IFNAR1

Interferon (alpha, beta and omega) receptor 1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsIFNAR1 ; AVP; IFN-alpha-REC; IFNAR; IFNBR; IFRC
External IDsOMIM: 107450 MGI: 107658 HomoloGene: 524 IUPHAR: 1723 ChEMBL: 1887 GeneCards: IFNAR1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez345415975
EnsemblENSG00000142166ENSMUSG00000022967
UniProtP17181P33896
RefSeq (mRNA)NM_000629NM_010508
RefSeq (protein)NP_000620NP_034638
Location (UCSC)Chr 21:
34.7 – 34.73 Mb		Chr 16:
91.49 – 91.51 Mb
PubMed search

Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the IFNAR1 gene.[1][2]

Function

The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor.[2]

Interactions

IFNAR1 has been shown to interact with:

References

  1. ↑ Novick D, Cohen B, Rubinstein M (Jun 1994). "The human interferon alpha/beta receptor: characterization and molecular cloning". Cell 77 (3): 391–400. doi:10.1016/0092-8674(94)90154-6. PMID 8181059.
  2. ↑ 2.0 2.1 "Entrez Gene: IFNAR1 interferon (alpha, beta and omega) receptor 1".
  3. ↑ Abramovich C, Yakobson B, Chebath J, Revel M (Jan 1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
  4. ↑ Li X, Leung S, Kerr IM, Stark GR (Apr 1997). "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling". Mol. Cell. Biol. 17 (4): 2048–56. PMC 232052. PMID 9121453.
  5. ↑ Uddin S, Chamdin A, Platanias LC (Oct 1995). "Interaction of the transcriptional activator Stat-2 with the type I interferon receptor". J. Biol. Chem. 270 (42): 24627–30. doi:10.1074/jbc.270.42.24627. PMID 7559568.
  6. ↑ Yan H, Krishnan K, Greenlund AC, Gupta S, Lim JT, Schreiber RD et al. (Mar 1996). "Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein". EMBO J. 15 (5): 1064–74. PMC 450004. PMID 8605876.
  7. ↑ Richter MF, Duménil G, Uzé G, Fellous M, Pellegrini S (Sep 1998). "Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon alpha/beta receptor component IFNAR1". J. Biol. Chem. 273 (38): 24723–9. doi:10.1074/jbc.273.38.24723. PMID 9733772.
  8. ↑ Kumar KG, Varghese B, Banerjee A, Baker DP, Constantinescu SN, Pellegrini S et al. (Jul 2008). "Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif". J. Biol. Chem. 283 (27): 18566–72. doi:10.1074/jbc.M800991200. PMC 2441555. PMID 18474601.

Further reading

  • Bürglin TR, Barnes TM (1992). "Introns in sequence tags". Nature 357 (6377): 367–8. doi:10.1038/357367a0. PMID 1350660.
  • Qiujing Y, Yuliya V K, et a, Serge Y F (2015). "DNA-Damage-Induced Type I Interferon Promotes Senescence and Inhibits Stem Cell Function". Cell Reports. doi:10.1016/j.celrep.2015.03.069.Error: vauthors format
  • Lutfalla G, Gardiner K, Proudhon D, Vielh E, Uzé G (1992). "The structure of the human interferon alpha/beta receptor gene". J. Biol. Chem. 267 (4): 2802–9. PMID 1370833.
  • Flores I, Mariano TM, Pestka S (1991). "Human interferon omega (omega) binds to the alpha/beta receptor". J. Biol. Chem. 266 (30): 19875–7. PMID 1834641.
  • Lutfalla G, Roeckel N, Mogensen KE, Mattei MG, Uzé G (1990). "Assignment of the human interferon-alpha receptor gene to chromosome 21q22.1 by in situ hybridization". J. Interferon Res. 10 (5): 515–7. doi:10.1089/jir.1990.10.515. PMID 2148760.
  • Uzé G, Lutfalla G, Gresser I (1990). "Genetic transfer of a functional human interferon alpha receptor into mouse cells: cloning and expression of its cDNA". Cell 60 (2): 225–34. doi:10.1016/0092-8674(90)90738-Z. PMID 2153461.
  • Colamonici O, Yan H, Domanski P, Handa R, Smalley D, Mullersman J et al. (1994). "Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase". Mol. Cell. Biol. 14 (12): 8133–42. PMC 359352. PMID 7526154.
  • Uddin S, Chamdin A, Platanias LC (1995). "Interaction of the transcriptional activator Stat-2 with the type I interferon receptor". J. Biol. Chem. 270 (42): 24627–30. doi:10.1074/jbc.270.42.24627. PMID 7559568.
  • Domanski P, Witte M, Kellum M, Rubinstein M, Hackett R, Pitha P et al. (1995). "Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling". J. Biol. Chem. 270 (37): 21606–11. doi:10.1074/jbc.270.37.21606. PMID 7665574.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Yan H, Krishnan K, Greenlund AC, Gupta S, Lim JT, Schreiber RD et al. (1996). "Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein". EMBO J. 15 (5): 1064–74. PMC 450004. PMID 8605876.
  • Yang CH, Shi W, Basu L, Murti A, Constantinescu SN, Blatt L et al. (1996). "Direct association of STAT3 with the IFNAR-1 chain of the human type I interferon receptor". J. Biol. Chem. 271 (14): 8057–61. doi:10.1074/jbc.271.14.8057. PMID 8626489.
  • Abramovich C, Yakobson B, Chebath J, Revel M (1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
  • Eantuzzi L, Eid P, Malorni W, Rainaldi G, Gauzzi MC, Pellegrini S et al. (1997). "Post-translational up-regulation of the cell surface-associated alpha component of the human type I interferon receptor during differentiation of peripheral blood monocytes: role in the biological response to type I interferon". Eur. J. Immunol. 27 (5): 1075–81. doi:10.1002/eji.1830270506. PMID 9174595.
  • Gessani S, Borghi P, Fantuzzi L, Varano B, Conti L, Puddu P et al. (1997). "Induction of cytokines by HIV-1 and its gp120 protein in human peripheral blood monocyte/macrophages and modulation of cytokine response during differentiation". J. Leukoc. Biol. 62 (1): 49–53. PMID 9225992.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Krishnan K, Singh B, Krolewski JJ (1998). "Identification of amino acid residues critical for the Src-homology 2 domain-dependent docking of Stat2 to the interferon alpha receptor". J. Biol. Chem. 273 (31): 19495–501. doi:10.1074/jbc.273.31.19495. PMID 9677371.
  • Richter MF, Duménil G, Uzé G, Fellous M, Pellegrini S (1998). "Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon alpha/beta receptor component IFNAR1". J. Biol. Chem. 273 (38): 24723–9. doi:10.1074/jbc.273.38.24723. PMID 9733772.
  • Rani MR, Leaman DW, Han Y, Leung S, Croze E, Fish EN et al. (1999). "Catalytically active TYK2 is essential for interferon-beta-mediated phosphorylation of STAT3 and interferon-alpha receptor-1 (IFNAR-1) but not for activation of phosphoinositol 3-kinase". J. Biol. Chem. 274 (45): 32507–11. doi:10.1074/jbc.274.45.32507. PMID 10542297.