision
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Chromophore Metal-binding Zinc
Molecular function	G-protein coupled receptor Photoreceptor protein Receptor Retinal protein Transducer
PTM	Acetylation Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to light stimulus Inferred from mutant phenotype PubMed 21052544. 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: Compara retina development in camera-type eye Inferred from mutant phenotype PubMed 21052544. Source: MGI rhodopsin mediated signaling pathway Inferred from electronic annotation. Source: Compara sensory perception of light stimulus Inferred from mutant phenotype PubMed 16723493. Source: MGI visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from sequence orthology PubMed 11773008. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor inner segment membrane Inferred from sequence or structural similarity. Source: UniProtKB photoreceptor outer segment membrane Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara
Molecular_function	G-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: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	Rhodopsin		PRO_0000197687
Regions
	Topological domain	1 – 36	36	Extracellular
	Transmembrane	37 – 61	25	Helical; Name=1; Potential
	Topological domain	62 – 73	12	Cytoplasmic
	Transmembrane	74 – 98	25	Helical; Name=2; Potential
	Topological domain	99 – 113	15	Extracellular
	Transmembrane	114 – 133	20	Helical; Name=3; Potential
	Topological domain	134 – 152	19	Cytoplasmic
	Transmembrane	153 – 176	24	Helical; Name=4; Potential
	Topological domain	177 – 202	26	Extracellular
	Transmembrane	203 – 230	28	Helical; Name=5; Potential
	Topological domain	231 – 252	22	Cytoplasmic
	Transmembrane	253 – 276	24	Helical; Name=6; Potential
	Topological domain	277 – 284	8	Extracellular
	Transmembrane	285 – 309	25	Helical; Name=7; Potential
	Topological domain	310 – 348	39	Cytoplasmic
	Region	113 – 125	13	Retinal chromophore binding By similarity
	Region	207 – 212	6	Retinal chromophore binding By similarity
	Motif	134 – 137	4	'Ionic lock' involved in activated form stabilization
Sites
	Metal binding	201	1	Zinc By similarity
	Metal binding	279	1	Zinc By similarity
	Binding site	265	1	Retinal chromophore By similarity
	Binding site	296	1	Retinal chromophore (covalent) By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	296	1	N6-(retinylidene)lysine
	Modified residue	334	1	Phosphoserine Ref.7
	Modified residue	336	1	Phosphothreonine By similarity
	Modified residue	338	1	Phosphoserine Ref.7
	Modified residue	340	1	Phosphothreonine By similarity
	Modified residue	342	1	Phosphothreonine By similarity
	Modified residue	343	1	Phosphoserine Ref.7
	Lipidation	322	1	S-palmitoyl cysteine By similarity
	Lipidation	323	1	S-palmitoyl cysteine By similarity
	Glycosylation	2	1	N-linked (GlcNAc...) By similarity
	Glycosylation	15	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	110 ↔ 187		By similarity
Experimental info
	Sequence conflict	20	1	V → G in AAA39861. Ref.1
	Sequence conflict	20	1	V → G in AAA63392. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P15409 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: B336C04B699AFF75	FASTA	348	39,070
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00130448.
PIR	A23665.
RefSeq	NP_663358.1. NM_145383.1.
UniGene	Mm.2965. Mm.406156.
3D structure databases
ProteinModelPortal	P15409.
SMR	P15409. Positions 1-326.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1795197.
STRING	10090.ENSMUSP00000032471.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P15409.
Proteomic databases
PRIDE	P15409.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324.
GeneID	212541.
KEGG	mmu:212541.
Organism-specific databases
CTD	6010.
MGI	MGI:97914. Rho.
Phylogenomic databases
eggNOG	NOG311294.
GeneTree	ENSGT00700000104057.
HOGENOM	HOG000253932.
HOVERGEN	HBG107442.
InParanoid	Q8K0D8.
KO	K04250.
OMA	LAAYMFM.
OrthoDB	EOG4P5K9D.
Gene expression databases
Bgee	P15409.
CleanEx	MM_RHO.
Genevestigator	P15409.
GermOnline	ENSMUSG00000030324. Mus musculus.
Family and domain databases
Gene3D	4.10.840.10. 1 hit.
InterPro	IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR001760. Opsin. IPR000732. Rhodopsin. IPR019477. Rhodopsin_N. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. PF10413. Rhodopsin_N. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00238. OPSIN. PR00579. RHODOPSIN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. PS00238. OPSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RHO. mouse.
NextBio	373628.
SOURCE	Search...

Entry information

Entry name

OPSD_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program