Biology:ILF3

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.[1][2]

Function

Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.[3]

Interactions

ILF3 has been shown to interact with:

Small NF90/ILF3-associated RNAs (snaR) (~120 nucleotides long) and are known to interact with ILF3 double-stranded RNA-binding motifs.[13] snaR-A is abundant in human testis and has been shown to associate with ribosomes in HeLa cells. snaR-A is present in human and gorilla but not in chimpanzee. Other snaR RNAs are found in African Great Apes (including chimpanzee and bonobo).[14]

ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus,[15][16] in canine systemic rheumatic autoimmune disease,[17] and as a rare finding in humans with autoimmune disease.[18]

References

  1. ↑ "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90". The Journal of Biological Chemistry 269 (32): 20691–9. August 1994. doi:10.1016/S0021-9258(17)32048-3. PMID 7519613. 
  2. ↑ "Identification of novel M phase phosphoproteins by expression cloning". Molecular Biology of the Cell 7 (9): 1455–69. September 1996. doi:10.1091/mbc.7.9.1455. PMID 8885239. 
  3. ↑ "Entrez Gene: ILF3 interleukin enhancer binding factor 3, 90kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3609. 
  4. ↑ "DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45". The Journal of Biological Chemistry 273 (4): 2136–45. January 1998. doi:10.1074/jbc.273.4.2136. PMID 9442054. 
  5. ↑ 5.0 5.1 "Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR". The Journal of Biological Chemistry 276 (34): 32300–12. August 2001. doi:10.1074/jbc.M104207200. PMID 11438536. 
  6. ↑ "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". The Journal of Biological Chemistry 275 (26): 19866–76. June 2000. doi:10.1074/jbc.M000023200. PMID 10749851. 
  7. ↑ "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Reports 3 (3): 268–73. March 2002. doi:10.1093/embo-reports/kvf052. PMID 11850402. 
  8. ↑ "Nuclear factor-90 of activated T-cells: A double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR". Biochemistry 38 (19): 6361–8. May 1999. doi:10.1021/bi982410u. PMID 10320367. 
  9. ↑ "Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase". The Journal of Biological Chemistry 276 (35): 32522–30. August 2001. doi:10.1074/jbc.M104408200. PMID 11438540. 
  10. ↑ "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR". The Journal of Biological Chemistry 274 (29): 20432–7. July 1999. doi:10.1074/jbc.274.29.20432. PMID 10400669. 
  11. ↑ "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins". The Journal of Cell Biology 156 (1): 53–64. January 2002. doi:10.1083/jcb.200110082. PMID 11777942. 
  12. ↑ "Multiple myeloma-associated chromosomal translocation activates orphan snoRNA ACA11 to suppress oxidative stress". The Journal of Clinical Investigation 122 (8): 2793–806. August 2012. doi:10.1172/jci63051. PMID 22751105. 
  13. ↑ "Novel rapidly evolving hominid RNAs bind nuclear factor 90 and display tissue-restricted distribution". Nucleic Acids Research 35 (18): 6249–58. 2007. doi:10.1093/nar/gkm668. PMID 17855395. 
  14. ↑ "The evolution and expression of the snaR family of small non-coding RNAs". Nucleic Acids Research 39 (4): 1485–500. March 2011. doi:10.1093/nar/gkq856. PMID 20935053. 
  15. ↑ "Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity". The Journal of Biological Chemistry 274 (49): 34598–604. December 1999. doi:10.1074/jbc.274.49.34598. PMID 10574923. 
  16. ↑ "Induction of lupus-related specific autoantibodies by non-specific inflammation caused by an intraperitoneal injection of n-hexadecane in BALB/c mice". Toxicology 218 (2–3): 186–96. February 2006. doi:10.1016/j.tox.2005.10.011. PMID 16309812. 
  17. ↑ "ILF2 and ILF3 are autoantigens in canine systemic autoimmune disease". Scientific Reports 8 (1): 4852. March 2018. doi:10.1038/s41598-018-23034-w. PMID 29556082. Bibcode: 2018NatSR...8.4852B. 
  18. ↑ "Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity". The Journal of Biological Chemistry 274 (49): 34598–604. December 1999. doi:10.1074/jbc.274.49.34598. PMID 10574923. 

Further reading

External links

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



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