Retinoic acid receptor gamma

Protein-coding gene in the species Homo sapiens
RARG
Available structures
PDBOrtholog search: H3BMH6 PDBe H3BMH6 RCSB
List of PDB id codes

1EXA, 1EXX, 1FCX, 1FCY, 1FCZ, 1FD0, 2LBD, 3LBD, 4LBD

Identifiers
AliasesRARG, NR1B3, RARC, retinoic acid receptor gamma, RARgamma
External IDsOMIM: 180190 MGI: 97858 HomoloGene: 20263 GeneCards: RARG
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for RARG
Genomic location for RARG
Band12q13.13Start53,210,567 bp[1]
End53,232,980 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for RARG
Genomic location for RARG
Band15 F2|15 57.4 cMStart102,143,373 bp[2]
End102,165,952 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of abdomen

  • stromal cell of endometrium

  • canal of the cervix

  • right coronary artery

  • vagina

  • right uterine tube

  • tibial nerve

  • minor salivary glands

  • right lobe of thyroid gland

  • ascending aorta
Top expressed in
  • axial skeleton

  • lip

  • vertebral column

  • shoulder

  • ankle

  • vertebra

  • scapula

  • molar

  • rib

  • esophagus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • sequence-specific DNA binding
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding
  • zinc ion binding
  • metal ion binding
  • steroid hormone receptor activity
  • protein binding
  • DNA-binding transcription factor activity
  • DNA binding
  • retinoid X receptor binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • transcription cis-regulatory region binding
  • transcription factor binding
  • nuclear receptor coactivator activity
  • signaling receptor activity
  • nuclear receptor activity
Cellular component
  • integral component of membrane
  • nucleoplasm
  • nucleus
  • transcription regulator complex
  • RNA polymerase II transcription regulator complex
Biological process
  • regulation of cell size
  • growth plate cartilage development
  • cellular response to retinoic acid
  • gland development
  • regulation of transcription, DNA-templated
  • negative regulation of cartilage development
  • response to retinoic acid
  • multicellular organism growth
  • negative regulation of cell differentiation
  • bone morphogenesis
  • chondrocyte development
  • negative regulation of apoptotic process
  • retinal pigment epithelium development
  • transcription, DNA-templated
  • epithelium development
  • embryonic camera-type eye development
  • reproductive structure development
  • limb development
  • face development
  • neural tube closure
  • negative regulation of chondrocyte differentiation
  • Harderian gland development
  • prostate gland epithelium morphogenesis
  • regulation of myelination
  • positive regulation of gene expression
  • retina development in camera-type eye
  • positive regulation of cell population proliferation
  • growth plate cartilage chondrocyte growth
  • canonical Wnt signaling pathway
  • regulation of gene expression
  • camera-type eye development
  • transcription initiation from RNA polymerase II promoter
  • regulation of myeloid cell differentiation
  • bone development
  • trachea cartilage development
  • anterior/posterior pattern specification
  • glandular epithelial cell development
  • steroid hormone mediated signaling pathway
  • negative regulation of transcription by RNA polymerase II
  • positive regulation of transcription by RNA polymerase II
  • embryonic hindlimb morphogenesis
  • retinoic acid receptor signaling pathway
  • negative regulation of cell population proliferation
  • embryonic eye morphogenesis
  • positive regulation of apoptotic process
  • positive regulation of programmed cell death
  • cellular response to leukemia inhibitory factor
  • multicellular organism development
  • hormone-mediated signaling pathway
  • cell differentiation
  • response to lipid
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5916

19411

Ensembl

ENSG00000172819

ENSMUSG00000001288

UniProt

P13631

P18911

RefSeq (mRNA)

NM_000966
NM_001042728
NM_001243730
NM_001243731
NM_001243732

NM_001042727
NM_011244

RefSeq (protein)

NP_000957
NP_001036193
NP_001230659
NP_001230660
NP_001230661

NP_001036192
NP_035374

Location (UCSC)Chr 12: 53.21 – 53.23 MbChr 15: 102.14 – 102.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Retinoic acid receptor gamma (RAR-γ), also known as NR1B3 (nuclear receptor subfamily 1, group B, member 3) is a nuclear receptor encoded by the RARG gene.[5][6] Adapalene selectively targets retinoic acid receptor beta and retinoic acid receptor gamma[7] and its agonism of the gamma subtype is largely responsible for adapalene's observed effects.[8]

Interactions

Retinoic acid receptor gamma has been shown to interact with NCOR1.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172819 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001288 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: RARG retinoic acid receptor, gamma".
  6. ^ Lehmann JM, Hoffmann B, Pfahl M (Feb 1991). "Genomic organization of the retinoic acid receptor gamma gene". Nucleic Acids Research. 19 (3): 573–8. doi:10.1093/nar/19.3.573. PMC 333650. PMID 1849262.
  7. ^ Mukherjee S, Date A, Patravale V, Korting HC, Roeder A, Weindl G (2006). "Retinoids in the treatment of skin aging: an overview of clinical efficacy and safety". Clinical Interventions in Aging. 1 (4): 327–48. doi:10.2147/ciia.2006.1.4.327. PMC 2699641. PMID 18046911.
  8. ^ Michel S, Jomard A, Démarchez M (October 1998). "Pharmacology of adapalene". The British Journal of Dermatology. 139 (Suppl 52): 3–7. doi:10.1046/j.1365-2133.1998.1390s2003.x. PMID 9990413. S2CID 23084886.
  9. ^ Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (May 1999). "Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein". The Journal of Biological Chemistry. 274 (22): 15901–7. doi:10.1074/jbc.274.22.15901. PMID 10336495.

Further reading

  • Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Garnier JM, Mader S (Jan 1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently". Cell. 68 (2): 377–95. doi:10.1016/0092-8674(92)90478-U. PMID 1310259. S2CID 40617478.
  • Vollberg TM, Nervi C, George MD, Fujimoto W, Krust A, Jetten AM (May 1992). "Retinoic acid receptors as regulators of human epidermal keratinocyte differentiation". Molecular Endocrinology. 6 (5): 667–76. doi:10.1210/mend.6.5.1318502. PMID 1318502. S2CID 35884680.
  • Lehmann JM, Zhang XK, Pfahl M (Jul 1992). "RAR gamma 2 expression is regulated through a retinoic acid response element embedded in Sp1 sites". Molecular and Cellular Biology. 12 (7): 2976–85. doi:10.1128/mcb.12.7.2976. PMC 364511. PMID 1320193.
  • Mattei MG, Rivière M, Krust A, Ingvarsson S, Vennström B, Islam MQ, Levan G, Kautner P, Zelent A, Chambon P (Aug 1991). "Chromosomal assignment of retinoic acid receptor (RAR) genes in the human, mouse, and rat genomes" (PDF). Genomics. 10 (4): 1061–9. doi:10.1016/0888-7543(91)90199-O. hdl:1946/20678. PMID 1655630.
  • Kastner P, Krust A, Mendelsohn C, Garnier JM, Zelent A, Leroy P, Staub A, Chambon P (Apr 1990). "Murine isoforms of retinoic acid receptor gamma with specific patterns of expression". Proceedings of the National Academy of Sciences of the United States of America. 87 (7): 2700–4. Bibcode:1990PNAS...87.2700K. doi:10.1073/pnas.87.7.2700. PMC 53758. PMID 2157210.
  • Giguère V, Shago M, Zirngibl R, Tate P, Rossant J, Varmuza S (May 1990). "Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo". Molecular and Cellular Biology. 10 (5): 2335–40. doi:10.1128/mcb.10.5.2335. PMC 360581. PMID 2157970.
  • Ishikawa T, Umesono K, Mangelsdorf DJ, Aburatani H, Stanger BZ, Shibasaki Y, Imawari M, Evans RM, Takaku F (Jun 1990). "A functional retinoic acid receptor encoded by the gene on human chromosome 12". Molecular Endocrinology. 4 (6): 837–44. doi:10.1210/mend-4-6-837. PMID 2172793.
  • Krust A, Kastner P, Petkovich M, Zelent A, Chambon P (Jul 1989). "A third human retinoic acid receptor, hRAR-gamma". Proceedings of the National Academy of Sciences of the United States of America. 86 (14): 5310–4. Bibcode:1989PNAS...86.5310K. doi:10.1073/pnas.86.14.5310. PMC 297611. PMID 2546152.
  • Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D (Dec 1995). "Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid". Nature. 378 (6558): 681–9. Bibcode:1995Natur.378..681R. doi:10.1038/378681a0. PMID 7501014. S2CID 4259376.
  • Zhou L, Pang J, Munroe DG, Lau C (May 1993). "A human retinoic acid receptor gamma isoform is homologous to the murine retinoic acid receptor gamma 7". Nucleic Acids Research. 21 (10): 2520. doi:10.1093/nar/21.10.2520. PMC 309563. PMID 7685085.
  • Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA (Feb 1994). "Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts". Journal of Immunology. 152 (3): 1419–27. doi:10.4049/jimmunol.152.3.1419. PMID 8301142. S2CID 20598143.
  • Botling J, Castro DS, Oberg F, Nilsson K, Perlmann T (Apr 1997). "Retinoic acid receptor/retinoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation". The Journal of Biological Chemistry. 272 (14): 9443–9. doi:10.1074/jbc.272.14.9443. PMID 9083083.
  • Lømo J, Smeland EB, Ulven S, Natarajan V, Blomhoff R, Gandhi U, Dawson MI, Blomhoff HK (Apr 1998). "RAR-, not RXR, ligands inhibit cell activation and prevent apoptosis in B-lymphocytes". Journal of Cellular Physiology. 175 (1): 68–77. doi:10.1002/(SICI)1097-4652(199804)175:1<68::AID-JCP8>3.0.CO;2-A. PMID 9491782. S2CID 21489004.
  • Klaholz BP, Renaud JP, Mitschler A, Zusi C, Chambon P, Gronemeyer H, Moras D (Mar 1998). "Conformational adaptation of agonists to the human nuclear receptor RAR gamma". Nature Structural Biology. 5 (3): 199–202. doi:10.1038/nsb0398-199. PMID 9501913. S2CID 30471226.
  • Zhang ZP, Gambone CJ, Gabriel JL, Wolfgang CL, Soprano KJ, Soprano DR (Dec 1998). "Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor gamma". The Journal of Biological Chemistry. 273 (51): 34016–21. doi:10.1074/jbc.273.51.34016. PMID 9852056.
  • Yang C, Zhou D, Chen S (Dec 1998). "Modulation of aromatase expression in the breast tissue by ERR alpha-1 orphan receptor". Cancer Research. 58 (24): 5695–700. PMID 9865725.
  • Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA (Aug 1999). "Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor". The Journal of Biological Chemistry. 274 (32): 22563–8. doi:10.1074/jbc.274.32.22563. PMID 10428834.
  • Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D (Jun 2000). "Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid". The EMBO Journal. 19 (11): 2592–601. doi:10.1093/emboj/19.11.2592. PMC 212755. PMID 10835357.
  • Boudjelal M, Voorhees JJ, Fisher GJ (Mar 2002). "Retinoid signaling is attenuated by proteasome-mediated degradation of retinoid receptors in human keratinocyte HaCaT cells". Experimental Cell Research. 274 (1): 130–7. doi:10.1006/excr.2001.5450. PMID 11855864.
  • v
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  • 1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1
    1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1
  • 1exa: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.
    1exa: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.
  • 1exx: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE INACTIVE S-ENANTIOMER BMS270395.
    1exx: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE INACTIVE S-ENANTIOMER BMS270395.
  • 1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394
    1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394
  • 1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564
    1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564
  • 1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156
    1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156
  • 1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254
    1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254
  • 1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
    1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
  • 2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
    2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
  • 3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID
    3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID
  • 4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961
    4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961
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(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
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RARTooltip Retinoic acid receptor
  • Antagonists: BMS-195614
  • BMS-493
  • CD-2665
  • ER-50891
  • LE-135
  • MM-11253
  • Retinoic acid metabolism inhibitors: Liarozole
RXRTooltip Retinoid X receptor
  • Antagonists: HX-531
  • HX-630
  • LG-100754
  • PA-452
  • UVI-3003
  • HX-603
  • LE135 (RAR beta selective)
  • LE-540
  • CD3254
  • PA-451
  • PA-452
  • Rhein
  • HX-711
  • 6-(N-ethyl-N-(5-isobutoxy-4-isopropyl-2-(E)-styrylphenyl)amino)nicotinic acid
See also
Receptor/signaling modulators