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RXRA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BY4, 1DSZ, 1FBY, 1FM6, 1FM9, 1G1U, 1G5Y, 1K74, 1LBD, 1MV9, 1MVC, 1MZN, 1R0N, 1RDT, 1RXR, 1XLS, 1XV9, 1XVP, 1YNW, 2ACL, 2NLL, 2P1T, 2P1U, 2P1V, 2ZXZ, 2ZY0, 3DZU, 3DZY, 3E00, 3E94, 3FAL, 3FC6, 3FUG, 3H0A, 3KWY, 3NSP, 3NSQ, 3OAP, 3OZJ, 3PCU, 3R29, 3R2A, 3R5M, 3UVV, 4CN2, 4CN3, 4CN5, 4CN7, 4J5W, 4J5X, 4K4J, 4K6I, 4M8E, 4M8H, 4N5G, 4N8R, 4NQA, 4OC7, 4POH, 4POJ, 4PP3, 4PP5, 4RFW, 4RMC, 4RMD, 4RME, 4ZO1, 5EC9, 4ZSH
Identifiers
Aliases	RXRA, NR2B1, Retinoid X receptor alpha, RXR-alpha, RXRalpha
External IDs	OMIM: 180245; MGI: 98214; HomoloGene: 2220; GeneCards: RXRA; OMA:RXRA - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q34.2 Start 134,317,098 bp End 134,440,585 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 A3|2 19.38 cM Start 27,566,452 bp End 27,652,969 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of hip gingival epithelium pancreatic ductal cell gastrocnemius muscle right lobe of liver vastus lateralis muscle Skeletal muscle tissue of rectus abdominis blood Skeletal muscle tissue of biceps brachii trabecular bone Top expressed in lip muscle of thigh medulla of thymus left lobe of liver transitional epithelium of urinary bladder Ileal epithelium genital tubercle medullary collecting duct ankle molar More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding DNA-binding transcription factor activity vitamin D response element binding transcription coactivator activity transcription factor binding retinoic acid-responsive element binding metal ion binding steroid hormone receptor activity nuclear receptor activity protein binding protein heterodimerization activity enzyme binding chromatin DNA binding vitamin D receptor binding retinoic acid binding double-stranded DNA binding zinc ion binding nuclear receptor binding peptide binding DNA binding domain binding LBD domain binding DNA-binding transcription factor activity, RNA polymerase II-specific signaling receptor activity Cellular component receptor complex nucleoplasm RNA polymerase II transcription regulator complex nucleus protein-containing complex Biological process steroid hormone mediated signaling pathway regulation of branching involved in prostate gland morphogenesis regulation of transcription, DNA-templated placenta development peroxisome proliferator activated receptor signaling pathway regulation of transcription by RNA polymerase II cholesterol metabolic process in utero embryonic development negative regulation of transcription by RNA polymerase II cardiac muscle cell proliferation secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development transcription, DNA-templated positive regulation of transcription, DNA-templated ventricular cardiac muscle tissue morphogenesis heart development retinoic acid receptor signaling pathway maternal placenta development modulation by virus of host process vitamin metabolic process bile acid and bile salt transport ventricular cardiac muscle cell differentiation camera-type eye development viral process protein homotetramerization transcription initiation from RNA polymerase II promoter embryo implantation positive regulation of translational initiation by iron positive regulation of transcription by RNA polymerase II positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus response to retinoic acid regulation of lipid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6256 20181 Ensembl ENSG00000186350 ENSMUSG00000015846 UniProt P19793 P28700 RefSeq (mRNA) NM_002957 NM_001291920 NM_001291921 NM_001290481 NM_001290482 NM_011305 RefSeq (protein) NP_001278849 NP_001278850 NP_002948 NP_001277410 NP_001277411 NP_035435 Location (UCSC) Chr 9: 134.32 – 134.44 Mb Chr 2: 27.57 – 27.65 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 (nuclear receptor subfamily 2, group B, member 1) is a nuclear receptor that in humans is encoded by the RXRA gene.

Function

Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcription factors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the cytochrome P450 system genes.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

1. The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

Interactions

Retinoid X receptor alpha has been shown to interact with:

• BCL3,
• BRD8,
• CLOCK,
• FXR
• IGFBP3,
• ITGB3BP,
• LXR-β,
• MyoD,
• NCOA6,
• NFKBIB,
• NPAS2,
• NRIP1,
• NR4A1,
• NCOA2,
• NCOA3,
• POU2F1,
• PPARGC1A,
• PPAR-γ,
• RNF8,
• RAR-α,
• SHP,
• TADA3L,
• TBP,
• TRIM24,
• TR-β, and
• VDR.

See also

• Retinoid X receptor

References

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2. ^ GRCm38: Ensembl release 89: ENSMUSG00000015846 – Ensembl, May 2017
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4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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6. "Entrez Gene: RXRA retinoid X receptor, alpha".
7. "Retinoic acid receptor RXR-alpha - Homo sapiens (Human)". UniProt.
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23. ^ Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.
24. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM (1997). "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300". Cell. 90 (3): 569–80. doi:10.1016/S0092-8674(00)80516-4. PMID 9267036. S2CID 15284825.
25. Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ (1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". J. Biol. Chem. 274 (38): 26713–9. doi:10.1074/jbc.274.38.26713. PMID 10480874.
26. Kakizawa T, Miyamoto T, Ichikawa K, Kaneko A, Suzuki S, Hara M, Nagasawa T, Takeda T, Mori Ji, Kumagai M, Hashizume K (1999). "Functional interaction between Oct-1 and retinoid X receptor". J. Biol. Chem. 274 (27): 19103–8. doi:10.1074/jbc.274.27.19103. PMID 10383413.
27. Delerive P, Wu Y, Burris TP, Chin WW, Suen CS (2002). "PGC-1 functions as a transcriptional coactivator for the retinoid X receptors". J. Biol. Chem. 277 (6): 3913–7. doi:10.1074/jbc.M109409200. PMID 11714715.
28. Tontonoz P, Graves RA, Budavari AI, Erdjument-Bromage H, Lui M, Hu E, Tempst P, Spiegelman BM (1994). "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha". Nucleic Acids Res. 22 (25): 5628–34. doi:10.1093/nar/22.25.5628. PMC 310126. PMID 7838715.
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30. Gampe RT, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE (2000). "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors". Mol. Cell. 5 (3): 545–55. doi:10.1016/S1097-2765(00)80448-7. PMID 10882139.
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32. Benkoussa M, Brand C, Delmotte MH, Formstecher P, Lefebvre P (2002). "Retinoic acid receptors inhibit AP1 activation by regulating extracellular signal-regulated kinase and CBP recruitment to an AP1-responsive promoter". Mol. Cell. Biol. 22 (13): 4522–34. doi:10.1128/MCB.22.13.4522-4534.2002. PMC 133906. PMID 12052862.
33. Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992). "RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors". EMBO J. 11 (4): 1409–18. doi:10.1002/j.1460-2075.1992.tb05186.x. PMC 556590. PMID 1314167.
34. Lee YK, Dell H, Dowhan DH, Hadzopoulou-Cladaras M, Moore DD (2000). "The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression". Mol. Cell. Biol. 20 (1): 187–95. doi:10.1128/MCB.20.1.187-195.2000. PMC 85074. PMID 10594021.
35. Brendel C, Schoonjans K, Botrugno OA, Treuter E, Auwerx J (2002). "The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity". Mol. Endocrinol. 16 (9): 2065–76. doi:10.1210/me.2001-0194. PMID 12198243.
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37. Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. Bibcode:1995PNAS...92.8288S. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283.
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40. Monden T, Wondisford FE, Hollenberg AN (1997). "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein". J. Biol. Chem. 272 (47): 29834–41. doi:10.1074/jbc.272.47.29834. PMID 9368056.
41. Jeyakumar M, Tanen MR, Bagchi MK (1997). "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. doi:10.1210/mend.11.6.0003. PMID 9171239.
42. Baudino TA, Kraichely DM, Jefcoat SC, Winchester SK, Partridge NC, MacDonald PN (1998). "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription". J. Biol. Chem. 273 (26): 16434–41. doi:10.1074/jbc.273.26.16434. PMID 9632709.

Further reading

• Szanto A, Narkar V, Shen Q, Uray IP, Davies PJ, Nagy L (December 2004). "Retinoid X receptors: X-ploring their (patho)physiological functions". Cell Death Differ. 11 (Suppl 2): S126–43. doi:10.1038/sj.cdd.4401533. PMID 15608692.
• Heyman RA, Mangelsdorf DJ, Dyck JA, Stein RB, Eichele G, Evans RM, Thaller C (January 1992). "9-cis retinoic acid is a high affinity ligand for the retinoid X receptor". Cell. 68 (2): 397–406. doi:10.1016/0092-8674(92)90479-V. PMID 1310260. S2CID 39338234.
• Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM (January 1992). "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling". Nature. 355 (6359): 446–9. Bibcode:1992Natur.355..446K. doi:10.1038/355446a0. PMC 6159885. PMID 1310351.
• Kliewer SA, Umesono K, Heyman RA, Mangelsdorf DJ, Dyck JA, Evans RM (February 1992). "Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1448–52. Bibcode:1992PNAS...89.1448K. doi:10.1073/pnas.89.4.1448. PMC 48468. PMID 1311101.
• Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (April 1992). "RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors". EMBO J. 11 (4): 1409–18. doi:10.1002/j.1460-2075.1992.tb05186.x. PMC 556590. PMID 1314167.
• Berrodin TJ, Marks MS, Ozato K, Linney E, Lazar MA (September 1992). "Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein". Mol. Endocrinol. 6 (9): 1468–78. doi:10.1210/mend.6.9.1331778. PMID 1331778. S2CID 24291055.
• Mangelsdorf DJ, Umesono K, Kliewer SA, Borgmeyer U, Ong ES, Evans RM (August 1991). "A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR". Cell. 66 (3): 555–61. doi:10.1016/0092-8674(81)90018-0. PMID 1651173. S2CID 13444623.
• Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (May 1990). "Nuclear receptor that identifies a novel retinoic acid response pathway". Nature. 345 (6272): 224–9. Bibcode:1990Natur.345..224M. doi:10.1038/345224a0. PMID 2159111. S2CID 4232833.
• Oñate SA, Tsai SY, Tsai MJ, O'Malley BW (1995). "Sequence and characterization of a coactivator for the steroid hormone receptor superfamily". Science. 270 (5240): 1354–7. Bibcode:1995Sci...270.1354O. doi:10.1126/science.270.5240.1354. PMID 7481822. S2CID 28749162.
• Chen JD, Evans RM (1995). "A transcriptional co-repressor that interacts with nuclear hormone receptors". Nature. 377 (6548): 454–7. Bibcode:1995Natur.377..454C. doi:10.1038/377454a0. PMID 7566127. S2CID 4361329.
• Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (August 1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. Bibcode:1995PNAS...92.8288S. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283.
• Perlmann T, Jansson L (April 1995). "A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1". Genes Dev. 9 (7): 769–82. doi:10.1101/gad.9.7.769. PMID 7705655.
• Rastinejad F, Perlmann T, Evans RM, Sigler PB (1995). "Structural determinants of nuclear receptor assembly on DNA direct repeats". Nature. 375 (6528): 203–11. Bibcode:1995Natur.375..203R. doi:10.1038/375203a0. PMID 7746322. S2CID 4373097.
• Forman BM, Umesono K, Chen J, Evans RM (1995). "Unique response pathways are established by allosteric interactions among nuclear hormone receptors". Cell. 81 (4): 541–50. doi:10.1016/0092-8674(95)90075-6. PMID 7758108. S2CID 3203590.
• Seol W, Choi HS, Moore DD (1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors". Mol. Endocrinol. 9 (1): 72–85. doi:10.1210/mend.9.1.7760852. PMID 7760852.
• Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D (June 1995). "Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha". Nature. 375 (6530): 377–82. Bibcode:1995Natur.375..377B. doi:10.1038/375377a0. PMID 7760929. S2CID 4371873.
• Lee JW, Choi HS, Gyuris J, Brent R, Moore DD (February 1995). "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor". Mol. Endocrinol. 9 (2): 243–54. doi:10.1210/mend.9.2.7776974. PMID 7776974.
• Tontonoz P, Graves RA, Budavari AI, Erdjument-Bromage H, Lui M, Hu E, Tempst P, Spiegelman BM (December 1994). "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha". Nucleic Acids Res. 22 (25): 5628–34. doi:10.1093/nar/22.25.5628. PMC 310126. PMID 7838715.
• Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD (March 1995). "Interaction of thyroid-hormone receptor with a conserved transcriptional mediator". Nature. 374 (6517): 91–4. Bibcode:1995Natur.374...91L. doi:10.1038/374091a0. PMID 7870181. S2CID 4324595.
• Lee MS, Sem DS, Kliewer SA, Provencal J, Evans RM, Wright PE (September 1994). "NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix". Eur. J. Biochem. 224 (2): 639–50. doi:10.1111/j.1432-1033.1994.00639.x. PMID 7925381.

External links

• FactorBook RXRA

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

• Genes on human chromosome 9
• Intracellular receptors
• Transcription factors