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14-September-2008 18:02:44 - Rhodopsin This article is about the visual rhodopsin of vertebrates. For other types of rhodopsin, see retinylidene protein. Rhodopsin opsin 2, rod pigment retinitis pigmentosa 4, autosomal dominant Sensory rhodopsin II rainbow colored embedded in a lipid bilayer heads red and tails blue with Transducin below it. Gtα is colored red, Gtβ blue, and Gtγ yellow. There is a bound GDP molecule in the Gtα-subunit and a bound retinal black in the rhodopsin. The N-terminus terminus of rhodopsin is red and the C-terminus blue. Presumed anchoring of transducin to the membrane has been drawn in black. Available structures: 1eds, 1edx, 1f88, 1gzm, 1hzx, 1jfp, 1l9h, 1ln6, 1u19, 2g87, 2hpy, 2i35, 2i36, 2i37 Identifiers Symbols RHO; MGC138309; MGC138311; OPN2; RP4 External IDs OMIM: 180380 MGI: 97914 HomoloGene: 68068 Gene ontology Molecular function: rhodopsin-like receptor activity receptor activity Cellular component: photoreceptor outer segment plasma membrane integral to plasma membrane Biological process: G-protein coupled receptor protein signaling pathway visual perception phototransduction, visible light rhodopsin mediated signaling protein-chromophore linkage response to stimulus RNA expression pattern More reference expression data Orthologs Human Mouse Entrez 6010 212541 Ensembl ENSG00000163914 ENSMUSG00000030324 Uniprot P08100 Q8K0D8 Refseq NM_000539 mRNA NP_000530 protein NM_145383 mRNA NP_663358 protein Location Chr 3: 130.73 - 130.74 Mb Chr 6: 115.9 - 115.9 Mb Pubmed search 1 2 Rhodopsin, also known as visual purple, is a pigment of the retina that is responsible for both the formation of the photoreceptor cells and the first events in the perception of light. Rhodopsins belong to the G-protein coupled receptor family and are extremely sensitive to light, enabling vision in low-light conditions. Exposed to white light, the pigment immediately photobleaches, and it takes about 30 minutes to regenerate fully in humans. Contents 1 Structure 2 Rhodopsin and retinal disease 3 Microbial rhodopsins 4 References 5 Further reading 6 External links Structure Rhodopsin consists of the protein moiety opsin and a reversibly covalently bound cofactor, retinal. Opsin, a bundle of seven transmembrane helices, binds retinal, a photoreactive chromophore, in a central pocket. Retinal is produced in the retina from Vitamin A. Isomerization of 11-cis-retinal into all-trans-retinal by light induces a conformational change in opsin that activates the associated G protein and triggers a second messenger cascade. Rhodopsin of the rods most strongly absorbs green-blue light and therefore appears reddish-purple, which is why it is also called visual purple. It is responsible for monochromatic vision in the dark. Bovine rhodopsin Bovine rhodopsin Several closely related opsins, the photopsins, exist that differ only in a few amino acids and in the wavelengths of light that they absorb most strongly. These pigments are found in the different types of the cone cells of the retina and are the basis of color vision. Humans have three different other opsins beside rhodopsin, with absorption maxima for yellowish-green photopsin I, green photopsin II, and bluish-violet photopsin III light. The photoisomerization of rhodopsin has been studied in detail via x-ray crystallography on rhodopsin crystals. A first photoproduct called photorhodopsin forms within 200 femtoseconds after irradiation followed within picoseconds by a second one called bathorhodopsin with distorted all-trans bonds. This intermediate can be trapped and studied at cryogenic temperatures. Several models e.g. the bicycle-pedal mechanism, hula-twist mechanism attempt to explain how the retinal group can change its conformation without clashing with the enveloping rhodopsin protein pocket.123 Rhodopsin and retinal disease Mutation of the rhodopsin gene is a major contributor to various retinopathies such as retinitis pigmentosa. The disease-causing protein generally aggregates with ubiquitin in inclusion bodies, disrupts the intermediate filament network and impairs the ability of the cell to degrade non-functioning proteins which leads to photoreceptor apoptosis.4 Other mutations on rhodopsin lead to X-linked congenital stationary night blindness, mainly due to constitutive activation, when the mutations occur around the chromophore binding pocket of rhodopsin.5 Several other pathological states relating to rhodopsin have been discovered including poor post-Golgi trafficking, dysregulative activation, rod outer segment instability and arrestin binding.5 Microbial rhodopsins Main article: Bacterial rhodopsins Some prokaryotes express proton pumps called bacteriorhodopsin, proteorhodopsin, xanthorhodopsin to carry out phototrophy.6 Like rhodopsin, these contain retinal and have seven transmembrane alpha helices; however they are not coupled to a G protein. Bacterial halorhodopsin is a light-activated chloride pump.6 Finally, an alga is known to have an opsin that contains its own monolithic light-gated ion channel, channelrhodopsin. While bacteriorhodopsin, halorhodopsin, and channelrhodopsin all have significant sequence homology to one another, they have no detectable sequence identity to G-protein coupled receptor GPCR family where rhodopsins belong. Nevertheless, bacterial rhodopsins and GPCR are possibly evolutionary related, based on similarity of their three-dimensional structures. Therefore, they have been assigned to the same superfamily in Structural Classification of Proteins.7 References ^ Nakamichi H, Okada T June 2006. Crystallographic analysis of primary visual photochemistry. Angew. Chem. Int. Ed. Engl. 45 26: 4270-3. doi:10.1002/anie.200600595. PMID 16586416. ^ Schreiber M, Sugihara M, Okada T, Buss V June 2006. Quantum mechanical studies on the crystallographic model of bathorhodopsin. Angew. Chem. Int. Ed. Engl. 45 26: 4274-7. doi:10.1002/anie.200600585. PMID 16729349. ^ Weingart O September 2007. The twisted C11-C12 bond of the rhodopsin chromophore--a photochemical hot spot. J. Am. Chem. Soc. 129 35: 10618-9. doi:10.1021/ja071793t. PMID 17691730. ^ Saliba RS, Munro PM, Luthert PJ, Cheetham ME July 2002. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J. Cell. Sci. 115 Pt 14: 2907-18. PMID 12082151. ^ a b Mendes HF, van der Spuy J, Chapple JP, Cheetham ME April 2005. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol Med 11 4: 177-85. doi:10.1016/j.molmed.2005.02.007. PMID 15823756. ^ a b Bryant DA, Frigaard NU November 2006. Prokaryotic photosynthesis and phototrophy illuminated. Trends Microbiol. 14 11: 488-96. doi:10.1016/j.tim.2006.09.001. PMID 16997562. ^ http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.g.e.b.html. Further reading Humphries P, Kenna P, Farrar GJ 1992. On the molecular genetics of retinitis pigmentosa.. Science 256 5058: 804-8. doi:10.1126/science.1589761. PMID 1589761. Edwards SC 1995. Involvement of cGMP and calcium in the photoresponse in vertebrate photoreceptor cells.. The Journal of the Florida Medical Association 82 7: 485-8. PMID 7673885. al-Maghtheh M, Gregory C, Inglehearn C, et al. 1993. Rhodopsin mutations in autosomal dominant retinitis pigmentosa.. Hum. Mutat. 2 4: 249-55. doi:10.1002/humu.1380020403. PMID 8401533. Garriga P, Manyosa J 2002. The eye photoreceptor protein rhodopsin. Structural implications for retinal disease.. FEBS Lett. 528 1-3: 17-22. doi:10.1016/S0014-57930203241-6. PMID 12297272. Mendes HF, van der Spuy J, Chapple JP, Cheetham ME 2005. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy.. Trends in molecular medicine 11 4: 177-85. doi:10.1016/j.molmed.2005.02.007. PMID 15823756. Inglehearn CF, Keen TJ, Bashir R, et al. 1993. A completed screen for mutations of the rhodopsin gene in a panel of patients with autosomal dominant retinitis pigmentosa.. Hum. Mol. Genet. 1 1: 41-5. PMID 1301135. Farrar GJ, Findlay JB, Kumar-Singh R, et al. 1993. Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin gene in the original 3q linked family.. Hum. Mol. Genet. 1 9: 769-71. PMID 1302614. Robinson PR, Cohen GB, Zhukovsky EA, Oprian DD 1992. Constitutively active mutants of rhodopsin.. Neuron 9 4: 719-25. doi:10.1016/0896-62739290034-B. PMID 1356370. Fujiki K, Hotta Y, Hayakawa M, et al. 1992. Point mutations of rhodopsin gene found in Japanese families with autosomal dominant retinitis pigmentosa ADRP.. Jpn. J. Hum. Genet. 37 2: 125-32. doi:10.1007/BF01899733. PMID 1391967. Olsson JE, Gordon JW, Pawlyk BS, et al. 1992. Transgenic mice with a rhodopsin mutation Pro23His: a mouse model of autosomal dominant retinitis pigmentosa.. Neuron 9 5: 815-30. doi:10.1016/0896-62739290236-7. PMID 1418997. Andréasson S, Ehinger B, Abrahamson M, Fex G 1993. A six-generation family with autosomal dominant retinitis pigmentosa and a rhodopsin gene mutation arginine-135-leucine.. Ophthalmic paediatrics and genetics 13 3: 145-53. PMID 1484692. Inglehearn CF, Lester DH, Bashir R, et al. 1992. Recombination between rhodopsin and locus D3S47 C17 in rhodopsin retinitis pigmentosa families.. Am. J. Hum. Genet. 50 3: 590-7. PMID 1539595. Fishman GA, Stone EM, Gilbert LD, Sheffield VC 1992. Ocular findings associated with a rhodopsin gene codon 106 mutation. Glycine-to-arginine change in autosomal dominant retinitis pigmentosa.. Arch. Ophthalmol. 110 5: 646-53. PMID 1580841. Keen TJ, Inglehearn CF, Lester DH, et al. 1992. Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal attachment site.. Genomics 11 1: 199-205. PMID 1765377. Dryja TP, Hahn LB, Cowley GS, et al. 1991. Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa.. Proc. Natl. Acad. Sci. U.S.A. 88 20: 9370-4. doi:10.1073/pnas.88.20.9370. PMID 1833777. Gal A, Artlich A, Ludwig M, et al. 1992. Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa.. Genomics 11 2: 468-70. PMID 1840561. Sung CH, Davenport CM, Hennessey JC, et al. 1991. Rhodopsin mutations in autosomal dominant retinitis pigmentosa.. Proc. Natl. Acad. Sci. U.S.A. 88 15: 6481-5. PMID 1862076. Jacobson SG, Kemp CM, Sung CH, Nathans J 1991. Retinal function and rhodopsin levels in autosomal dominant retinitis pigmentosa with rhodopsin mutations.. Am. J. Ophthalmol. 112 3: 256-71. PMID 1882937. Sheffield VC, Fishman GA, Beck JS, et al. 1991. Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-clamped denaturing gradient gel electrophoresis.. Am. J. Hum. Genet. 49 4: 699-706. PMID 1897520. External links Wikimedia Commons has media related to: Rhodopsins The Rhodopsin Protein Photoisomerization of rhodopsin, animation. Rhodopsin and the eye, summary with pictures. UMich Orientation of Proteins in Membranes families/superfamily-6 - Calculated spatial positions of rhodopsin-like proteins in membrane MeSH Rhodopsin v d e Transmembrane receptor: G protein-coupled receptors Class A: Rhodopsin like Adrenergic α1 A, B, D, α2 A, B, C, β1, β2, β3 Eicosanoid CysLT 1, 2, LTB4 1, 2, FPRL1, OXE, Prostaglandin DP, EP 1, 2, 3, 4, PGF, Prostacyclin, Thromboxane Neuropeptide B/W 1, 2, FF 1, 2, S, Y 1, 2, 4, 5 Orphan GPR 1, 3, 4, 6, 12, 15, 17, 18, 19, 20, 21, 22, 23, 25, 26, 27, 31, 32, 33, 34, 35, 37, 39, 42, 44, 45, 50, 52, 55, 61, 62, 63, 65, 68, 75, 77, 78, 79, 82, 83, 84, 85, 87, 88, 92, 101, 103, 119, 120, 132, 135, 139, 141, 142, 146, 148, 149, 150, 151, 152, 153, 160, 161, 162, 171, 172, 173, 174, 176, 177, 182 Purinergics Adenosine A1, A2a, A2b, A3, P2Y, 1, 2, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14 Serotonin all but 5-HT3 5-HT1 A, B, D, E, F, 5-HT2 A, B, C, 5-HT 4, 5A, 6, 7 Other Acetylcholine M1, M2, M3, M4, M5 - Adrenomedullin - Anaphylatoxin C3a, C5a - Angiotensin 1, 2 - Apelin - Bile acid - Bombesin BRS3, GRPR, NMBR - Bradykinin B1, B2 - Cannabinoid CB1, CB2 - Chemokine - Cholecystokinin A, B - Dopamine D1, D2, D3, D4, D5 - EBI2 - Endothelin A, B - Estrogen - Formyl peptide 1, L1, L2 - Free fatty acid 1, 2, 3, 4 - FSH - Galanin 1, 2, 3 - Gonadotropin-releasing hormone 1, 2 - Ghrelin - Histamine H1, H2, H3, H4 - Kisspeptin - Luteinizing hormone/choriogonadotropin - Lysophospholipid 1, 2, 3, 4, 5, 6, 7, 8 - MAS 1, 1L, D, E, F, G, X1, X2, X3, X4 - Melanocortin 1, 2, 3, 4, 5 - MCHR 1, 2 - Melatonin 1A, 1B- Motilin - neuromedin B, U 1, 2 - Neurotensin 1, 2 - Opioid Delta, Kappa, Mu, Nociceptin, but not Sigma - Olfactory - Opsin 3, 4, 5, 1LW, 1MW, 1SW, RGR, RRH - Orexin 1, 2 - Oxytocin - Oxoglutarate - PAF - Prokineticin 1, 2 - Prolactin-releasing peptide - Protease-activated 1, 2, 3, 4 - Relaxin 1, 2, 3, 4 - Somatostatin 1, 2, 3, 4, 5 - SREB - Succinate - TAAR 1, 2, 3, 5, 6, 8, 9 - Tachykinin 1, 2, 3 - Thyrotropin - Thyrotropin-releasing hormone - Urotensin-II - Vasopressin 1A, 1B, 2 Class B: Secretin like Brain-specific angiogenesis inhibitor 1, 2, 3 - Cadherin 1, 2, 3 - Calcitonin - CD97 - Corticotropin-releasing hormone 1, 2 - EMR 1, 2, 3 - Glucagon GR, GIPR, GLP1R, GLP2R - Growth hormone releasing hormone - PACAPR1- GPR 56, 64, 97, 98, 110, 111, 112, 113, 114, 115, 116, 123, 124, 125, 126, 128, 133, 143, 144, 157 - Latrophilin 1, 2, 3, ELTD1 - Parathyroid hormone 1, 2 - Secretin - Vasoactive intestinal peptide 1, 2 Class C: Metabotropic glutamate / pheromone Calcium-sensing receptor - GABA B 1, 2 - Glutamate receptor Metabotropic glutamate 1, 2, 3, 4, 5, 6, 7, 8 - GPRC6A - GPR 156, 158, 179 - RAIG 1, 2, 3, 4 - Taste receptors TAS1R 1, 2, 3 TAS2R 1, 3, 4, 5, 8, 9, 10, 12, 13, 14, 16, 38, 39, 40, 41, 43, 44, 45, 46, 47, 48, 49, 50 Frizzled / Smoothened Frizzled 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 - Smoothened v d e Eye proteins Opsin retinylidene protein Rhodopsin - Melanopsin - Photopsin Crystallin Alpha crystallin Other Arrestin - Guanylate cyclase activator - Recoverin - Rhodopsin kinase Retrieved from http://en..org/wiki/Rhodopsin Categories: Genes on chromosome 3 | Human proteins | G protein coupled receptors | Sensory receptors | Pigments | Eye Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages العربية Català Česky Dansk Deutsch Español Français Hrvatski Italiano עברית Lietuvių Nederlands 日本語 Polski Português РуÑ?Ñ?кий Suomi УкраїнÑ?ька This page was last modified on 22 July 2008, at 07:17
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