Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Rxra. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Rxra
  • participates in the following biological processes:
    • positive regulation of transcription from RNA polymerase II promoter ^{[1, 3, 18]}
    • regulation of transcription, DNA-dependent ^[13]
    • retinoic acid receptor signaling pathway ^[19]
  • performs the following molecular functions:
    • 9-cis retinoic acid receptor activity ^[19]
    • chromatin DNA binding ^[6]
    • DNA binding ^{[7, 8, 11, 21]}
    • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity ^[13]
    • transcription regulatory region DNA binding ^[3]
  • is located in the following cellular components:
    • nucleus ^[6]
• The gene product of Rxra has been shown to bind to the gene products of Asxl1, Med25, Nsd1, Psmc5, Trim24. ^{[5, 10, 14, 16, 20, 24, 25]} Researchers have inferred, based on physical interactions, that the gene product of Rxra
  • performs the following molecular functions:
    • DNA binding ^[7]
    • transcription factor binding ^[16]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Rxra
  • participates in the following biological processes:
    • cardiac muscle cell proliferation ^[12]
    • heart development ^[4]
    • placenta development ^[22]
    • regulation of branching involved in prostate gland morphogenesis ^[9]
    • secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development ^[9]
    • ventricular cardiac muscle cell differentiation ^[12]
    • ventricular cardiac muscle tissue morphogenesis ^[12]
• Researchers have inferred, based on genetic interactions, that the gene product of Rxra
  • participates in the following biological processes:
    • cardiac muscle cell proliferation based on interactions with Rxrb ^[12]
    • embryo implantation based on interactions with Rxrb ^[26]
    • in utero embryonic development based on interactions with Rxrb ^[26]
    • maternal placenta development based on interactions with Rxrb ^[26]
    • positive regulation of transcription from RNA polymerase II promoter based on interactions with Arnt, Gata4, Hif1a, Rara, Rarb, Rarg, Tgif1, Zfpm2 ^{[1, 17]}
    • positive regulation of transcription, DNA-dependent based on interactions with Trim24 ^[15]
    • regulation of transcription from RNA polymerase II promoter based on interactions with Nr1h2, Nr1h4 ^[23]
    • ventricular cardiac muscle cell differentiation based on interactions with Rxrb ^[12]
  • performs the following molecular functions:
    • sequence-specific DNA binding based on interactions with Rara, Rarb ^[2]
    • sequence-specific DNA binding transcription factor activity based on interactions with Nr1h2, Nr1h4 ^[23]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Rxra:
  • participates in the following biological processes:
    • negative regulation of cell proliferation
    • negative regulation of transcription from RNA polymerase II promoter
    • peroxisome proliferator activated receptor signaling pathway
    • positive regulation of apoptotic process
    • positive regulation of transcription from RNA polymerase II promoter
    • regulation of myelination
    • regulation of transcription, DNA-dependent
    • response to glucocorticoid stimulus
    • response to retinoic acid
    • retinoic acid receptor signaling pathway
    • virus-host interaction
  • performs the following molecular functions:
    • DNA binding
    • double-stranded DNA binding
    • enzyme binding
    • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity
    • protein complex binding
    • protein domain specific binding
    • protein heterodimerization activity
    • retinoic acid receptor binding
    • retinoic acid-responsive element binding
    • sequence-specific DNA binding transcription factor activity
    • vitamin D receptor binding
  • is located in the following cellular components:
    • axon
    • nuclear chromatin
    • nucleus

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Summary text based on GO annotations supported by structural data

• Rxra encodes a protein or proteins that contain the following InterPro domains: Nuclear hormone receptor, ligand-binding, Nuclear hormone receptor, ligand-binding, core, Protein of unknown function DUF3345, Retinoid X receptor/HNF4, Steroid hormone receptor, Zinc finger, NHR/GATA-type, Zinc finger, nuclear hormone receptor-type, indicating that the gene product:
  • participates in the following biological processes:
    • steroid hormone mediated signaling pathway
  • performs the following molecular functions:
    • steroid hormone receptor activity
    • zinc ion binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Rxra indicates that it:
  • participates in the following biological processes:
    • transcription, DNA-dependent
  • performs the following molecular functions:
    • metal ion binding

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References

1. Bartholin L et al. (2006) TGIF inhibits retinoid signaling. Mol Cell Biol, 26:990-1001. (PubMed:16428452)
2. Ben-Shushan E et al. (1995) A dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and retinoic acid receptor:retinoid X receptor heterodimers regulates Oct-3/4 expression in embryonal carcinoma cells. Mol Cell Biol, 15:1034-48. (PubMed:7823919)
3. Cha JY et al. (2007) The liver X receptor (LXR) and hepatic lipogenesis. The carbohydrate-response element-binding protein is a target gene of LXR. J Biol Chem, 282:743-51. (PubMed:17107947)
4. Chen J et al. (1998) Ventricular muscle-restricted targeting of the RXRalpha gene reveals a non-cell-autonomous requirement in cardiac chamber morphogenesis. Development, 125:1943-9. (PubMed:9550726)
5. Cho YS et al. (2006) Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor. J Biol Chem, 281:17588-98. (PubMed:16606617)
6. Compe E et al. (2007) Neurological defects in trichothiodystrophy reveal a coactivator function of TFIIH. Nat Neurosci, 10:1414-22. (PubMed:17952069)
7. Guan HP et al. (2005) Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes. Genes Dev, 19:453-61. (PubMed:15681609)
8. Helledie T et al. (2002) The gene encoding the Acyl-CoA-binding protein is activated by peroxisome proliferator-activated receptor gamma through an intronic response element functionally conserved between humans and rodents. J Biol Chem, 277:26821-30. (PubMed:12015306)
9. Huang J et al. (2002) Prostatic intraepithelial neoplasia in mice with conditional disruption of the retinoid X receptor alpha allele in the prostate epithelium. Cancer Res, 62:4812-9. (PubMed:12183441)
10. Huang N et al. (1998) Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators. EMBO J, 17:3398-412. (PubMed:9628876)
11. Kabe Y et al. (2005) NF-Y is essential for the recruitment of RNA polymerase II and inducible transcription of several CCAAT box-containing genes. Mol Cell Biol, 25:512-22. (PubMed:15601870)
12. Kastner P et al. (1997) Vitamin A deficiency and mutations of RXRalpha, RXRbeta and RARalpha lead to early differentiation of embryonic ventricular cardiomyocytes. Development, 124:4749-58. (PubMed:9428411)
13. Khetchoumian K et al. (2004) TIF1delta, a novel HP1-interacting member of the transcriptional intermediary factor 1 (TIF1) family expressed by elongating spermatids. J Biol Chem, 279:48329-41. (PubMed:15322135)
14. Le Douarin B et al. (1996) A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J, 15:6701-15. (PubMed:8978696)
15. LeDouarin B et al. (1995) The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. EMBO J, 14:2020-33. (PubMed:7744009)
16. Lee HK et al. (2007) MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation. EMBO J, 26:3545-57. (PubMed:17641689)
17. Makita T et al. (2005) Retinoic acid, hypoxia, and GATA factors cooperatively control the onset of fetal liver erythropoietin expression and erythropoietic differentiation. Dev Biol, 280:59-72. (PubMed:15766748)
18. Malik S et al. (2004) Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors. Mol Cell Biol, 24:8244-54. (PubMed:15340084)
19. Mangelsdorf DJ et al. (1992) Characterization of three RXR genes that mediate the action of 9-cis retinoic acid. Genes Dev, 6:329-44. (PubMed:1312497)
20. Mathur M et al. (2001) PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol, 21:2298-311. (PubMed:11259580)
21. Nakamura K et al. (2004) Expression and regulation of multiple murine ATP-binding cassette transporter G1 mRNAs/isoforms that stimulate cellular cholesterol efflux to high density lipoprotein. J Biol Chem, 279:45980-9. (PubMed:15319426)
22. Sapin V et al. (1997) Defects of the chorioallantoic placenta in mouse RXRalpha null fetuses. Dev Biol, 191:29-41. (PubMed:9356169)
23. Seol W et al. (1995) Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors. Mol Endocrinol, 9:72-85. (PubMed:7760852)
24. Song KH et al. (2003) Molecular cloning and characterization of a novel inhibitor of apoptosis protein from Xenopus laevis. Biochem Biophys Res Commun, 301:236-42. (PubMed:12535669)
25. vom Baur E et al. (1996) Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J, 15:110-24. (PubMed:8598193)
26. Wendling O et al. (1999) Retinoid X receptors are essential for early mouse development and placentogenesis. Proc Natl Acad Sci U S A, 96:547-51. (PubMed:9892670)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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