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P02699

- OPSD_BOVIN

UniProt

P02699 - OPSD_BOVIN

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Protein
Rhodopsin
Gene
RHO
Organism
Bos taurus (Bovine)
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 By similarity.2 Publications

Absorptioni

Abs(max)=495 nm

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011Zinc
Binding sitei265 – 2651Retinal chromophore
Metal bindingi279 – 2791Zinc

GO - Molecular functioni

  1. G-protein coupled photoreceptor activity Source: AgBase
  2. guanyl-nucleotide exchange factor activity Source: Reactome
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular response to light stimulus Source: Ensembl
  2. phototransduction, visible light Source: AgBase
  3. protein phosphorylation Source: Ensembl
  4. protein-chromophore linkage Source: UniProtKB-KW
  5. regulation of GTPase activity Source: GOC
  6. retina development in camera-type eye Source: Ensembl
  7. visual perception Source: UniProtKB-KW
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_203536. Opsins.
REACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_210568. G alpha (i) signalling events.
REACT_211562. Activation of the phototransduction cascade.
REACT_211834. The canonical retinoid cycle in rods (twilight vision).

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin
Gene namesi
Name:RHO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 22

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 – 3636Extracellular
Add
BLAST
Transmembranei37 – 6327Helical; Name=1
Add
BLAST
Topological domaini64 – 7310Cytoplasmic
Transmembranei74 – 9623Helical; Name=2
Add
BLAST
Topological domaini97 – 11014Extracellular
Add
BLAST
Transmembranei111 – 13323Helical; Name=3
Add
BLAST
Topological domaini134 – 15219Cytoplasmic
Add
BLAST
Transmembranei153 – 17321Helical; Name=4
Add
BLAST
Topological domaini174 – 20229Extracellular
Add
BLAST
Transmembranei203 – 22422Helical; Name=5
Add
BLAST
Topological domaini225 – 24925Cytoplasmic
Add
BLAST
Transmembranei250 – 27425Helical; Name=6
Add
BLAST
Topological domaini275 – 28612Extracellular
Add
BLAST
Transmembranei287 – 30822Helical; Name=7
Add
BLAST
Topological domaini309 – 34840Cytoplasmic
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. integral component of plasma membrane Source: AgBase
  3. photoreceptor disc membrane Source: Reactome
  4. photoreceptor inner segment membrane Source: UniProtKB
  5. photoreceptor outer segment membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21N → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-282 and D-15. 1 Publication
Mutagenesisi15 – 151N → D: Normal light absorption; when associated with C-2 and C-282. 1 Publication
Mutagenesisi282 – 2821D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Rhodopsin
PRO_0000197653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine
Glycosylationi2 – 21N-linked (GlcNAc...)3 Publications
Glycosylationi15 – 151N-linked (GlcNAc...)3 Publications
Disulfide bondi110 ↔ 1871 Publication
Modified residuei296 – 2961N6-(retinylidene)lysine
Lipidationi322 – 3221S-palmitoyl cysteine3 Publications
Lipidationi323 – 3231S-palmitoyl cysteine3 Publications
Modified residuei334 – 3341Phosphoserine By similarity
Modified residuei335 – 3351Phosphothreonine2 Publications
Modified residuei336 – 3361Phosphothreonine2 Publications
Modified residuei338 – 3381Phosphoserine By similarity
Modified residuei340 – 3401Phosphothreonine2 Publications
Modified residuei342 – 3421Phosphothreonine2 Publications
Modified residuei343 – 3431Phosphoserine; by RK and GRK73 Publications

Post-translational modificationi

Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.3 Publications
Contains one covalently linked retinal chromophore.

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

PTM databases

UniCarbKBiP02699.

Expressioni

Tissue specificityi

Rod shaped photoreceptor cells which mediates vision in dim light.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-29225N.
IntActiP02699. 3 interactions.
MINTiMINT-1507462.
STRINGi9913.ENSBTAP00000001730.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi10 – 134
Helixi15 – 173
Turni23 – 253
Turni29 – 313
Helixi34 – 6431
Helixi66 – 683
Helixi71 – 8919
Helixi91 – 10010
Helixi103 – 1053
Helixi106 – 13934
Beta strandi143 – 1453
Helixi150 – 16819
Helixi170 – 1723
Turni175 – 1773
Beta strandi179 – 1813
Turni182 – 1854
Beta strandi186 – 1883
Helixi192 – 1954
Helixi196 – 1983
Helixi200 – 21011
Helixi213 – 22311
Turni224 – 2285
Turni229 – 2313
Turni235 – 2384
Beta strandi239 – 2413
Helixi242 – 27736
Turni278 – 2803
Helixi285 – 29410
Helixi295 – 2995
Helixi301 – 3088
Helixi311 – 32111
Turni322 – 3243
Turni328 – 3303
Beta strandi332 – 3343
Beta strandi336 – 3383
Beta strandi339 – 3424

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOJmodel-A1-348[»]
1BOKmodel-A1-348[»]
1EDSNMR-A93-123[»]
1EDVNMR-A172-205[»]
1EDWNMR-A268-293[»]
1EDXNMR-A1-40[»]
1F88X-ray2.80A/B1-348[»]
1FDFNMR-A291-315[»]
1GZMX-ray2.65A/B1-348[»]
1HZXX-ray2.80A/B1-348[»]
1JFPNMR-A1-348[»]
1L9HX-ray2.60A/B1-348[»]
1LN6NMR-A1-348[»]
1N3Mmodel-A/B/C/D/E/F1-348[»]
1NZSNMR-A330-348[»]
1OV0model-A1-348[»]
1OV1model-A1-348[»]
1U19X-ray2.20A/B1-348[»]
1VQXNMR-A330-348[»]
2G87X-ray2.60A/B1-348[»]
2HPYX-ray2.80A/B1-348[»]
2I35X-ray3.80A1-348[»]
2I36X-ray4.10A/B/C1-348[»]
2I37X-ray4.15A/B/C1-348[»]
2IQKmodel-A1-348[»]
2J4YX-ray3.40A/B1-348[»]
2PEDX-ray2.95A/B1-348[»]
2X72X-ray3.00A1-348[»]
3C9LX-ray2.65A1-348[»]
3C9MX-ray3.40A1-348[»]
3CAPX-ray2.90A/B1-348[»]
3DQBX-ray3.20A1-348[»]
3OAXX-ray2.60A/B1-348[»]
3PQRX-ray2.85A1-348[»]
3PXOX-ray3.00A1-348[»]
4A4MX-ray3.30A1-348[»]
4BEYX-ray2.90A1-348[»]
4BEZX-ray3.30A1-348[»]
4J4QX-ray2.65A1-348[»]
DisProtiDP00271.
ProteinModelPortaliP02699.
SMRiP02699. Positions 1-348.

Miscellaneous databases

EvolutionaryTraceiP02699.

Family & Domainsi

Region

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

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.
InParanoidiP02699.
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.

P02699-1 [UniParc]FASTAAdd to Basket

« Hide

MNGTEGPNFY VPFSNKTGVV RSPFEAPQYY LAEPWQFSML AAYMFLLIML    50
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH 100
GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE 150
NHAIMGVAFT WVMALACAAP PLVGWSRYIP EGMQCSCGID YYTPHEETNN 200
ESFVIYMFVV HFIIPLIVIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV 250
TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SDFGPIFMTI PAFFAKTSAV 300
YNPVIYIMMN KQFRNCMVTT LCCGKNPLGD DEASTTVSKT ETSQVAPA 348
Length:348
Mass (Da):39,008
Last modified:July 21, 1986 - v1
Checksum:i33FDA196803E81F3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811S → F in AAA30675. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K00506
, K00502, K00503, K00504, K00505 Genomic DNA. Translation: AAA30674.1.
M21606 mRNA. Translation: AAA30675.1.
PIRiA90840. OOBO.
RefSeqiNP_001014890.1. NM_001014890.1.
UniGeneiBt.12753.

Genome annotation databases

EnsembliENSBTAT00000001730; ENSBTAP00000001730; ENSBTAG00000001310.
GeneIDi509933.
KEGGibta:509933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K00506
, K00502 , K00503 , K00504 , K00505 Genomic DNA. Translation: AAA30674.1 .
M21606 mRNA. Translation: AAA30675.1 .
PIRi A90840. OOBO.
RefSeqi NP_001014890.1. NM_001014890.1.
UniGenei Bt.12753.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BOJ model - A 1-348 [» ]
1BOK model - A 1-348 [» ]
1EDS NMR - A 93-123 [» ]
1EDV NMR - A 172-205 [» ]
1EDW NMR - A 268-293 [» ]
1EDX NMR - A 1-40 [» ]
1F88 X-ray 2.80 A/B 1-348 [» ]
1FDF NMR - A 291-315 [» ]
1GZM X-ray 2.65 A/B 1-348 [» ]
1HZX X-ray 2.80 A/B 1-348 [» ]
1JFP NMR - A 1-348 [» ]
1L9H X-ray 2.60 A/B 1-348 [» ]
1LN6 NMR - A 1-348 [» ]
1N3M model - A/B/C/D/E/F 1-348 [» ]
1NZS NMR - A 330-348 [» ]
1OV0 model - A 1-348 [» ]
1OV1 model - A 1-348 [» ]
1U19 X-ray 2.20 A/B 1-348 [» ]
1VQX NMR - A 330-348 [» ]
2G87 X-ray 2.60 A/B 1-348 [» ]
2HPY X-ray 2.80 A/B 1-348 [» ]
2I35 X-ray 3.80 A 1-348 [» ]
2I36 X-ray 4.10 A/B/C 1-348 [» ]
2I37 X-ray 4.15 A/B/C 1-348 [» ]
2IQK model - A 1-348 [» ]
2J4Y X-ray 3.40 A/B 1-348 [» ]
2PED X-ray 2.95 A/B 1-348 [» ]
2X72 X-ray 3.00 A 1-348 [» ]
3C9L X-ray 2.65 A 1-348 [» ]
3C9M X-ray 3.40 A 1-348 [» ]
3CAP X-ray 2.90 A/B 1-348 [» ]
3DQB X-ray 3.20 A 1-348 [» ]
3OAX X-ray 2.60 A/B 1-348 [» ]
3PQR X-ray 2.85 A 1-348 [» ]
3PXO X-ray 3.00 A 1-348 [» ]
4A4M X-ray 3.30 A 1-348 [» ]
4BEY X-ray 2.90 A 1-348 [» ]
4BEZ X-ray 3.30 A 1-348 [» ]
4J4Q X-ray 2.65 A 1-348 [» ]
DisProti DP00271.
ProteinModelPortali P02699.
SMRi P02699. Positions 1-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29225N.
IntActi P02699. 3 interactions.
MINTi MINT-1507462.
STRINGi 9913.ENSBTAP00000001730.

Chemistry

BindingDBi P02699.
ChEMBLi CHEMBL5739.

Protein family/group databases

GPCRDBi Search...

PTM databases

UniCarbKBi P02699.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000001730 ; ENSBTAP00000001730 ; ENSBTAG00000001310 .
GeneIDi 509933.
KEGGi bta:509933.

Organism-specific databases

CTDi 6010.

Phylogenomic databases

eggNOGi NOG311294.
GeneTreei ENSGT00710000106574.
HOGENOMi HOG000253932.
HOVERGENi HBG107442.
InParanoidi P02699.
KOi K04250.
OMAi LAAYMFM.
OrthoDBi EOG72NRQJ.
TreeFami TF324998.

Enzyme and pathway databases

Reactomei REACT_203536. Opsins.
REACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_210568. G alpha (i) signalling events.
REACT_211562. Activation of the phototransduction cascade.
REACT_211834. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

EvolutionaryTracei P02699.
NextBioi 20869202.

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

  1. "Rhodopsin and bacteriorhodopsin: structure-function relationships."
    Ovchinnikov Y.A.
    FEBS Lett. 148:179-191(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, RETINAL-BINDING SITE AT LYS-296.
  2. "Isolation, sequence analysis, and intron-exon arrangement of the gene encoding bovine rhodopsin."
    Nathans J., Hogness D.S.
    Cell 34:807-814(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Multiple opsin mRNA species in bovine retina."
    Kuo C.-H., Yamagata K., Moyzis R.K., Bitensky M.W., Miki N.
    Brain Res. 387:251-260(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-348.
  4. "Isolation and nucleotide sequence of a partial cDNA clone for bovine opsin."
    Koike S., Nabeshima Y., Ogata K., Fukui T., Ohtsuka E., Ikehara M., Tokunaga F.
    Biochem. Biophys. Res. Commun. 116:563-567(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-348.
  5. "Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin."
    Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B., Galijatovic A., Chen N., Crouch R.K., Knapp D.R.
    Protein Sci. 7:758-764(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Retina.
  6. "Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus."
    Fukuda M.N., Papermaster D.S., Hargrave P.A.
    J. Biol. Chem. 254:8201-8207(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-2 AND ASN-15.
  7. "Structural studies on membrane-bound bovine rhodopsin."
    Mullen E., Akhtar M.
    Biochem. J. 211:45-54(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETINAL-BINDING SITE.
  8. "Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated."
    Ovchinnikov Y.A., Abdulaev N.G., Bogachuk A.S.
    FEBS Lett. 230:1-5(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
  9. "Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187."
    Karnik S.S., Khorana H.G.
    J. Biol. Chem. 265:17520-17524(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  10. "Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin."
    Brown N.G., Fowles C., Sharma R., Akhtar M.
    Eur. J. Biochem. 208:659-667(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-343.
  11. "Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry."
    Papac D.I., Thornburg K.R., Buellesbach E.E., Crouch R.K., Knapp D.R.
    J. Biol. Chem. 267:16889-16894(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-322 AND CYS-323.
  12. "Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops."
    Cai K., Langen R., Hubbell W.L., Khorana H.G.
    Proc. Natl. Acad. Sci. U.S.A. 94:14267-14272(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  14. "Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)."
    Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E.
    Biochemistry 40:7761-7772(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE AND ZINC ION, PALMITOYLATION AT CYS-322 AND CYS-323, GLYCOSYLATION AT ASN-2 AND ASN-15.
  15. "Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms."
    Yeagle P.L., Choi G., Albert A.D.
    Biochemistry 40:11932-11937(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
  16. "Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin."
    Choi G., Landin J., Galan J.F., Birge R.R., Albert A.D., Yeagle P.L.
    Biochemistry 41:7318-7324(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN INACTIVATED AND ACTIVATED FORMS.
  17. "Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography."
    Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y.
    Proc. Natl. Acad. Sci. U.S.A. 99:5982-5987(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  18. "The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin."
    Kisselev O.G., McDowell J.H., Hargrave P.A.
    FEBS Lett. 564:307-311(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
  19. "Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions."
    Kisselev O.G., Downs M.A., McDowell J.H., Hargrave P.A.
    J. Biol. Chem. 279:51203-51207(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 330-348 IN COMPLEX WITH THE INHIBITOR VISUAL ARRESTIN, PHOSPHORYLATION AT SER-334; THR-335; THR-336; SER-338; THR-340; THR-342 AND SER-343.
  20. "The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure."
    Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., Buss V.
    J. Mol. Biol. 342:571-583(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  21. "Structure of bovine rhodopsin in a trigonal crystal form."
    Li J., Edwards P.C., Burghammer M., Villa C., Schertler G.F.
    J. Mol. Biol. 343:1409-1438(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
  22. "Structure of the third cytoplasmic loop of bovine rhodopsin."
    Yeagle P.L., Alderfer J.L., Albert A.D.
    Biochemistry 34:14621-14625(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 231-252.
  23. "Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin."
    Yeagle P.L., Salloum A., Chopra A., Bhawsar N., Ali L., Kuzmanovski G., Alderfer J.L., Albert A.D.
    J. Pept. Res. 55:455-465(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-40; 93-123; 172-205 AND 268-293.
  24. "Three dimensional structure of the seventh transmembrane helical domain of the G-protein receptor, rhodopsin."
    Yeagle P.L., Danis C., Choi G., Alderfer J.L., Albert A.D.
    Mol. Vis. 6:125-131(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 291-315.
  25. "Crystallographic analysis of primary visual photochemistry."
    Nakamichi H., Okada T.
    Angew. Chem. Int. Ed. 45:4270-4273(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RETINAL CHROMOPHORE.
  26. "Local peptide movement in the photoreaction intermediate of rhodopsin."
    Nakamichi H., Okada T.
    Proc. Natl. Acad. Sci. U.S.A. 103:12729-12734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
  27. Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS, FUNCTION.
  28. "Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography."
    Nakamichi H., Buss V., Okada T.
    Biophys. J. 92:L106-L108(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) INACTIVATED AND ACTIVATED FORMS IN COMPLEX WITH RETINAL CHROMOPHORE.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-348, MUTAGENESIS OF ASN-2; ASN-15 AND ASP-282.
  30. "Alternative models for two crystal structures of bovine rhodopsin."
    Stenkamp R.E.
    Acta Crystallogr. D 64:902-904(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
  31. "Crystal structure of the ligand-free G-protein-coupled receptor opsin."
    Park J.H., Scheerer P., Hofmann K.P., Choe H.-W., Ernst O.P.
    Nature 454:183-187(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), DIMERIZATION.
  32. "Crystal structure of opsin in its G-protein-interacting conformation."
    Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.-W., Hofmann K.P., Ernst O.P.
    Nature 455:497-502(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), ACTIVATION MECHANISM.

Entry informationi

Entry nameiOPSD_BOVIN
AccessioniPrimary (citable) accession number: P02699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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