RRH
RRH | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | RRH,retinal pigment epithelium-derived rhodopsin homolog | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM:605224;MGI:1097709;HomoloGene:55977;GeneCards:RRH;OMA:RRH - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Peropsin,a visual pigment-like receptor, is aproteinthat in humans is encoded by theRRHgene.[5][6]It belongs like other animalopsinsto theG protein-coupled receptors.[6]Even so, the first peropsins were already discovered inmiceandhumansin 1997,[5]not much is known about them.[7]
Photochemistry
[edit]Like most opsins, peropsins have in its seventhtransmembrane domainalysinecorresponding toamino acidposition 296 incattlerhodopsin,[5][7]which is important for retinal binding and light sensing.[8]
Inamphioxus,acephalochordate,a peropsin binds in the dark-state all-trans-retinalinstead of 11-cis-retinal,[9]as it is in cattle rhodopsin.[10][11][12][13][14]Therefore, peropsins have been suggested to be photoisomerases.[9]
Tissue localization
[edit]In mice, a peropsin is localized to the apicalmicrovilliof theretinal pigment epithelium(RPE).[5]There, it regulates storage or the movement ofvitamin Afrom theretinato the RPE.[15]A peropsin is also expressed inkeratinocytesof the humanskin.In keratinocytecell culture,it reacts toUV lightif retinal is supplied.[16]Inchicken,a peropsin is expressed with an RGR-opsin in thepineal glandand the retina.[17]
Gene localization and structure
[edit]The human peropsin gene lies onchromosome4 band 4q25 and has sixintrons[6][18]like RGR-opsins. However only two of these introns are inserted at the same place, which still indicates that peropsins and RGR-opsins are more closely related to each other than to the ciliary and rhabdomeric opsins.[18]This shared gene structure is also reflected in opsin phylogenies, where peropsins and RGR-opsins are in the same group: The chromopsins.[18][7][19][20]
Phylogeny
[edit]The peropsins are restricted to thecraniatesand the cephalochordates.[7]Thecraniatesare thetaxonthat containsmammalsand with them humans. The peropsins are one of the seven subgroups of the chromopsins. The other groups are theRGR-opsins,theretinochromes,the nemopsins, the astropsins, the varropsins, and the gluopsins.[7]The chromopsins are one of three subgroups of the tetraopsins (also known as RGR/Go or Group 4 opsins). The other groups are theneuropsinsand the Go-opsins. The tetraopsins are one of the five major groups of the animalopsins,also known as type 2 opsins). The other groups are the ciliary opsins (c-opsins, cilopsins), the rhabdomeric opsins (r-opsins, rhabopsins), the xenopsins, and the nessopsins. Four of these subclades occur inBilateria(all but the nessopsins).[7][19]However, the bilaterian clades constitute aparaphyletictaxon without the opsins from thecnidarians.[7][19][20][21]
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Phylogenetic reconstruction of the opsins. The outgroup contains otherG protein-coupled receptors.The frame highlights the tetraopsins, which are expanded in the next image.
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Phylogenetic reconstruction of the tetraopsins. The outgroup contains other G protein-coupled receptors including the other opsins. The frame highlights the chromopsins, which are expanded in the next image.
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Phylogenetic reconstruction of the chromopsins. The outgroup contains other G protein-coupled receptors including the other opsins. The frame highlights the peropsins.
In thephylogenyabove, Eachcladecontains sequences from opsins and other G protein-coupled receptors. The number of sequences and two pie charts are shown next to the clade. The first pie chart shows the percentage of a certainamino acidat the position in the sequences corresponding to position 296 in cattle rhodopsin. The amino acids are color-coded. The colors are red forlysine(K), purple forglutamic acid(E), orange forarginine(R), dark and mid-gray for other amino acids, and light gray for sequences that have no data at that position. The second pie chart gives the taxon composition for each clade, green stands forcraniates,dark green forcephalochordates,mid green forechinoderms,brown fornematodes,pale pink forannelids,dark blue forarthropods,light blue formollusks,and purple forcnidarians.The branches to the clades have pie charts, which give support values for the branches. The values are from right to left SH-aLRT/aBayes/UFBoot. The branches are considered supported when SH-aLRT ≥ 80%, aBayes ≥ 0.95, and UFBoot ≥ 95%. If a support value is above its threshold the pie chart is black otherwise gray.[7]
Clinical significance
[edit]SinceRGR-opsinmay be associated withretinitis pigmentosa,[22]which is like peropsin also expressed in the retinal pigment epithelium, peropsin was screened for a link with retinitis pigmentosa.[23]However, no link could be established.[23][24]
References
[edit]- ^abcGRCh38: Ensembl release 89: ENSG00000180245–Ensembl,May 2017
- ^abcGRCm38: Ensembl release 89: ENSMUSG00000028012–Ensembl,May 2017
- ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^abcdSun H, Gilbert DJ, Copeland NG, Jenkins NA, Nathans J (September 1997)."Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium".Proceedings of the National Academy of Sciences of the United States of America.94(18): 9893–9898.Bibcode:1997PNAS...94.9893S.doi:10.1073/pnas.94.18.9893.PMC23288.PMID9275222.
- ^abc"Entrez Gene: RRH retinal pigment epithelium-derived rhodopsin homolog".
- ^abcdefghGühmann M, Porter ML, Bok MJ (August 2022)."The Gluopsins: Opsins without the Retinal Binding Lysine".Cells.11(15): 2441.doi:10.3390/cells11152441.PMC9368030.PMID35954284.
Material was copied and adapted from this source, which is available under aCreative Commons Attribution 4.0 International License.
- ^Leung NY, Thakur DP, Gurav AS, Kim SH, Di Pizio A, Niv MY, et al. (April 2020)."Functions of Opsins in Drosophila Taste".Current Biology.30(8): 1367–1379.e6.Bibcode:2020CBio...30E1367L.doi:10.1016/j.cub.2020.01.068.PMC7252503.PMID32243853.
- ^abKoyanagi M, Terakita A, Kubokawa K, Shichida Y (November 2002)."Amphioxus homologs of Go-coupled rhodopsin and peropsin having 11-cis- and all-trans-retinals as their chromophores".FEBS Letters.531(3): 525–528.doi:10.1016/s0014-5793(02)03616-5.PMID12435605.S2CID11669142.
- ^Wald G (July 1934)."Carotenoids and the Vitamin A Cycle in Vision".Nature.134(3376): 65.Bibcode:1934Natur.134...65W.doi:10.1038/134065a0.S2CID4022911.
- ^Wald G, Brown PK, Hubbard R, Oroshnik W (July 1955)."Hindered Cis Isomers of Vitamin A and Retinene: The Structure of the Neo-B Isomer".Proceedings of the National Academy of Sciences of the United States of America.41(7): 438–451.Bibcode:1955PNAS...41..438W.doi:10.1073/pnas.41.7.438.PMC528115.PMID16589696.
- ^Brown PK, Wald G (October 1956)."The neo-b isomer of vitamin A and retinene".The Journal of Biological Chemistry.222(2): 865–877.doi:10.1016/S0021-9258(20)89944-X.PMID13367054.
- ^Oroshnik W (June 1956). "The Synthesis and Configuration of Neo-B Vitamin A and Neoretinine b".Journal of the American Chemical Society.78(11): 2651–2652.doi:10.1021/ja01592a095.
- ^Oroshnik W, Brown PK, Hubbard R, Wald G (September 1956)."Hindered Cis Isomers of Vitamin A and Retinene: The Structure of the Neo-B Isomer".Proceedings of the National Academy of Sciences of the United States of America.42(9): 578–580.Bibcode:1956PNAS...42..578O.doi:10.1073/pnas.42.9.578.PMC534254.PMID16589909.
- ^Cook JD, Ng SY, Lloyd M, Eddington S, Sun H, Nathans J, et al. (December 2017)."Peropsin modulates transit of vitamin A from retina to retinal pigment epithelium".The Journal of Biological Chemistry.292(52): 21407–21416.doi:10.1074/jbc.M117.812701.PMC5766940.PMID29109151.
- ^Toh PP, Bigliardi-Qi M, Yap AM, Sriram G, Stelmashenko O, Bigliardi P (December 2016)."Expression of peropsin in human skin is related to phototransduction of violet light in keratinocytes".Experimental Dermatology.25(12): 1002–1005.doi:10.1111/exd.13226.PMID27676658.S2CID1373924.
- ^Bailey MJ, Cassone VM (March 2004). "Opsin photoisomerases in the chick retina and pineal gland: characterization, localization, and circadian regulation".Investigative Ophthalmology & Visual Science.45(3): 769–775.doi:10.1167/iovs.03-1125.PMID14985289.
- ^abcBellingham J, Wells DJ, Foster RG (January 2003)."In silico characterisation and chromosomal localisation of human RRH (peropsin)--implications for opsin evolution".BMC Genomics.4(1): 3.doi:10.1186/1471-2164-4-3.PMC149353.PMID12542842.
- ^abcRamirez MD, Pairett AN, Pankey MS, Serb JM, Speiser DI, Swafford AJ, et al. (26 October 2016)."The last common ancestor of most bilaterian animals possessed at least 9 opsins".Genome Biology and Evolution:evw248.doi:10.1093/gbe/evw248.PMC5521729.PMID27797948.
- ^abPorter ML, Blasic JR, Bok MJ, Cameron EG, Pringle T, Cronin TW, et al. (January 2012)."Shedding new light on opsin evolution".Proceedings. Biological Sciences.279(1726): 3–14.doi:10.1098/rspb.2011.1819.PMC3223661.PMID22012981.
- ^Liegertová M, Pergner J, Kozmiková I, Fabian P, Pombinho AR, Strnad H, et al. (July 2015)."Cubozoan genome illuminates functional diversification of opsins and photoreceptor evolution".Scientific Reports.5:11885.Bibcode:2015NatSR...511885L.doi:10.1038/srep11885.PMC5155618.PMID26154478.
- ^Morimura H, Saindelle-Ribeaudeau F, Berson EL, Dryja TP (December 1999). "Mutations in RGR, encoding a light-sensitive opsin homologue, in patients with retinitis pigmentosa".Nature Genetics.23(4): 393–394.doi:10.1038/70496.PMID10581022.S2CID35176366.
- ^abKsantini M, Sénéchal A, Humbert G, Arnaud B, Hamel CP (March 2007)."RRH, encoding the RPE-expressed opsin-like peropsin, is not mutated in retinitis pigmentosa and allied diseases"(PDF).Ophthalmic Genetics.28(1): 31–37.doi:10.1080/13816810701202052.PMID17454745.S2CID225451.
- ^Rivolta C, Berson EL, Dryja TP (December 2006). "Mutation screening of the peropsin gene, a retinal pigment epithelium specific rhodopsin homolog, in patients with retinitis pigmentosa and allied diseases".Molecular Vision.12:1511–1515.PMID17167409.
This article incorporates text from theUnited States National Library of Medicine,which is in thepublic domain.