OPN5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | OPN5, GPR136, GRP136, PGR12, TMEM13, opsin 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 609042; MGI: 2662912; HomoloGene: 72341; GeneCards: OPN5; OMA:OPN5 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Opsin-5, also known as G-protein coupled receptor 136 or neuropsin is a protein that in humans is encoded by the OPN5 gene. Opsin-5 is a member of the opsin subfamily of the G protein-coupled receptors.[5][6][7] It is a photoreceptor protein sensitive to ultraviolet (UV) light. The OPN5 gene was discovered in mouse and human genomes and its mRNA expression was also found in neural tissues. Neuropsin is bistable at 0 °C and activates a UV-sensitive, heterotrimeric G protein Gi-mediated pathway in mammalian and avian tissues.[8][9]
Function
[edit]Human neuropsin is expressed in the eye, brain, testes, and spinal cord. Neuropsin belongs to the seven-exon subfamily of mammalian opsin genes that includes peropsin (RRH) and retinal G protein coupled receptor (RGR). Neuropsin has different isoforms created by alternative splicing.[7]
Photochemistry
[edit]When reconstituted with 11-cis-retinal, mouse and human neuropsins absorb maximally at 380 nm. When illuminated these neuropsins are converted into blue-absorbing photoproducts (470 nm), which are stable in the dark. The photoproducts are converted back to the UV-absorbing form, when they are illuminated with orange light (> 520 nm).[8]
Species distribution
[edit]Neuropsins are known from echinoderms,[10] annelids, arthropods, brachiopods, tardigrades, mollusks, and most are known from craniates.[11] The craniates are the taxon that contains mammals and with them humans. However, neuropsin orthologs have only been experimentally verified in a small number of animals, among them human, mouse (Mus musculus),[5] chicken (Gallus gallus domesticus),[9][12] the Japanese quail (Coturnix japonica),[13] the European brittle star Amphiura filiformis (related to starfish),[10] the tardigrade water bear (Hypsibius dujardini),[14] and the tadpole of Xenopus laevis.[15]
Searches of publicly available databases of genetic sequences have found putative neuropsin orthologs in both major branches of Bilateria: protostomes and deuterostomes. Among protostomes, putative neuropsins have been found in the molluscs owl limpet (Lottia gigantea) (a species of sea snail) and Pacific oyster (Crassostrea gigas), in the water flea (Daphnia pulex) (an arthropod), and in the annelid worm Capitella teleta.[14]
Phylogeny
[edit]The neuropsins are one of three subgroups of the tetraopsins (also known as RGR/Go or Group 4 opsins). The other groups are the chromopsins and the Go-opsins. The tetraopsins are one of the five major groups of the animal opsins, 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 in Bilateria (all but the nessopsins).[11][16] However, the bilaterian clades constitute a paraphyletic taxon without the opsins from the cnidarians.[11][16][17][18]
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Phylogenetic reconstruction of the opsins. The outgroup contains other G 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 neuropsins, which are expanded in the next image.
In the phylogeny above, Each clade contains 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 certain amino acid at the position in the sequences corresponding to position 296 in cattle rhodopsin. The amino acids are color-coded. The colors are red for lysine (K), purple for glutamic acid (E), 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 for craniates, dark green for cephalochordates, mid green for echinoderms, pale pink for annelids, dark blue for arthropods, light blue for mollusks, and purple for cnidarians. The branches 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.[11]
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000124818 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000043972 – 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.
- ^ a b Tarttelin EE, Bellingham J, Hankins MW, Foster RG, Lucas RJ (Nov 2003). "Neuropsin (Opn5): a novel opsin identified in mammalian neural tissue". FEBS Letters. 554 (3): 410–6. doi:10.1016/S0014-5793(03)01212-2. PMID 14623103. S2CID 9577067.
- ^ Fredriksson R, Höglund PJ, Gloriam DE, Lagerström MC, Schiöth HB (Nov 2003). "Seven evolutionarily conserved human rhodopsin G protein-coupled receptors lacking close relatives". FEBS Letters. 554 (3): 381–8. doi:10.1016/S0014-5793(03)01196-7. PMID 14623098. S2CID 11563502.
- ^ a b "Entrez Gene: OPN5 opsin 5".
- ^ a b Kojima D, Mori S, Torii M, Wada A, Morishita R, Fukada Y (2011). "UV-sensitive photoreceptor protein OPN5 in humans and mice". PLOS ONE. 6 (10): e26388. Bibcode:2011PLoSO...626388K. doi:10.1371/journal.pone.0026388. PMC 3197025. PMID 22043319.
- ^ a b Yamashita T, Ohuchi H, Tomonari S, Ikeda K, Sakai K, Shichida Y (December 2010). "Opn5 is a UV-sensitive bistable pigment that couples with Gi subtype of G protein". Proceedings of the National Academy of Sciences of the United States of America. 107 (51): 22084–22089. Bibcode:2010PNAS..10722084Y. doi:10.1073/pnas.1012498107. PMC 3009823. PMID 21135214.
- ^ a b Delroisse J, Ullrich-Lüter E, Ortega-Martinez O, Dupont S, Arnone MI, Mallefet J, Flammang P (2014). "High opsin diversity in a non-visual infaunal brittle star". BMC Genomics. 15 (1): 1035. doi:10.1186/1471-2164-15-1035. PMC 4289182. PMID 25429842.
- ^ a b c d Gühmann M, Porter ML, Bok MJ (August 2022). "The Gluopsins: Opsins without the Retinal Binding Lysine". Cells. 11 (15): 2441. doi:10.3390/cells11152441. PMC 9368030. PMID 35954284.
Material was copied and adapted from this source, which is available under a Creative Commons Attribution 4.0 International License.
- ^ Tomonari S, Migita K, Takagi A, Noji S, Ohuchi H (Jul 2008). "Expression patterns of the opsin 5-related genes in the developing chicken retina". Developmental Dynamics. 237 (7): 1910–22. doi:10.1002/dvdy.21611. PMID 18570255. S2CID 42113764.
- ^ Nakane Y, Ikegami K, Ono H, Yamamoto N, Yoshida S, Hirunagi K, Ebihara S, Kubo Y, Yoshimura T (Aug 2010). "A mammalian neural tissue opsin (Opsin 5) is a deep brain photoreceptor in birds". Proceedings of the National Academy of Sciences of the United States of America. 107 (34): 15264–8. Bibcode:2010PNAS..10715264N. doi:10.1073/pnas.1006393107. PMC 2930557. PMID 20679218.
- ^ a b Hering L, Mayer G (Sep 2014). "Analysis of the opsin repertoire in the tardigrade Hypsibius dujardini provides insights into the evolution of opsin genes in panarthropoda". Genome Biology and Evolution. 6 (9): 2380–91. doi:10.1093/gbe/evu193. PMC 4202329. PMID 25193307.
- ^ Currie SP, Doherty GH, Sillar KT (May 2016). "Deep-brain photoreception links luminance detection to motor output in Xenopus frog tadpoles". Proceedings of the National Academy of Sciences of the United States of America. 113 (21): 6053–6058. Bibcode:2016PNAS..113.6053C. doi:10.1073/pnas.1515516113. PMC 4889350. PMID 27166423.
- ^ a b Ramirez MD, Pairett AN, Pankey MS, Serb JM, Speiser DI, Swafford AJ, Oakley TH (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. PMC 5521729. PMID 27797948.
- ^ Porter ML, Blasic JR, Bok MJ, Cameron EG, Pringle T, Cronin TW, Robinson PR (January 2012). "Shedding new light on opsin evolution". Proceedings. Biological Sciences. 279 (1726): 3–14. doi:10.1098/rspb.2011.1819. PMC 3223661. PMID 22012981.
- ^ 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. PMC 5155618. PMID 26154478.
Further reading
[edit]- Terakita A (2005). "The opsins". Genome Biology. 6 (3): 213. doi:10.1186/gb-2005-6-3-213. PMC 1088937. PMID 15774036.
- Vassilatis DK, Hohmann JG, Zeng H, Li F, Ranchalis JE, Mortrud MT, Brown A, Rodriguez SS, Weller JR, Wright AC, Bergmann JE, Gaitanaris GA (Apr 2003). "The G protein-coupled receptor repertoires of human and mouse". Proceedings of the National Academy of Sciences of the United States of America. 100 (8): 4903–8. Bibcode:2003PNAS..100.4903V. doi:10.1073/pnas.0230374100. PMC 153653. PMID 12679517.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.