Retinoid X receptor gamma

From Wikipedia, the free encyclopedia

Retinoid X receptor, gamma

Crystallographic structure of the DNA-binding domain of the Retinoid X receptor, gamma. PDB rendering based on 1by4.

Available structures: 1by4, 1dsz, 1r0n, 1rxr, 2gl8, 2nll

Identifiers

Symbol(s)

RXRG; NR2B3; RXRC

External IDs

OMIM: 180247 MGI: 98216 HomoloGene: 21373

Gene ontology
Molecular Function:	• transcription factor activity • steroid hormone receptor activity • retinoid-X receptor activity • steroid binding • zinc ion binding • tRNA-pseudouridine synthase activity • sequence-specific DNA binding • metal ion binding
Cellular Component:	• nucleus
Biological Process:	• transcription • regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001009598 (mRNA)
NP_001009598 (protein)

NM_009107 (mRNA)
NP_033133 (protein)

Location

Chr 1: 163.64 - 163.68 Mb

Chr 1: 169.44 - 169.48 Mb

Pubmed search

[1]

[2]

Retinoic acid receptor gamma (RXR-gamma), also known as NR2B3 (nuclear receptor subfamily 2, group B, member 3) is a nuclear receptor encoded by the RXRG gene.^[1]

This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the antiproliferative effects of retinoic acid (RA). This receptor forms homodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. This gene is expressed at significantly lower levels in non-small cell lung cancer cells. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[1]

[edit] See also

Retinoid X receptor

[edit] References

^ ^a ^b Entrez Gene: RXRG retinoid X receptor, gamma.

[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.
Leid M, Kastner P, Lyons R, et al. (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. PMID 1310259.
Mangelsdorf DJ, Borgmeyer U, Heyman RA, et al. (1992). "Characterization of three RXR genes that mediate the action of 9-cis retinoic acid.". Genes Dev. 6 (3): 329–44. PMID 1312497.
Nagata T, Weiss EH, Abe K, et al. (1995). "Physical mapping of the retinoid X receptor B gene in mouse and human.". Immunogenetics 41 (2-3): 83–90. PMID 7806300.
Almasan A, Mangelsdorf DJ, Ong ES, et al. (1994). "Chromosomal localization of the human retinoid X receptors.". Genomics 20 (3): 397–403. doi:10.1006/geno.1994.1193. PMID 8034312.
Muscat GE, Mynett-Johnson L, Dowhan D, et al. (1994). "Activation of myoD gene transcription by 3,5,3'-triiodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors.". Nucleic Acids Res. 22 (4): 583–91. PMID 8127707.
Kamei Y, Xu L, Heinzel T, et al. (1996). "A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors.". Cell 85 (3): 403–14. PMID 8616895.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Sanno N, Sugawara A, Teramoto A, et al. (1997). "Immunohistochemical expression of retinoid X receptor isoforms in human pituitaries and pituitary adenomas.". Neuroendocrinology 65 (4): 299–306. PMID 9143002.
Reichrath J, Mittmann M, Kamradt J, Müller SM (1997). "Expression of retinoid-X receptors (-alpha,-beta,-gamma) and retinoic acid receptors (-alpha,-beta,-gamma) in normal human skin: an immunohistological evaluation.". Histochem. J. 29 (2): 127–33. PMID 9147069.
Xu XC, Sozzi G, Lee JS, et al. (1997). "Suppression of retinoic acid receptor beta in non-small-cell lung cancer in vivo: implications for lung cancer development.". J. Natl. Cancer Inst. 89 (9): 624–9. PMID 9150186.
Yusta B, Alarid ET, Gordon DF, et al. (1998). "The thyrotropin beta-subunit gene is repressed by thyroid hormone in a novel thyrotrope cell line, mouse T alphaT1 cells.". Endocrinology 139 (11): 4476–82. PMID 9794455.
Ito K, Suzuki T, Moriya T, et al. (2001). "Retinoid receptors in the human endometrium and its disorders: a possible modulator of 17 beta-hydroxysteroid dehydrogenase.". J. Clin. Endocrinol. Metab. 86 (6): 2721–7. PMID 11397877.
Kim SW, Kim HJ, Jung DJ, et al. (2001). "Retinoid-dependent antagonism of serum response factor transactivation mediated by transcriptional coactivator proteins.". Oncogene 20 (45): 6638–42. doi:10.1038/sj.onc.1204695. PMID 11641790.
Brabender J, Danenberg KD, Metzger R, et al. (2002). "The role of retinoid X receptor messenger RNA expression in curatively resected non-small cell lung cancer.". Clin. Cancer Res. 8 (2): 438–43. PMID 11839661.
Wansa KD, Harris JM, Muscat GE (2002). "The activation function-1 domain of Nur77/NR4A1 mediates trans-activation, cell specificity, and coactivator recruitment.". J. Biol. Chem. 277 (36): 33001–11. doi:10.1074/jbc.M203572200. PMID 12082103.
Wang Q, Fujii H, Knipp GT (2003). "Expression of PPAR and RXR isoforms in the developing rat and human term placentas.". Placenta 23 (8-9): 661–71. PMID 12361685.
Kimura Y, Suzuki T, Kaneko C, et al. (2003). "Retinoid receptors in the developing human lung.". Clin. Sci. 103 (6): 613–21. doi:10.1042/. PMID 12444914.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Alfaro JM, Fraile B, Lobo MV, et al. (2003). "Immunohistochemical detection of the retinoid X receptors alpha, beta, and gamma in human prostate.". J. Androl. 24 (1): 113–9. PMID 12514092.

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)	AP-2

(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	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	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)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	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	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	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

Categories: Genes on chromosome 1 | Human proteins | Chromosome 1 gene stubs | Intracellular receptors | Transcription factors

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Retinoid X receptor gamma

From Wikipedia, the free encyclopedia

[edit] See also

[edit] References

[edit] Further reading

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