AC T01333
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ID T01333
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DT 25.10.1994 (created); ewi.
DT 11.12.2015 (updated); sup.
CO Copyright (C), QIAGEN.
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FA RXR-gamma
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SY NR2B3; retinoid X receptor gamma; RXR-gamma; RXRG.
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OS mouse, Mus musculus
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae
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GE G006696 Rxrg.
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CL C0002; CC (rec); 2.1.3.1.3.
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SF 2 mRNA-species with 1.9 and 2.3 kb exist;
SF T-box important for interaction with other nuclear receptors in DNA-binding (heterodimerization) [7];
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CP (embryo:) E12.5, E13.5, E14.5, E15.5, E16.5, E17.5, E18.5 [3]; E10-E13 (in situ): somites [3]; E11 (in situ): pituitary [3]; E13.5 (in situ): corpus striatum [3]; E16.5 (in situ): strong signals in corpus striatum, pituitary, weaker signals in neck, skeletal muscle, tongue [3]; (adult:) heart, muscle; (intermediate:) liver; (weak:) brain, kidney, adrenal, lung, skin [3].
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FF natural occurring high affinity ligand (retinoid X) is 9-cis retinoic acid which induces transactivation activity [3];
FF responds to a variety of endogenous retinoids, but again 9-cis retinoic acid is most potent ligand with high transactivation activity (up to 40-fold more active than all-trans retinoic acid) [3];
FF all-trans retinoic acid, which is a low affinity ligand, could serve as a metabolic precursor for a high affinity ligands like 9-cis retinoic acid [3];
FF AF-2 is ligand-inducible and promoter context-dependent;
FF modulating function is also promoter context-dependent, but ligand-independent;
FF can bind as a heterodimeric complex with T3R-alpha to a TRE of myoD gene during muscle cell differentiation [5];
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IN T08499 CBP; mouse, Mus musculus.
IN T01354 PPARgamma; clawed frog, Xenopus laevis.
IN T01330 RAR-gamma1; human, Homo sapiens.
IN T00720 RAR-gamma; human, Homo sapiens.
IN T01329 RAR-gamma; mouse, Mus musculus.
IN T01351 T3R-alpha; chick, Gallus gallus.
IN T02143 TIF1; mouse, Mus musculus.
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MX M00963 V$T3R_Q6.
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BS R01321.
BS R39981.
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DR TRANSPATH: MO000025592.
DR UniProtKB: P28705;
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RN [1]; RE0000265.
RX PUBMED: 1310259.
RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewski T., Chen J.-Y., Staub A., Garnier J.-M., Mader S., Chambon P.
RT Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently
RL Cell 68:377-395 (1992).
RN [2]; RE0000270.
RX PUBMED: 1326406.
RA Nagpal S., Saunders M., Kastner P., Durand B., Nakshatri H., Chambon P.
RT Promoter context-and response element-dependent specificity of the transcriptional activation and modulating functions of retinoic acid receptors
RL Cell 70:1007-1019 (1992).
RN [3]; RE0000789.
RX PUBMED: 1312497.
RA Mangelsdorf D. J., Borgmeyer U., Heyman R. A., Zhou J. Y., Ong E. S., Oro A. E., Kakizuka A., Evans R. M.
RT Characterization of three RXR genes that mediate the action of 9-cis retinoic acid
RL Genes Dev. 6:329-344 (1992).
RN [4]; RE0002413.
RX PUBMED: 2554307.
RA Hamada K., Gleason S., Levi B.-Z., Hirschfeld S., Apella E., Ozato K.
RT H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds to both the regulatory element of major histocompatibility class I genes and the estrogen response element
RL Proc. Natl. Acad. Sci. USA 86:8289-8293 (1989).
RN [5]; RE0003240.
RX PUBMED: 8127707.
RA Muscat G. E. O., Mynett-Johnson L., Dowhan D., Downes M., Griggs R.
RT Activation of MyoD gene transcription by 3, 4, 3'-triiodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors
RL Nucleic Acids Res. 22:583-591 (1994).
RN [6]; RE0013625.
RX PUBMED: 10219237.
RA Nuclear Receptors Nomenclature Committee.
RT A unified nomenclature system for the nuclear receptor superfamily
RL Cell 97:161-163 (1999).
RN [7]; RE0017065.
RX PUBMED: 9242684.
RA IJpenberg A., Jeannin E., Wahli W., Desvergne B.
RT Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. A functional analysis of the malic enzyme gene PPAR response element
RL J. Biol. Chem. 272:20108-20117 (1997).
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