Jump to content
 







Main menu
   


Navigation  



Main page
Contents
Current events
Random article
About Wikipedia
Contact us
Donate
 




Contribute  



Help
Learn to edit
Community portal
Recent changes
Upload file
 








Search  

































Create account

Log in
 









Create account
 Log in
 




Pages for logged out editors learn more  



Contributions
Talk
 



















Contents

   



(Top)
 


1 Photochemistry  





2 Tissue localization  





3 Gene localization and structure  





4 Phylogeny  





5 Clinical significance  





6 References  














RRH






Српски / srpski
Srpskohrvatski / српскохрватски
Татарча / tatarça
Українська
 

Edit links
 









Article
Talk
 

















Read
Edit
View history
 








Tools
   


Actions  



Read
Edit
View history
 




General  



What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Cite this page
Get shortened URL
Download QR code
Wikidata item
 




Print/export  



Download as PDF
Printable version
 
















Appearance
   

 






From Wikipedia, the free encyclopedia
 


RRH

Identifiers

Aliases

RRH, retinal pigment epithelium-derived rhodopsin homolog

External IDs

OMIM: 605224; MGI: 1097709; HomoloGene: 55977; GeneCards: RRH; OMA:RRH - orthologs

Gene location (Human)

Chromosome 4 (human)

Chr.

Chromosome 4 (human)[1]

Chromosome 4 (human)

Genomic location for RRH

Genomic location for RRH

Band

4q25

Start

109,827,972 bp[1]

End

109,849,123 bp[1]

Gene location (Mouse)

Chromosome 3 (mouse)

Chr.

Chromosome 3 (mouse)[2]

Chromosome 3 (mouse)

Genomic location for RRH

Genomic location for RRH

Band

3 G3|3 59.09 cM

Start

129,598,057 bp[2]

End

129,616,236 bp[2]

Bgee

Mouse (ortholog)


  • retinal pigment epithelium

  • cerebellar cortex

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • prefrontal cortex

  • Achilles tendon

  • stromal cell of endometrium

  • Brodmann area 9

  • developmental structure

  • neural layer of retina

  • zygote

  • secondary oocyte

  • primary oocyte

  • morula

  • lens

  • ciliary body

  • embryo

  • Epithelium of choroid plexus
  • More reference expression data

    BioGPS

    More reference expression data

    Molecular function

  • signal transducer activity
  • G protein-coupled receptor activity
  • G protein-coupled photoreceptor activity
  • Cellular component

  • integral component of plasma membrane
  • membrane
  • photoreceptor outer segment
  • Biological process

  • response to stimulus
  • visual perception
  • G protein-coupled receptor signaling pathway
  • phototransduction
  • detection of visible light
  • cellular response to light stimulus
  • Sources:Amigo / QuickGO

    Species

    Human

    Mouse

    Entrez

    Ensembl

    UniProt

    RefSeq (mRNA)

    NM_006583

    NM_009102

    RefSeq (protein)

    NP_006574

    NP_033128

    Location (UCSC)

    Chr 4: 109.83 – 109.85 Mb

    Chr 3: 129.6 – 129.62 Mb

    PubMed search

    [3]

    [4]

    Wikidata

    Peropsin, a visual pigment-like receptor, is a protein that in humans is encoded by the RRH gene.[5][6] It belongs like other animal opsins to the G protein-coupled receptors.[6] Even so, the first peropsins were already discovered in mice and humans in 1997,[5] not much is known about them.[7]

    Photochemistry[edit]

    Like most opsins, peropsins have in its seventh transmembrane domainalysine corresponding to amino acid position 296 in cattle rhodopsin,[5][7] which is important for retinal binding and light sensing.[8]

    Inamphioxus, a cephalochordate, a peropsin binds in the dark-state all-trans-retinal instead 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 apical microvilli of the retinal pigment epithelium (RPE).[5] There, it regulates storage or the movement of vitamin A from the retina to the RPE.[15] A peropsin is also expressed in keratinocytes of the human skin. In keratinocyte cell culture, it reacts to UV light if retinal is supplied.[16]Inchicken, a peropsin is expressed with an RGR-opsin in the pineal gland and the retina.[17]

    Gene localization and structure[edit]

    The human peropsin gene lies on chromosome 4 band 4q25 and has six introns[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 the craniates and the cephalochordates.[7] The craniates are the taxon that contains mammals and with them humans. The peropsins are one of the seven subgroups of the chromopsins. The other groups are the RGR-opsins, the retinochromes, 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 the neuropsins 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).[7][19] However, the bilaterian clades constitute a paraphyletic taxon without the opsins from the cnidarians.[7][19][20][21]

    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.
  • 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.
    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.
  • Phylogenetic reconstruction of the chromopsins. The outgroup contains other G protein-coupled receptors including the other opsins. The frame highlights the peropsins.
    Phylogenetic reconstruction of the chromopsins. The outgroup contains other G protein-coupled receptors including the other opsins. The frame highlights the peropsins.
  • 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), orange for arginine (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 for craniates, dark green for cephalochordates, mid green for echinoderms, brown for nematodes, pale pink for annelids, dark blue for arthropods, light blue for mollusks, and purple for cnidarians. 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]

    Since RGR-opsin may be associated with retinitis 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]

  • ^ "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 c d Sun 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. PMC 23288. PMID 9275222.
  • ^ a b c "Entrez Gene: RRH retinal pigment epithelium-derived rhodopsin homolog".
  • ^ a b c d e f g h 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.
  • ^ 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. PMC 7252503. PMID 32243853.
  • ^ a b Koyanagi 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. PMID 12435605. S2CID 11669142.
  • ^ Wald G (July 1934). "Carotenoids and the Vitamin A Cycle in Vision". Nature. 134 (3376): 65. Bibcode:1934Natur.134...65W. doi:10.1038/134065a0. S2CID 4022911.
  • ^ 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. PMC 528115. PMID 16589696.
  • ^ 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. PMID 13367054.
  • ^ 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. PMC 534254. PMID 16589909.
  • ^ 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. PMC 5766940. PMID 29109151.
  • ^ 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. PMID 27676658. S2CID 1373924.
  • ^ 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. PMID 14985289.
  • ^ a b c Bellingham 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. PMC 149353. PMID 12542842.
  • ^ a b c Ramirez 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. PMC 5521729. PMID 27797948.
  • ^ a b Porter 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. 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.
  • ^ 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. PMID 10581022. S2CID 35176366.
  • ^ a b Ksantini 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. PMID 17454745. S2CID 225451.
  • ^ 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. PMID 17167409.
  • This article incorporates text from the United States National Library of Medicine, which is in the public domain.

    Opsin
    (retinylidene protein)

    visual

  • Cone opsins
  • OPN1MW/OPN1MW2
  • OPN1SW
  • nonvisual

  • OPN3
  • OPN5
  • RRH
  • RGR
  • Crystallin

  • B)
  • Beta (A1
  • A2
  • A4
  • B1
  • B2
  • B3)
  • Gamma (A
  • B
  • C
  • D
  • N
  • S)
  • Other

  • Guanylate cyclase activator
  • Recoverin
  • Rhodopsin kinase
  • α2 (A
  • B
  • C)
  • β1
  • β2
  • β3
  • Purinergic

  • A2A
  • A2B
  • A3)
  • P2Y (1
  • 2
  • 4
  • 5
  • 6
  • 8
  • 9
  • 10
  • 11
  • 12
  • 13
  • 14)
  • Serotonin

  • B
  • D
  • E
  • F)
  • 5-HT2 (A
  • B
  • C)
  • 5-HT (4
  • 5A
  • 6
  • 7)
  • Other

  • M2
  • M3
  • M4
  • M5)
  • Dopamine
  • GHB receptor
  • Histamine
  • Melatonin (1A
  • 1B
  • 1C)
  • TAAR (1
  • 2
  • 5
  • 6
  • 8
  • 9)
  • Metabolites and
    signaling molecules

    Eicosanoid

    • CysLT (1
  • 2)
  • LTB4
  • 2
  • FPRL1
  • OXE
  • Prostaglandin
  • Prostacyclin
  • Thromboxane
  • Other

  • Cannabinoid (CB1
  • CB2, GPR (18
  • 55
  • 119))
  • EBI2
  • Estrogen
  • Free fatty acid (1
  • 2
  • 3
  • 4)
  • Hydroxycarboxylic acids
  • Lysophosphatidic acid (1
  • 2
  • 3
  • 4
  • 5
  • 6)
  • Lysophospholipid (1
  • 2
  • 3
  • 4
  • 5
  • 6
  • 7
  • 8)
  • Oxoglutarate
  • PAF
  • Sphingosine-1-phosphate (1
  • 2
  • 3
  • 4
  • 5)
  • Succinate
  • Peptide

    Neuropeptide

  • 2)
  • FF (1
  • 2)
  • S
  • Y (1
  • 2
  • 4
  • 5)
  • Neuromedin (B
  • U (1
  • 2))
  • Neurotensin (1
  • 2)
  • Other

  • C5a (1
  • 2))
  • Angiotensin (1
  • 2)
  • Apelin
  • Bombesin
  • Chemokine
  • Cholecystokinin (A
  • B)
  • Endothelin
  • Formyl peptide (1
  • 2
  • 3)
  • FSH
  • Galanin (1
  • 2
  • 3)
  • Gonadotropin-releasing hormone (1
  • 2)
  • Ghrelin
  • Kisspeptin
  • Luteinizing hormone/choriogonadotropin
  • MAS (1
  • 1L
  • D
  • E
  • F
  • G
  • X1
  • X2
  • X3
  • X4)
  • Melanocortin (1
  • 2
  • 3
  • 4
  • 5)
  • MCHR (1
  • 2)
  • Motilin
  • Opioid (Delta
  • Kappa
  • Mu
  • Nociceptin & Zeta, but not Sigma)
  • Orexin (1
  • 2)
  • Oxytocin
  • Prokineticin (1
  • 2)
  • Prolactin-releasing peptide
  • Relaxin (1
  • 2
  • 3
  • 4)
  • Somatostatin (1
  • 2
  • 3
  • 4
  • 5)
  • Tachykinin (1
  • 2
  • 3)
  • Thyrotropin
  • Thyrotropin-releasing hormone
  • Urotensin-II
  • Vasopressin (1A
  • 1B
  • 2)
  • Miscellaneous

    Taste, bitter

    • TAS2R
  • 3
  • 4
  • 5
  • 7
  • 8
  • 9
  • 10
  • 13
  • 14
  • 16
  • 19
  • 20
  • 30
  • 31
  • 38
  • 39
  • 40
  • 41
  • 42
  • 43
  • 45
  • 46
  • 50
  • 60
  • Vomeronasal receptor type 1
  • 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
  • 78
  • 81
  • 82
  • 83
  • 84
  • 85
  • 87
  • 88
  • 92
  • 101
  • 103
  • 109A
  • 109B
  • 119
  • 120
  • 132
  • 135
  • 137B
  • 139
  • 141
  • 142
  • 146
  • 148
  • 149
  • 150
  • 151
  • 152
  • 153
  • 160
  • 161
  • 162
  • 171
  • 173
  • 174
  • 176
  • 177
  • 182
  • 183)
  • Other

  • Olfactory
  • Opsin (3
  • 4
  • 5
  • 1LW
  • 1MW
  • 1SW
  • RGR
  • RRH)
  • Protease-activated (1
  • 2
  • 3
  • 4)
  • SREB (1
  • 2
  • 3)
  • 2
  • 3
  • ADGRC
  • ADGRE
  • ADGRG
  • ADGRL
  • Orphan

  • 64
  • 97
  • 98
  • 110
  • 111
  • 112
  • 113
  • 114
  • 115
  • 116
  • 123
  • 124
  • 125
  • 126
  • 128
  • 133
  • 143
  • 144
  • 155
  • 157)
  • Other

  • CALCRL
  • Corticotropin-releasing hormone (1
  • 2)
  • Glucagon (GR
  • GIPR
  • GLP1R
  • GLP2R)
  • Growth-hormone-releasing hormone
  • PACAPR1
  • GPR
  • Methuselah-like proteins
  • Parathyroid hormone (1
  • 2)
  • Secretin
  • Vasoactive intestinal peptide (1
  • 2)
  • Taste, sweet

    • TAS1R
  • 2
  • 3
  • Vomeronasal receptor, type 2
  • Other

  • GABAB (1
  • 2)
  • Glutamate receptor (Metabotropic glutamate (1
  • 2
  • 3
  • 4
  • 5
  • 6
  • 7
  • 8))
  • GPRC6A
  • GPR (156
  • 158
  • 179)
  • RAIG (1
  • 2
  • 3
  • 4)
  • Class F: Frizzled & Smoothened

    Frizzled

  • 2
  • 3
  • 4
  • 5
  • 6
  • 7
  • 8
  • 9
  • 10)
  • Smoothened


    Retrieved from "https://en.wikipedia.org/w/index.php?title=RRH&oldid=1218444637"

    Categories: 
    Genes on human chromosome 4
    G protein-coupled receptors
    Hidden categories: 
    Articles with short description
    Short description matches Wikidata
    Wikipedia articles incorporating text from the United States National Library of Medicine
     



    This page was last edited on 11 April 2024, at 19:06 (UTC).

    Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.



    Privacy policy

    About Wikipedia

    Disclaimers

    Contact Wikipedia

    Code of Conduct

    Developers

    Statistics

    Cookie statement

    Mobile view



    Wikimedia Foundation
    Powered by MediaWiki