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P02699

- OPSD_BOVIN

UniProt

P02699 - OPSD_BOVIN

Protein

Rhodopsin

Gene

RHO

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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.By similarity

    Absorptioni

    Abs(max)=495 nm

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi201 – 2011Zinc
    Binding sitei265 – 2651Retinal chromophore3 Publications
    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. positive regulation of GTPase activity Source: GOC
    4. protein-chromophore linkage Source: UniProtKB-KW
    5. protein phosphorylation Source: Ensembl
    6. retina development in camera-type eye Source: Ensembl
    7. visual perception Source: UniProtKB-KW

    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

    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

    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. 2 Publications
    Mutagenesisi15 – 151N → D: Normal light absorption; when associated with C-2 and C-282. 2 Publications
    Mutagenesisi282 – 2821D → C: Stabilized by a disulfide bond and normal light absorption; when associated with C-2 and D-15. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348RhodopsinPRO_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 PublicationPROSITE-ProRule annotation
    Modified residuei296 – 2961N6-(retinylidene)lysine
    Lipidationi322 – 3221S-palmitoyl cysteine3 Publications
    Lipidationi323 – 3231S-palmitoyl cysteine3 Publications
    Modified residuei334 – 3341PhosphoserineBy similarity
    Modified residuei335 – 3351Phosphothreonine2 Publications
    Modified residuei336 – 3361Phosphothreonine2 Publications
    Modified residuei338 – 3381PhosphoserineBy 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.5 Publications

    Protein-protein interaction databases

    BioGridi166570. 2 interactions.
    DIPiDIP-29225N.
    IntActiP02699. 3 interactions.
    MINTiMINT-1507462.
    STRINGi9913.ENSBTAP00000001730.

    Structurei

    Secondary structure

    1
    348
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02699.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3636ExtracellularAdd
    BLAST
    Topological domaini64 – 7310Cytoplasmic
    Topological domaini97 – 11014ExtracellularAdd
    BLAST
    Topological domaini134 – 15219CytoplasmicAdd
    BLAST
    Topological domaini174 – 20229ExtracellularAdd
    BLAST
    Topological domaini225 – 24925CytoplasmicAdd
    BLAST
    Topological domaini275 – 28612ExtracellularAdd
    BLAST
    Topological domaini309 – 34840CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei37 – 6327Helical; Name=1Add
    BLAST
    Transmembranei74 – 9623Helical; Name=2Add
    BLAST
    Transmembranei111 – 13323Helical; Name=3Add
    BLAST
    Transmembranei153 – 17321Helical; Name=4Add
    BLAST
    Transmembranei203 – 22422Helical; Name=5Add
    BLAST
    Transmembranei250 – 27425Helical; Name=6Add
    BLAST
    Transmembranei287 – 30822Helical; Name=7Add
    BLAST

    Family & Domainsi

    Region

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi134 – 1374'Ionic lock' involved in activated form stabilization

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811S → F in AAA30675. (PubMed:2950966)Curated

    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

    BioGridi 166570. 2 interactions.
    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: October 1, 2014
    This is version 157 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