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IFNAR1

Summary

Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the IFNAR1 gene.[5][6]

IFNAR1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, interferon alpha and beta receptor subunit 1
External IDsOMIM: 107450 MGI: 107658 HomoloGene: 524 GeneCards: IFNAR1
Orthologs
SpeciesHumanMouse
Entrez

3454

15975

Ensembl

ENSG00000142166

ENSMUSG00000022967

UniProt

P17181

P33896

RefSeq (mRNA)

NM_000629

NM_010508

RefSeq (protein)

NP_000620

NP_034638

Location (UCSC)Chr 21: 33.32 – 33.36 MbChr 16: 91.28 – 91.3 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for type I interferons, including interferon-alpha, -beta, and -lambda. 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.[6]

Interactions edit

IFNAR1 has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142166 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022967 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 140206806.
  6. ^ a b "Entrez Gene: IFNAR1 interferon (alpha, beta and omega) receptor 1".
  7. ^ 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.
  8. ^ 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. doi:10.1128/mcb.17.4.2048. PMC 232052. PMID 9121453.
  9. ^ 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.
  10. ^ Yan H, Krishnan K, Greenlund AC, Gupta S, Lim JT, Schreiber RD, Schindler CW, Krolewski JJ (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. doi:10.1002/j.1460-2075.1996.tb00444.x. PMC 450004. PMID 8605876.
  11. ^ 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.
  12. ^ Kumar KG, Varghese B, Banerjee A, Baker DP, Constantinescu SN, Pellegrini S, Fuchs SY (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 edit

  • Bürglin TR, Barnes TM (1992). "Introns in sequence tags". Nature. 357 (6377): 367–8. Bibcode:1992Natur.357..367B. doi:10.1038/357367a0. PMID 1350660. S2CID 2693051.
  • Qiujing Yu; Yuliya V Katlinskaya; et al. (2015). "DNA-Damage-Induced Type I Interferon Promotes Senescence and Inhibits Stem Cell Function". Cell Reports. 11 (5): 785–797. doi:10.1016/j.celrep.2015.03.069. PMC 4426031. PMID 25921537.
  • 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. doi:10.1016/S0021-9258(18)45950-9. 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. doi:10.1016/S0021-9258(18)54862-6. 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. S2CID 54409221.
  • Colamonici O, Yan H, Domanski P, Handa R, Smalley D, Mullersman J, Witte M, Krishnan K, Krolewski J (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. doi:10.1128/mcb.14.12.8133. 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, Colamonici OR (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, Schindler CW, Krolewski JJ (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. doi:10.1002/j.1460-2075.1996.tb00444.x. PMC 450004. PMID 8605876.
  • Yang CH, Shi W, Basu L, Murti A, Constantinescu SN, Blatt L, Croze E, Mullersman JE, Pfeffer LM (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, Belardelli F, Gessani S (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. S2CID 6569287.
  • Gessani S, Borghi P, Fantuzzi L, Varano B, Conti L, Puddu P, Belardelli F (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. doi:10.1002/jlb.62.1.49. PMID 9225992. S2CID 31546644.
  • 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, Wolfman A, Ransohoff RM (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.