|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 162 out of 162 for Rgr

<< First    < Previous  |  Next >    Last >>
0.025s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
•
•
•
•
•
Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
•
•
•
•
•
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
•
•
•
•
•
Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
•
•
•
•
•
Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
•
•
•
•
•
Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
•
•
•
•
•
Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
•
•
•
•
•
Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
•
•
•
•
•
Publication
15342385 | J:92408
First Author: Jiménez M
Year: 2004
Journal: Cancer Res
Title: The Rgr oncogene induces tumorigenesis in transgenic mice.
Volume: 64
Issue: 17
Pages: 6041-9
•
•
•
•
•
Author
Mooli RGR
•
•
•
•
•
Author
Pinheiro RGR
•
•
•
•
•
Publication
35587733 | J:330241
 
First Author: Ferreirinha P
Year: 2022
Journal: Development
Title: Identification of fibroblast progenitors in the developing mouse thymus.
Volume: 149
Issue: 10
•
•
•
•
•
DO Term
DOID:0110394 | retinitis pigmentosa 44
•
•
•
•
•
Allele
Rgr<tm1.1Kpal> | MGI:7461672
Name: retinal G protein coupled receptor; targeted mutation 1.1, Krzysztof Palczewski
Allele Type: Targeted
Attribute String: Null/knockout
•
•
•
•
•
Strain
MGI:7461676 | C57BL/6-Rgr<tm1.1Kpal>/J
Attribute String: coisogenic, mutant strain, targeted mutation
•
•
•
•
•
Publication
33351782 | J:307556
 
First Author: Beppu LY
Year: 2021
Journal: JCI Insight
Title: Tregs facilitate obesity and insulin resistance via a Blimp-1/IL-10 axis.
Volume: 6
Issue: 3
•
•
•
•
•
Publication
22227036 | J:181498
First Author: Osei-Sarfo K
Year: 2012
Journal: Carcinogenesis
Title: p15(INK4b) plays a crucial role in murine lymphoid development and tumorigenesis.
Volume: 33
Issue: 3
Pages: 708-13
•
•
•
•
•
Protein
A0A286YCJ0
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
•
•
•
•
•
Publication
8258527 | -
First Author: Jiang M
Year: 1993
Journal: Invest Ophthalmol Vis Sci
Title: An opsin homologue in the retina and pigment epithelium.
Volume: 34
Issue: 13
Pages: 3669-78
•
•
•
•
•
Protein Domain
IPR001793 | RPE_GPCR
Type: Family
Description: G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Retinal pigment epithelium (RPE) hosts a putative GPCR. The RPE-retinalGPCR (RGR) covalently binds all-trans- and 11-cis-retinal after reductionby sodium borohydride []. All-trans-retinal is bound preferentially overthe 11-cis isomer. The human sequence is 86% identical to that of bovineRGR [, ], and a lysine residue, analogous to the retinaldehyde attachmentsite of rhodopsin, is conserved in TM domain 7 []. The human gene, whosestructure is distinct from that of the visual pigment genes, spans 14.8 kband is split into 7 exons []. This suggests that the rgr gene representsthe earliest independent branch of the vertebrate opsin gene family [].Since the RGR gene product preferentially binds all-trans-retinal, it isthought that one of its functions may be to catalyse isomerisation of thechromophore by a retinochrome-like mechanism [].
•
•
•
•
•
Publication
24634209 | J:213177
First Author: Masuda T
Year: 2014
Journal: J Biol Chem
Title: Transcription factor SOX9 plays a key role in the regulation of visual cycle gene expression in the retinal pigment epithelium.
Volume: 289
Issue: 18
Pages: 12908-21
•
•
•
•
•
Publication
7947717 | -
First Author: Shen D
Year: 1994
Journal: Biochemistry
Title: A human opsin-related gene that encodes a retinaldehyde-binding protein.
Volume: 33
Issue: 44
Pages: 13117-25
•
•
•
•
•
Publication
2953598 | -
First Author: Fryxell KJ
Year: 1987
Journal: EMBO J
Title: An opsin gene that is expressed only in the R7 photoreceptor cell of Drosophila.
Volume: 6
Issue: 2
Pages: 443-51
•
•
•
•
•
Publication
1663559 | -
First Author: Fryxell KJ
Year: 1991
Journal: J Mol Evol
Title: The evolution of rhodopsins and neurotransmitter receptors.
Volume: 33
Issue: 4
Pages: 367-78
•
•
•
•
•
Publication
2437266 | -
First Author: Zuker CS
Year: 1987
Journal: J Neurosci
Title: A rhodopsin gene expressed in photoreceptor cell R7 of the Drosophila eye: homologies with other signal-transducing molecules.
Volume: 7
Issue: 5
Pages: 1550-7
•
•
•
•
•
Publication
2952772 | -
First Author: Montell C
Year: 1987
Journal: J Neurosci
Title: A second opsin gene expressed in the ultraviolet-sensitive R7 photoreceptor cells of Drosophila melanogaster.
Volume: 7
Issue: 5
Pages: 1558-66
•
•
•
•
•
Publication
3303660 | -
First Author: Applebury ML
Year: 1986
Journal: Vision Res
Title: Molecular biology of the visual pigments.
Volume: 26
Issue: 12
Pages: 1881-95
•
•
•
•
•
Protein Domain
IPR001760 | Opsin
Type: Family
Description: Visual pigments [, ]are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to the chromophore cis-retinal. Vision is effected through the absorption of a photon by cis-retinal which is isomerised to trans-retinal. This isomerisation leads to a change of conformation of the protein. Opsins are integral membrane proteins with seven transmembrane regions that belong to family 1 of G-protein coupled receptors.In vertebrates four different pigments are generally found. Rod cells, which mediate vision in dim light, contain the pigment rhodopsin. Cone cells, which function in bright light, are responsible for colour vision and contain three or more colour pigments (for example, in mammals: red, blue and green).By contrast with vertebrate rhodopsin, which is found in rod cells, insect photoreceptors are found in the ommatidia that comprise the compound eyes. Each Drosophila eye has 800 ommatidia, each of which contains 8 photoreceptor cells (designated R1-R8): R1-R6 are outer cells, while R7 and R8are inner cells. Opsins RH3 and RH4 are sensitive to UV light [, , ]. In Drosophila, the eye is composed of 800 facets or ommatidia. Each ommatidium contains eight photoreceptor cells (R1-R8): the R1 to R6 cells are outer cells, R7 and R8 inner cells. Each of the three types of cells (R1-R6, R7 and R8) expresses a specific opsin.Proteins evolutionary related to opsins include:Squid retinochrome, also known as retinal photoisomerase, which converts various isomers of retinal into 11-cis retinal.Mammalian opsin 3 (Encephalopsin) that may play a role in encephalic photoreception.Mammalian opsin 4 (Melanopsin) that may mediate regulation of circadian rhythms and acute suppression of pineal melatonin.Mammalian retinal pigment epithelium (RPE) RGR [], a protein that may also act in retinal isomerisation.
•
•
•
•
•
Protein Domain
IPR027430 | Retinal_BS
Type: Binding_site
Description: Visual pigments [, ]are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to the chromophore cis-retinal. Visionis effected through the absorption of a photon by cis-retinal which is isomerised to trans-retinal. This isomerisation leads to a change of conformation of the protein. Opsins are integral membrane proteins with seven transmembrane regions that belong to family 1 of G-protein coupled receptors.In vertebrates four different pigments are generally found. Rod cells, which mediate vision in dim light, contain the pigment rhodopsin. Cone cells, which function in bright light, are responsible for colour vision and contain three or more colour pigments (for example, in mammals: red, blue and green).By contrast with vertebrate rhodopsin, which is found in rod cells, insect photoreceptors are found in the ommatidia that comprise the compound eyes. Each Drosophila eye has 800 ommatidia, each of which contains 8 photoreceptor cells (designated R1-R8): R1-R6 are outer cells, while R7 and R8are inner cells. Opsins RH3 and RH4 are sensitive to UV light [, , ]. In Drosophila, the eye is composed of 800 facets or ommatidia. Each ommatidium contains eight photoreceptor cells (R1-R8): the R1 to R6 cells are outer cells, R7 and R8 inner cells. Each of the three types of cells (R1-R6, R7 and R8) expresses a specific opsin.Proteins evolutionary related to opsins include:Squid retinochrome, also known as retinal photoisomerase, which converts various isomers of retinal into 11-cis retinal.Mammalian opsin 3 (Encephalopsin) that may play a role in encephalic photoreception.Mammalian opsin 4 (Melanopsin) that may mediate regulation of circadian rhythms and acute suppression of pineal melatonin.Mammalian retinal pigment epithelium (RPE) RGR [], a protein that may also actin retinal isomerisation.The attachment site for retinal in the above proteins is a conserved lysineresidue in the middle of the seventh transmembrane helix.
•
•
•
•
•
Protein
Q9Z2B3
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
•
•
•
•
•
Protein
Q543X1
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
•
•
•
•
•
Protein
A0A286YCJ5
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
•
•
•
•
•
Protein
Q3UEX9
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
•
•
•
•
•
Protein
Q9QXZ9
Organism: Mus musculus/domesticus
Length: 521  
Fragment?: false
•
•
•
•
•
Protein
O35599
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
•
•
•
•
•
Protein
P51491
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
•
•
•
•
•
Protein
A0A0N4SV48
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
•
•
•
•
•
Protein
B1AYN7
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
•
•
•
•
•
Protein
Q3UEX0
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
•
•
•
•
•
Protein
A0A0N4SUP8
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: true
•
•
•
•
•
Protein
P15409
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
•
•
•
•
•
Protein
Q6VZZ7
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
•
•
•
•
•
Protein
Q9WUK7
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
•
•
•
•
•
Protein
O35214
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
•
•
•
•
•
Protein
A0A0G2JF76
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
•
•
•
•
•
Protein
Q3SX53
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
•
•
•
•
•
Protein
Q543W9
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: false
•
•
•
•
•
Protein
G3UXM0
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: false
•
•
•
•
•
Protein
Q9D1T9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
•
•
•
•
•
Protein
A9NIH9
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: true
•
•
•
•
•
Protein
Q80XL3
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
•
•
•
•
•
Protein
Q3KR48
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: true
•
•
•
•
•
Publication
2111655 | -
 
First Author: Birnbaumer L
Year: 1990
Journal: Annu Rev Pharmacol Toxicol
Title: G proteins in signal transduction.
Volume: 30
Pages: 675-705
•
•
•
•
•
Publication
2830256 | -
First Author: Casey PJ
Year: 1988
Journal: J Biol Chem
Title: G protein involvement in receptor-effector coupling.
Volume: 263
Issue: 6
Pages: 2577-80
•
•
•
•
•
Publication
8386361 | -
First Author: Attwood TK
Year: 1993
Journal: Protein Eng
Title: Design of a discriminating fingerprint for G-protein-coupled receptors.
Volume: 6
Issue: 2
Pages: 167-76
•
•
•
•
•
Publication
12679517 | J:83410
First Author: Vassilatis DK
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: The G protein-coupled receptor repertoires of human and mouse.
Volume: 100
Issue: 8
Pages: 4903-8
•
•
•
•
•
Publication
8170923 | -
First Author: Attwood TK
Year: 1994
Journal: Protein Eng
Title: Fingerprinting G-protein-coupled receptors.
Volume: 7
Issue: 2
Pages: 195-203
•
•
•
•
•
Publication
8081729 | -
First Author: Kolakowski LF Jr
Year: 1994
Journal: Receptors Channels
Title: GCRDb: a G-protein-coupled receptor database.
Volume: 2
Issue: 1
Pages: 1-7
•
•
•
•
•
Publication
15914470 | -
First Author: Foord SM
Year: 2005
Journal: Pharmacol Rev
Title: International Union of Pharmacology. XLVI. G protein-coupled receptor list.
Volume: 57
Issue: 2
Pages: 279-88
•
•
•
•
•
Publication
18948278 | -
First Author: Harmar AJ
Year: 2009
Journal: Nucleic Acids Res
Title: IUPHAR-DB: the IUPHAR database of G protein-coupled receptors and ion channels.
Volume: 37
Issue: Database issue
Pages: D680-5
•
•
•
•
•
Publication
16753280 | J:115055
First Author: Bjarnadóttir TK
Year: 2006
Journal: Genomics
Title: Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse.
Volume: 88
Issue: 3
Pages: 263-73
•
•
•
•
•
Publication
23020293 | -
 
First Author: Civelli O
Year: 2013
Journal: Annu Rev Pharmacol Toxicol
Title: G protein-coupled receptor deorphanizations.
Volume: 53
Pages: 127-46
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom