Retinoid X receptor alpha

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Retinoid X receptor, alpha
PDB rendering based on 1by4.
Available structures: 1by4, 1dkf, 1dsz, 1fby, 1fm6, 1fm9, 1g1u, 1g5y, 1k74, 1lbd, 1mv9, 1mvc, 1mzn, 1r0n, 1rdt, 1rxr, 1xdk, 1xls, 1xv9, 1xvp, 1ynw, 2acl, 2nll
Identifiers
Symbol(s) RXRA; FLJ16020; FLJ16733; MGC102720; NR2B1
External IDs OMIM: 180245 MGI: 98214 HomoloGene: 2220
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6256 20181
Ensembl ENSG00000186350 ENSMUSG00000015846
Uniprot P19793 Q3UMU4
Refseq NM_002957 (mRNA)
NP_002948 (protein)		 XM_976705 (mRNA)
XP_981799 (protein)
Location Chr 9: 136.36 - 136.47 Mb Chr 2: 27.5 - 27.59 Mb
Pubmed search [1] [2]

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

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 transcriptional regulators.[1]

[edit] See also

[edit] References

  1. ^ Entrez Gene: RXRA retinoid X receptor, alpha.

[edit] Further reading

  • Szanto A, Narkar V, Shen Q, et al. (2005). "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, et al. (1992). "9-cis retinoic acid is a high affinity ligand for the retinoid X receptor.". Cell 68 (2): 397-406. PMID 1310260. 
  • Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM (1992). "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling.". Nature 355 (6359): 446-9. doi:10.1038/355446a0. PMID 1310351. 
  • Kliewer SA, Umesono K, Heyman RA, et al. (1992). "Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling.". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1448-52. PMID 1311101. 
  • 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. PMID 1314167. 
  • Berrodin TJ, Marks MS, Ozato K, et al. (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. PMID 1331778. 
  • Mangelsdorf DJ, Umesono K, Kliewer SA, et al. (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. PMID 1651173. 
  • Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (1990). "Nuclear receptor that identifies a novel retinoic acid response pathway.". Nature 345 (6272): 224-9. doi:10.1038/345224a0. PMID 2159111. 
  • 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. PMID 7481822. 
  • Chen JD, Evans RM (1995). "A transcriptional co-repressor that interacts with nuclear hormone receptors.". Nature 377 (6548): 454-7. doi:10.1038/377454a0. PMID 7566127. 
  • Schulman IG, Chakravarti D, Juguilon H, et al. (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. PMID 7667283. 
  • Perlmann T, Jansson L (1995). "A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1.". Genes Dev. 9 (7): 769-82. 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. doi:10.1038/375203a0. PMID 7746322. 
  • 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. PMID 7758108. 
  • 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. PMID 7760852. 
  • Bourguet W, Ruff M, Chambon P, et al. (1995). "Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha.". Nature 375 (6530): 377-82. doi:10.1038/375377a0. PMID 7760929. 
  • Lee JW, Choi HS, Gyuris J, et al. (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. PMID 7776974. 
  • Tontonoz P, Graves RA, Budavari AI, et al. (1995). "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. PMID 7838715. 
  • Lee JW, Ryan F, Swaffield JC, et al. (1995). "Interaction of thyroid-hormone receptor with a conserved transcriptional mediator.". Nature 374 (6517): 91-4. doi:10.1038/374091a0. PMID 7870181. 
  • Lee MS, Sem DS, Kliewer SA, et al. (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. PMID 7925381. 

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

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v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD