Rhodopsin - Homo sapiens (Human)

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P08100 (OPSD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 153. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Rhodopsin

Alternative name(s):
Opsin-2

Gene names

Name:	RHO
Synonyms:	OPN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.
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. Ref.33
Tissue specificity	Rod shaped photoreceptor cells which mediates vision in dim light.
Post-translational modification	Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. Contains one covalently linked retinal chromophore By similarity.
Involvement in disease	Retinitis pigmentosa 4 (RP4) [MIM:613731]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.31 Ref.33 Ref.34 Ref.35 Congenital stationary night blindness, autosomal dominant, 1 (CSNBAD1) [MIM:610445]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.29 Ref.32
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
Coding sequence diversity	Polymorphism
Disease	Congenital stationary night blindness Disease mutation Retinitis pigmentosa
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	protein phosphorylation Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara rhodopsin mediated signaling pathway Traceable author statement PubMed 8107847. Source: ProtInc visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 11767049. Source: MGI integral to plasma membrane Traceable author statement PubMed 8253795. Source: ProtInc photoreceptor inner segment membrane Inferred from direct assay Ref.33. Source: UniProtKB photoreceptor outer segment membrane Inferred from direct assay Ref.33. Source: UniProtKB rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara
Molecular_function	G-protein coupled receptor activity Traceable author statement PubMed 8107847. Source: ProtInc 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ZFYVE9	O95405	2	EBI-1394177,EBI-296817

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Rhodopsin

PRO_0000197677

Regions

Topological domain

1 – 36

Extracellular

Transmembrane

37 – 61

Helical; Name=1; Potential

Topological domain

62 – 73

Cytoplasmic

Transmembrane

74 – 98

Helical; Name=2; Potential

Topological domain

99 – 113

Extracellular

Transmembrane

114 – 133

Helical; Name=3; Potential

Topological domain

134 – 152

Cytoplasmic

Transmembrane

153 – 176

Helical; Name=4; Potential

Topological domain

177 – 202

Extracellular

Transmembrane

203 – 230

Helical; Name=5; Potential

Topological domain

231 – 252

Cytoplasmic

Transmembrane

253 – 276

Helical; Name=6; Potential

Topological domain

277 – 284

Extracellular

Transmembrane

285 – 309

Helical; Name=7; Potential

Topological domain

310 – 348

Cytoplasmic

Region

113 – 125

Retinal chromophore binding By similarity

Region

207 – 212

Retinal chromophore binding By similarity

Motif

134 – 137

'Ionic lock' involved in activated form stabilization

Sites

Metal binding

201

Zinc By similarity

Metal binding

279

Zinc By similarity

Binding site

265

Retinal chromophore By similarity

Binding site

296

Retinal chromophore (covalent) By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

296

N6-(retinylidene)lysine

Modified residue

334

Phosphoserine By similarity

Modified residue

336

Phosphothreonine By similarity

Modified residue

338

Phosphoserine By similarity

Modified residue

340

Phosphothreonine By similarity

Modified residue

342

Phosphothreonine By similarity

Modified residue

343

Phosphoserine By similarity

Lipidation

322

S-palmitoyl cysteine By similarity

Lipidation

323

S-palmitoyl cysteine By similarity

Glycosylation

N-linked (GlcNAc...) By similarity

Glycosylation

N-linked (GlcNAc...) By similarity

Disulfide bond

110 ↔ 187

By similarity

Natural variations

Natural variant

T → K in RP4.

VAR_004765

Natural variant

N → S in RP4. Ref.18

VAR_004766

Natural variant

T → M in RP4. Ref.11 Ref.16

VAR_004767

Natural variant

P → H in RP4; most common variant, leads to interaction with EDEM1 followed by degradation by the ERAD system. Ref.8 Ref.9 Ref.11 Ref.33

VAR_004768

Natural variant

P → L in RP4.

VAR_004769

Natural variant

Q → H in RP4.

VAR_004770

Natural variant

L → R in RP4. Ref.25

VAR_004771

Natural variant

M → T in RP4. Ref.21

VAR_004772

Natural variant

F → L in RP4.

VAR_004773

Natural variant

L → R in RP4.

VAR_004774

Natural variant

G → A. Ref.17

VAR_004775

Natural variant

G → R in RP4.

VAR_004776

Natural variant

G → V in RP4.

VAR_004777

Natural variant

P → R in RP4.
Corresponds to variant rs28933395 [ dbSNP | Ensembl ].

VAR_004778

Natural variant

T → R in RP4. Ref.9 Ref.11
Corresponds to variant rs28933394 [ dbSNP | Ensembl ].

VAR_004779

Natural variant

68 – 71

Missing in RP4.

VAR_004780

Natural variant

V → D in RP4.

VAR_004781

Natural variant

G → D in RP4.

VAR_004782

Natural variant

G → D in CSNBAD1. Ref.29

VAR_004783

Natural variant

T → I in CSNBAD1. Ref.32

VAR_004784

Natural variant

104

V → I. Ref.17

VAR_004785

Natural variant

106

G → R in RP4. Ref.17
Corresponds to variant rs28933994 [ dbSNP | Ensembl ].

VAR_004786

Natural variant

106

G → W in RP4.

VAR_004787

Natural variant

109

G → R in RP4. Ref.31

VAR_004788

Natural variant

110

C → F in RP4. Ref.22

VAR_004789

Natural variant

110

C → Y in RP4.

VAR_004790

Natural variant

114

G → D in RP4.

VAR_004791

Natural variant

125

L → R in RP4.

VAR_004792

Natural variant

127

S → F in RP4. Ref.24

VAR_004793

Natural variant

131

L → P in RP4. Ref.22 Ref.24

VAR_004794

Natural variant

135

R → G in RP4. Ref.17

VAR_004795

Natural variant

135

R → L in RP4.

VAR_004796

Natural variant

135

R → W in RP4. Ref.30 Ref.35

VAR_004797

Natural variant

140

C → S in RP4. Ref.17

VAR_004798

Natural variant

150

E → K in RP4; autosomal recessive. Ref.27 Ref.34

VAR_004799

Natural variant

164

A → E in RP4.

VAR_004800

Natural variant

164

A → V in RP4. Ref.22

VAR_004801

Natural variant

167

C → R in RP4.

VAR_004802

Natural variant

171

P → L in RP4.

VAR_004803

Natural variant

171

P → Q in RP4. Ref.23

VAR_004804

Natural variant

171

P → S in RP4.

VAR_004805

Natural variant

178

Y → C in RP4.

VAR_004806

Natural variant

178

Y → N in RP4. Ref.24

VAR_004807

Natural variant

180

P → S in RP4. Ref.35

VAR_068359

Natural variant

181

E → K in RP4.

VAR_004808

Natural variant

182

G → S in RP4. Ref.11

VAR_004809

Natural variant

186

S → P in RP4.

VAR_004810

Natural variant

188

G → E in RP4. Ref.17

VAR_004811

Natural variant

188

G → R in RP4.

VAR_004812

Natural variant

190

D → G in RP4.

VAR_004814

Natural variant

190

D → N in RP4.
Corresponds to variant rs28933992 [ dbSNP | Ensembl ].

VAR_004813

Natural variant

190

D → Y in RP4.

VAR_004815

Natural variant

207

M → R in RP4. Ref.15
Corresponds to variant rs28933995 [ dbSNP | Ensembl ].

VAR_004816

Natural variant

209

V → M Effect not known. Ref.17

VAR_004817

Natural variant

211

H → P in RP4.
Corresponds to variant rs28933993 [ dbSNP | Ensembl ].

VAR_004818

Natural variant

211

H → R in RP4. Ref.17

VAR_004819

Natural variant

214

I → N in RP4. Ref.35

VAR_068360

Natural variant

216

M → K in RP4. Ref.25

VAR_004820

Natural variant

220

F → C in RP4.

VAR_004821

Natural variant

222

C → R in RP4.

VAR_004822

Natural variant

255

Missing in RP4. Ref.10

VAR_004823

Natural variant

264

Missing in RP4.

VAR_004824

Natural variant

267

P → L in RP4. Ref.11

VAR_004825

Natural variant

267

P → R in RP4. Ref.24

VAR_004826

Natural variant

292

A → E in CSNBAD1. Ref.19

VAR_004827

Natural variant

296

K → E in RP4.
Corresponds to variant rs29001653 [ dbSNP | Ensembl ].

VAR_004828

Natural variant

297

S → R in RP4. Ref.24

VAR_004829

Natural variant

342

T → M in RP4.

VAR_004830

Natural variant

345

V → L in RP4. Ref.26

VAR_004831

Natural variant

345

V → M in RP4.

VAR_004832

Natural variant

347

P → A in RP4. Ref.28

VAR_004833

Natural variant

347

P → L in RP4; common variant. Ref.9 Ref.16

VAR_004834

Natural variant

347

P → Q in RP4.

VAR_004835

Natural variant

347

P → R in RP4. Ref.12
Corresponds to variant rs29001566 [ dbSNP | Ensembl ].

VAR_004836

Natural variant

347

P → S in RP4. Ref.9
Corresponds to variant rs29001637 [ dbSNP | Ensembl ].

VAR_004837

Sequences

Sequence

Length

Mass (Da)

Tools

P08100 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 6F4F6FCBA34265B2
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FASTA

348

38,893

        10         20         30         40         50         60 
MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY 

        70         80         90        100        110        120 
VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG 

       130        140        150        160        170        180 
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP 

       190        200        210        220        230        240 
EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES 

       250        260        270        280        290        300 
ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI 

       310        320        330        340 
YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and nucleotide sequence of the gene encoding human rhodopsin." Nathans J., Hogness D.S. Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes." Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Retina.
[4]	"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].
[5]	"Sequence analysis of the 5.34-kb 5' flanking region of the human rhodopsin-encoding gene." Bennett J., Beller B., Sun D., Kariko K. Gene 167:317-320(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
[6]	"Rhodopsin mutations in autosomal dominant retinitis pigmentosa." Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A., Bhattacharya S. Hum. Mutat. 2:249-255(1993) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON RP4 VARIANTS.
[7]	"Autosomal dominant retinitis pigmentosa: absence of the rhodopsin proline-->histidine substitution (codon 23) in pedigrees from Europe." Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G., Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., Watty A., Ludwig M., Schinzel A., Samanns C., Gal A., Bhattacharya S.S., Humphries P. Am. J. Hum. Genet. 47:941-945(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4.
[8]	"A point mutation of the rhodopsin gene in one form of retinitis pigmentosa." Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., Yandell D.W., Sandberg M.A., Berson E.L. Nature 343:364-366(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 HIS-23.
[9]	"Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa." Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E., Sandberg M.A., Berson E.L. N. Engl. J. Med. 323:1302-1307(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347.
[10]	"A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa." Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C., Bhattacharya S.S. Am. J. Hum. Genet. 48:26-30(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 ILE-255 DEL.
[11]	"Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-clamped denaturing gradient gel electrophoresis." Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M. Am. J. Hum. Genet. 49:699-706(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
[12]	"Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa." Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E., Schinzel A. Genomics 11:468-470(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 ARG-347.
[13]	"Rhodopsin mutations in autosomal dominant retinitis pigmentosa." Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G., Gouras P., Nathans J. Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4.
[14]	"Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa." Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L. Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4.
[15]	"Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin gene in the original 3q linked family." Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M., Sharpe E., Humphries P. Hum. Mol. Genet. 1:769-771(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 ARG-207.
[16]	"Point mutations of rhodopsin gene found in Japanese families with autosomal dominant retinitis pigmentosa (ADRP)." Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., Kanai A. Jpn. J. Hum. Genet. 37:125-132(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 MET-17 AND LEU-347.
[17]	"Identification of novel rhodopsin mutations responsible for retinitis pigmentosa: implications for the structure and function of rhodopsin." Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C., Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R., Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J. Am. J. Hum. Genet. 53:80-89(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, VARIANTS ALA-51; ILE-104 AND MET-209.
[18]	"Autosomal dominant 'sector' retinitis pigmentosa due to a point mutation predicting an Asn-15-Ser substitution of rhodopsin." Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P., Duvigneau C., Gal A. Hum. Mol. Genet. 2:813-814(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 SER-15.
[19]	"Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness." Dryja T.P., Berson E.L., Rao V.R., Oprian D.D. Nat. Genet. 4:280-283(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSNBAD1 GLU-292.
[20]	"Further screening of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa." Vaithinathan R., Berson E.L., Dryja T.P. Genomics 21:461-463(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4.
[21]	"Identification of a novel rhodopsin mutation (Met-44-Thr) in a simplex case of retinitis pigmentosa." Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C., Carballo M. Hum. Genet. 94:283-286(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 THR-44.
[22]	"Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with autosomal dominant retinitis pigmentosa." Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S., Humphries P., Gal A. Hum. Mol. Genet. 3:1203-1203(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 PHE-110; PRO-131 AND VAL-164.
[23]	"Identification of a new mutation at codon 171 of rhodopsin gene causing autosomal dominant retinitis pigmentosa." Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., Cabeza J.C. Hum. Mol. Genet. 3:1421-1421(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 GLN-171.
[24]	"Five novel missense mutations of the rhodopsin gene in autosomal dominant retinitis pigmentosa." Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I., Philip N., Soubrane G., Coscas G., Munnich A. Hum. Mol. Genet. 3:1433-1434(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
[25]	"Two new rhodopsin transversion mutations (L40R; M216K) in families with autosomal dominant retinitis pigmentosa." Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., Bhattacharya S. Hum. Mutat. 3:409-410(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 ARG-40 AND LYS-216.
[26]	"Autosomal dominant retinitis pigmentosa in a large family: a clinical and molecular genetic study." Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J. Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 LEU-345.
[27]	"Missense rhodopsin mutation in a family with recessive RP." Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R., Orth U., Oehlmann R., Gal A. Nat. Genet. 8:10-11(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARRP LYS-150.
[28]	"Rhodopsin mutation proline347-to-alanine in a family with autosomal dominant retinitis pigmentosa indicates an important role for proline at position 347." Macke J.P., Hennessey J.C., Nathans J. Hum. Mol. Genet. 4:775-776(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 ALA-347.
[29]	"Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation." Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., Alpern M. Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSNBAD1 ASP-90.
[30]	"Retinitis punctata albescens associated with the Arg135Trp mutation in the rhodopsin gene." Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., Munnich A., Kaplan J. Am. J. Ophthalmol. 121:19-25(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 TRP-135.
[31]	"Rhodopsin mutation G109R in a family with autosomal dominant retinitis pigmentosa." Goliath R., Bardien S., September A., Martin R., Ramesar R., Greenberg J. Hum. Mutat. Suppl. 1:S40-S41(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 ARG-109.
[32]	"A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness." Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N., Findlay J.B.C., Humphries P., Kenna P.F. Hum. Mutat. 13:75-81(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSNBAD1 ILE-94.
[33]	"A dual role for EDEM1 in the processing of rod opsin." Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E. J. Cell Sci. 122:4465-4472(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, SUBCELLULAR LOCATION.
[34]	"A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani families with autosomal recessive retinitis pigmentosa." Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., Sadeque A., Bokhari H., Collin R.W., Orth U., van Genderen M.M., den Hollander A.I., Cremers F.P., Qamar R. Mol. Vis. 15:2526-2534(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RP4 LYS-150.
[35]	"Next-generation genetic testing for retinitis pigmentosa." Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. Scheffer H. Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RP4 TRP-135; SER-180 AND ASN-214.
+	Additional computationally mapped references.

Web resources

Mutations of the RHO gene

Retina International's Scientific Newsletter

GeneReviews

Wikipedia

Rhodopsin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	U49742 Genomic DNA. Translation: AAC31763.1. AB065668 Genomic DNA. Translation: BAC05894.1. BX537381 mRNA. Translation: CAD97623.1. BC112104 mRNA. Translation: AAI12105.1. BC112106 mRNA. Translation: AAI12107.1. U16824 Genomic DNA. Translation: AAA97436.1. S81166 Genomic DNA. Translation: AAB35906.1.
IPI	IPI00027391.
PIR	OOHU. A41200.
RefSeq	NP_000530.1. NM_000539.3.
UniGene	Hs.247565.
3D structure databases
ProteinModelPortal	P08100.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08100. 3 interactions.
STRING	9606.ENSP00000296271.
Protein family/group databases
GPCRDB	Search...
PTM databases
GlycoSuiteDB	P08100.
PhosphoSite	P08100.
Polymorphism databases
DMDM	129207.
Proteomic databases
PaxDb	P08100.
PRIDE	P08100.
Protocols and materials databases
DNASU	6010.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296271; ENSP00000296271; ENSG00000163914.
GeneID	6010.
KEGG	hsa:6010.
UCSC	uc003emt.3. human.
Organism-specific databases
CTD	6010.
GeneCards	GC03P129247.
HGNC	HGNC:10012. RHO.
MIM	180380. gene. 610445. phenotype. 613731. phenotype.
neXtProt	NX_P08100.
Orphanet	215. Congenital stationary night blindness. 791. Retinitis pigmentosa. 52427. Retinitis punctata albescens.
PharmGKB	PA34390.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG311294.
HOGENOM	HOG000253932.
HOVERGEN	HBG107442.
InParanoid	P08100.
KO	K04250.
OMA	LAAYMFM.
OrthoDB	EOG4P5K9D.
PhylomeDB	P08100.
Enzyme and pathway databases
Pathway_Interaction_DB	rhodopsin_pathway. Visual signal transduction: Rods.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
Bgee	P08100.
CleanEx	HS_RHO.
Genevestigator	P08100.
GermOnline	ENSG00000163914. Homo sapiens.
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
DrugBank	DB01159. Halothane.
GenomeRNAi	6010.
NextBio	23449.
SOURCE	Search...

Entry information

Entry name

OPSD_HUMAN

Accession

Primary (citable) accession number: P08100
Secondary accession number(s): Q16414, Q2M249

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents