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P08100 (OPSD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhodopsin
Alternative name(s):
Opsin-2
Gene names
Name:RHO
Synonyms:OPN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

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

Night blindness, congenital stationary, 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 processSensory transduction
Vision
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseCongenital stationary night blindness
Disease mutation
Retinitis pigmentosa
   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_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 2218504. Source: ProtInc

phototransduction, visible light

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

red, far-red light phototransduction

Inferred from electronic annotation. Source: Ensembl

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11767049. Source: MGI

integral component of plasma membrane

Traceable author statement PubMed 8253795. Source: ProtInc

photoreceptor disc membrane

Traceable author statement. Source: Reactome

photoreceptor inner segment

Inferred from direct assay PubMed 11767049. Source: MGI

photoreceptor inner segment membrane

Inferred from direct assay Ref.33. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay PubMed 11767049. Source: MGI

photoreceptor outer segment membrane

Inferred from direct assay Ref.33. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: LIFEdb

rough endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-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: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZFYVE9O954052EBI-1394177,EBI-296817

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Rhodopsin
PRO_0000197677

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 By similarity
Modified residue3361Phosphothreonine By similarity
Modified residue3381Phosphoserine By similarity
Modified residue3401Phosphothreonine By similarity
Modified residue3421Phosphothreonine By similarity
Modified residue3431Phosphoserine By similarity
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

Natural variations

Natural variant41T → K in RP4.
VAR_004765
Natural variant151N → S in RP4. Ref.18
VAR_004766
Natural variant171T → M in RP4. Ref.11 Ref.16
VAR_004767
Natural variant231P → 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 variant231P → L in RP4.
VAR_004769
Natural variant281Q → H in RP4.
VAR_004770
Natural variant401L → R in RP4. Ref.25
VAR_004771
Natural variant441M → T in RP4. Ref.21
VAR_004772
Natural variant451F → L in RP4.
Corresponds to variant rs104893770 [ dbSNP | Ensembl ].
VAR_004773
Natural variant461L → R in RP4.
VAR_004774
Natural variant511G → A. Ref.17
Corresponds to variant rs149079952 [ dbSNP | Ensembl ].
VAR_004775
Natural variant511G → R in RP4.
VAR_004776
Natural variant511G → V in RP4.
VAR_004777
Natural variant531P → R in RP4.
Corresponds to variant rs28933395 [ dbSNP | Ensembl ].
VAR_004778
Natural variant581T → R in RP4. Ref.9 Ref.11
Corresponds to variant rs28933394 [ dbSNP | Ensembl ].
VAR_004779
Natural variant68 – 714Missing in RP4.
VAR_004780
Natural variant871V → D in RP4.
VAR_004781
Natural variant891G → D in RP4.
VAR_004782
Natural variant901G → D in CSNBAD1. Ref.29
VAR_004783
Natural variant941T → I in CSNBAD1. Ref.32
VAR_004784
Natural variant1041V → I. Ref.17
Corresponds to variant rs144317206 [ dbSNP | Ensembl ].
VAR_004785
Natural variant1061G → R in RP4. Ref.17
Corresponds to variant rs28933994 [ dbSNP | Ensembl ].
VAR_004786
Natural variant1061G → W in RP4.
VAR_004787
Natural variant1091G → R in RP4. Ref.31
VAR_004788
Natural variant1101C → F in RP4. Ref.22
VAR_004789
Natural variant1101C → Y in RP4.
VAR_004790
Natural variant1141G → D in RP4.
VAR_004791
Natural variant1251L → R in RP4.
VAR_004792
Natural variant1271S → F in RP4. Ref.24
VAR_004793
Natural variant1311L → P in RP4. Ref.22 Ref.24
VAR_004794
Natural variant1351R → G in RP4. Ref.17
VAR_004795
Natural variant1351R → L in RP4.
VAR_004796
Natural variant1351R → W in RP4. Ref.30 Ref.35
VAR_004797
Natural variant1401C → S in RP4. Ref.17
VAR_004798
Natural variant1501E → K in RP4; autosomal recessive. Ref.27 Ref.34
VAR_004799
Natural variant1641A → E in RP4.
VAR_004800
Natural variant1641A → V in RP4. Ref.22
VAR_004801
Natural variant1671C → R in RP4.
VAR_004802
Natural variant1711P → L in RP4.
VAR_004803
Natural variant1711P → Q in RP4. Ref.23
VAR_004804
Natural variant1711P → S in RP4.
VAR_004805
Natural variant1781Y → C in RP4.
VAR_004806
Natural variant1781Y → N in RP4. Ref.24
VAR_004807
Natural variant1801P → S in RP4. Ref.35
VAR_068359
Natural variant1811E → K in RP4.
VAR_004808
Natural variant1821G → S in RP4. Ref.11
VAR_004809
Natural variant1861S → P in RP4.
VAR_004810
Natural variant1881G → E in RP4. Ref.17
VAR_004811
Natural variant1881G → R in RP4.
VAR_004812
Natural variant1901D → G in RP4.
VAR_004814
Natural variant1901D → N in RP4.
Corresponds to variant rs28933992 [ dbSNP | Ensembl ].
VAR_004813
Natural variant1901D → Y in RP4.
VAR_004815
Natural variant2071M → R in RP4. Ref.15
Corresponds to variant rs28933995 [ dbSNP | Ensembl ].
VAR_004816
Natural variant2091V → M Effect not known. Ref.17
VAR_004817
Natural variant2111H → P in RP4.
Corresponds to variant rs28933993 [ dbSNP | Ensembl ].
VAR_004818
Natural variant2111H → R in RP4. Ref.17
VAR_004819
Natural variant2141I → N in RP4. Ref.35
VAR_068360
Natural variant2161M → K in RP4. Ref.25
VAR_004820
Natural variant2201F → C in RP4.
VAR_004821
Natural variant2221C → R in RP4.
VAR_004822
Natural variant2551Missing in RP4. Ref.10
VAR_004823
Natural variant2641Missing in RP4.
VAR_004824
Natural variant2671P → L in RP4. Ref.11
VAR_004825
Natural variant2671P → R in RP4. Ref.24
VAR_004826
Natural variant2921A → E in CSNBAD1. Ref.19
VAR_004827
Natural variant2961K → E in RP4.
Corresponds to variant rs29001653 [ dbSNP | Ensembl ].
VAR_004828
Natural variant2971S → R in RP4. Ref.24
VAR_004829
Natural variant3421T → M in RP4.
VAR_004830
Natural variant3451V → L in RP4. Ref.26
VAR_004831
Natural variant3451V → M in RP4.
VAR_004832
Natural variant3471P → A in RP4. Ref.28
VAR_004833
Natural variant3471P → L in RP4; common variant. Ref.9 Ref.16
VAR_004834
Natural variant3471P → Q in RP4.
VAR_004835
Natural variant3471P → R in RP4. Ref.12
Corresponds to variant rs29001566 [ dbSNP | Ensembl ].
VAR_004836
Natural variant3471P → S in RP4. Ref.9
Corresponds to variant rs29001637 [ dbSNP | Ensembl ].
VAR_004837

Sequences

Sequence LengthMass (Da)Tools
P08100 [UniParc].

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

FASTA34838,893
        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 

« Hide

References

« Hide '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. expand/collapse author list , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., 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.
PIROOHU. A41200.
RefSeqNP_000530.1. NM_000539.3.
UniGeneHs.247565.

3D structure databases

ProteinModelPortalP08100.
SMRP08100. Positions 1-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111942. 13 interactions.
IntActP08100. 3 interactions.
STRING9606.ENSP00000296271.

Chemistry

DrugBankDB01159. Halothane.

Protein family/group databases

TCDB9.A.14.1.2. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP08100.
UniCarbKBP08100.

Polymorphism databases

DMDM129207.

Proteomic databases

PaxDbP08100.
PRIDEP08100.

Protocols and materials databases

DNASU6010.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296271; ENSP00000296271; ENSG00000163914.
GeneID6010.
KEGGhsa:6010.
UCSCuc003emt.3. human.

Organism-specific databases

CTD6010.
GeneCardsGC03P129247.
HGNCHGNC:10012. RHO.
MIM180380. gene.
610445. phenotype.
613731. phenotype.
neXtProtNX_P08100.
Orphanet215. Congenital stationary night blindness.
791. Retinitis pigmentosa.
52427. Retinitis punctata albescens.
PharmGKBPA34390.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311294.
HOGENOMHOG000253932.
HOVERGENHBG107442.
InParanoidP08100.
KOK04250.
OMALAAYMFM.
OrthoDBEOG72NRQJ.
PhylomeDBP08100.
TreeFamTF324998.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP08100.

Gene expression databases

BgeeP08100.
CleanExHS_RHO.
GenevestigatorP08100.

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

GeneWikiRhodopsin.
GenomeRNAi6010.
NextBio23449.
PROP08100.
SOURCESearch...

Entry information

Entry nameOPSD_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries