IRF7

Protein-coding gene in the species Homo sapiens
IRF7
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2O61

Identifiers
AliasesIRF7, IRF-7H, IRF7A, IRF7B, IRF7C, IRF7H, IMD39, interferon regulatory factor 7, IRF-7
External IDsOMIM: 605047 MGI: 1859212 HomoloGene: 128624 GeneCards: IRF7
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for IRF7
Genomic location for IRF7
Band11p15.5Start612,553 bp[1]
End615,983 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for IRF7
Genomic location for IRF7
Band7|7 F5Start140,842,619 bp[2]
End140,846,394 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • right lobe of liver

  • spleen

  • monocyte

  • lymph node

  • bone marrow

  • bone marrow cells

  • sural nerve

  • appendix

  • left lobe of thyroid gland
Top expressed in
  • blood

  • mucous cell of stomach

  • ileum

  • jejunum

  • duodenum

  • large intestine

  • colon

  • thymus

  • spleen

  • submandibular gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • DNA-binding transcription factor activity
  • protein binding
  • RNA polymerase II core promoter sequence-specific DNA binding
  • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • cis-regulatory region sequence-specific DNA binding
Cellular component
  • nucleoplasm
  • endosome membrane
  • nucleus
  • cytoplasm
  • cytosol
Biological process
  • positive regulation of type I interferon-mediated signaling pathway
  • regulation of transcription, DNA-templated
  • positive regulation of interferon-alpha production
  • MDA-5 signaling pathway
  • interferon-gamma-mediated signaling pathway
  • immune system process
  • regulation of adaptive immune response
  • response to virus
  • negative regulation of transcription by RNA polymerase II
  • transcription by RNA polymerase II
  • transcription, DNA-templated
  • regulation of type I interferon production
  • cellular response to DNA damage stimulus
  • TRIF-dependent toll-like receptor signaling pathway
  • positive regulation of transcription, DNA-templated
  • negative regulation of macrophage apoptotic process
  • type I interferon signaling pathway
  • immunoglobulin mediated immune response
  • establishment of viral latency
  • regulation of immune response
  • viral process
  • regulation of monocyte differentiation
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of interferon-beta production
  • interferon-beta production
  • regulation of MyD88-independent toll-like receptor signaling pathway
  • positive regulation of type I interferon production
  • innate immune response
  • regulation of MyD88-dependent toll-like receptor signaling pathway
  • interferon-alpha production
  • defense response to virus
  • regulation of gene expression
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3665

54123

Ensembl

ENSG00000276561
ENSG00000185507

ENSMUSG00000025498

UniProt

Q92985

P70434

RefSeq (mRNA)

NM_001572
NM_004029
NM_004030
NM_004031

NM_001252600
NM_001252601
NM_016850

RefSeq (protein)

NP_001563
NP_004020
NP_004022

NP_001239529
NP_001239530
NP_058546

Location (UCSC)Chr 11: 0.61 – 0.62 MbChr 7: 140.84 – 140.85 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interferon regulatory factor 7, also known as IRF7, is a member of the interferon regulatory factor family of transcription factors.

Function

IRF7 encodes interferon regulatory factor 7, a member of the interferon regulatory transcription factor (IRF) family. IRF7 has been shown to play a role in the transcriptional activation of virus-inducible cellular genes, including the type I interferon genes. In particular, IRF7 regulates many interferon-alpha genes.[5] Constitutive expression of IRF7 is largely restricted to lymphoid tissue, largely plasmacytoid dendritic cells, whereas IRF7 is inducible in many tissues. Multiple IRF7 transcript variants have been identified, although the functional consequences of these have not yet been established.[6]

The IRF7 pathway was shown to be silenced in some metastatic breast cancer cell lines, which may help the cells avoid the host immune response.[7] Restoring IRF7 to these cell lines reduced metastases and increased host survival time in animal models.

The IRF7 gene and product were shown to be defective in a patient with severe susceptibility to H1N1 influenza, while susceptibility to other viral diseases such as CMV, RSV, and parainfluenza was unaffected.[8]

Interactions

IRF7 has been shown to interact with IRF3.[9] Also, IRF7 has been shown to interact with Aryl Hydrocarbon Receptor Interacting Protein (AIP), which is a negative regulator for the antiviral pathway.[10]

See also

References

  1. ^ a b c ENSG00000185507 GRCh38: Ensembl release 89: ENSG00000276561, ENSG00000185507 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025498 – 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. ^ Marié I, Durbin JE, Levy DE (November 1998). "Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7". The EMBO Journal. 17 (22): 6660–9. doi:10.1093/emboj/17.22.6660. PMC 1171011. PMID 9822609.
  6. ^ "Entrez Gene: IRF7 interferon regulatory factor 7".
  7. ^ Bidwell (2012). "Silencing of Irf7 pathways in breast cancer cells promotes bone metastasis through immune escape". Nature Medicine. 18 (8): 1224–1231. doi:10.1038/nm.2830. PMID 22820642. S2CID 6727932.
  8. ^ Ciancanelli MJ, Huang SX, Luthra P, Garner H, Itan Y, Volpi S, Lafaille FG, Trouillet C, Schmolke M, Albrecht RA, Israelsson E, Lim HK, Casadio M, Hermesh T, Lorenzo L, Leung LW, Pedergnana V, Boisson B, Okada S, Picard C, Ringuier B, Troussier F, Chaussabel D, Abel L, Pellier I, Notarangelo LD, García-Sastre A, Basler CF, Geissmann F, Zhang SY, Snoeck HW, Casanova JL (April 2015). "Infectious disease. Life-threatening influenza and impaired interferon amplification in human IRF7 deficiency". Science. 348 (6233): 448–53. doi:10.1126/science.aaa1578. PMC 4431581. PMID 25814066.
  9. ^ Au WC, Yeow WS, Pitha PM (February 2001). "Analysis of functional domains of interferon regulatory factor 7 and its association with IRF-3". Virology. 280 (2): 273–82. doi:10.1006/viro.2000.0782. PMID 11162841.
  10. ^ Zhou Q, Lavorgna A, Bowman M, Hiscott J, Harhaj EW (June 2015). "Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon". The Journal of Biological Chemistry. 290 (23): 14729–39. doi:10.1074/jbc.M114.633065. PMC 4505538. PMID 25911105.

Further reading

  • Ning S, Pagano JS, Barber GN (September 2011). "IRF7: activation, regulation, modification and function". Genes and Immunity. 12 (6): 399–414. doi:10.1038/gene.2011.21. PMC 4437765. PMID 21490621.
  • Pitha PM, Au WC, Lowther W, Juang YT, Schafer SL, Burysek L, Hiscott J, Moore PA (1999). "Role of the interferon regulatory factors (IRFs) in virus-mediated signaling and regulation of cell growth". Biochimie. 80 (8–9): 651–8. doi:10.1016/S0300-9084(99)80018-2. PMID 9865487.
  • Zhang L, Pagano JS (January 2002). "Structure and function of IRF-7". Journal of Interferon & Cytokine Research. 22 (1): 95–101. doi:10.1089/107999002753452700. PMID 11846980.
  • Zhang L, Pagano JS (October 1997). "IRF-7, a new interferon regulatory factor associated with Epstein-Barr virus latency". Molecular and Cellular Biology. 17 (10): 5748–57. doi:10.1128/MCB.17.10.5748. PMC 232423. PMID 9315633.
  • Wathelet MG, Lin CH, Parekh BS, Ronco LV, Howley PM, Maniatis T (March 1998). "Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo". Molecular Cell. 1 (4): 507–18. doi:10.1016/S1097-2765(00)80051-9. PMID 9660935.
  • Au WC, Moore PA, LaFleur DW, Tombal B, Pitha PM (October 1998). "Characterization of the interferon regulatory factor-7 and its potential role in the transcription activation of interferon A genes". The Journal of Biological Chemistry. 273 (44): 29210–7. doi:10.1074/jbc.273.44.29210. PMID 9786932.
  • Lu R, Au WC, Yeow WS, Hageman N, Pitha PM (October 2000). "Regulation of the promoter activity of interferon regulatory factor-7 gene. Activation by interferon and silencing by hypermethylation". The Journal of Biological Chemistry. 275 (41): 31805–12. doi:10.1074/jbc.M005288200. PMID 10924517.
  • Paris MJ, Williams BR (October 2000). "Characterization of a 500-kb contig spanning the region between c-Ha-Ras and MUC2 on chromosome 11p15.5". Genomics. 69 (2): 196–202. doi:10.1006/geno.2000.6339. PMID 11031102.
  • Marié I, Smith E, Prakash A, Levy DE (December 2000). "Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain". Molecular and Cellular Biology. 20 (23): 8803–14. doi:10.1128/MCB.20.23.8803-8814.2000. PMC 86519. PMID 11073981.
  • Smith EJ, Marié I, Prakash A, García-Sastre A, Levy DE (March 2001). "IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein". The Journal of Biological Chemistry. 276 (12): 8951–7. doi:10.1074/jbc.M008717200. PMID 11124948.
  • Au WC, Yeow WS, Pitha PM (February 2001). "Analysis of functional domains of interferon regulatory factor 7 and its association with IRF-3". Virology. 280 (2): 273–82. doi:10.1006/viro.2000.0782. PMID 11162841.
  • Lu R, Moore PA, Pitha PM (May 2002). "Stimulation of IRF-7 gene expression by tumor necrosis factor alpha: requirement for NFkappa B transcription factor and gene accessibility". The Journal of Biological Chemistry. 277 (19): 16592–8. doi:10.1074/jbc.M111440200. PMID 11877397.
  • Morin P, Bragança J, Bandu MT, Lin R, Hiscott J, Doly J, Civas A (March 2002). "Preferential binding sites for interferon regulatory factors 3 and 7 involved in interferon-A gene transcription". Journal of Molecular Biology. 316 (5): 1009–22. doi:10.1006/jmbi.2001.5401. PMID 11884139.
  • Caillaud A, Prakash A, Smith E, Masumi A, Hovanessian AG, Levy DE, Marié I (December 2002). "Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein (CBP)-associated factor (PCAF) impairs its DNA binding". The Journal of Biological Chemistry. 277 (51): 49417–21. doi:10.1074/jbc.M207484200. PMID 12374802.
  • Izmailova E, Bertley FM, Huang Q, Makori N, Miller CJ, Young RA, Aldovini A (February 2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages". Nature Medicine. 9 (2): 191–7. doi:10.1038/nm822. PMID 12539042. S2CID 26145639.
  • Yang H, Lin CH, Ma G, Baffi MO, Wathelet MG (May 2003). "Interferon regulatory factor-7 synergizes with other transcription factors through multiple interactions with p300/CBP coactivators". The Journal of Biological Chemistry. 278 (18): 15495–504. doi:10.1074/jbc.M212940200. PMID 12604599.
  • Ning S, Hahn AM, Huye LE, Pagano JS (September 2003). "Interferon regulatory factor 7 regulates expression of Epstein-Barr virus latent membrane protein 1: a regulatory circuit". Journal of Virology. 77 (17): 9359–68. doi:10.1128/JVI.77.17.9359-9368.2003. PMC 187426. PMID 12915551.
  • Fitzgerald KA, Rowe DC, Barnes BJ, Caffrey DR, Visintin A, Latz E, Monks B, Pitha PM, Golenbock DT (October 2003). "LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF". The Journal of Experimental Medicine. 198 (7): 1043–55. doi:10.1084/jem.20031023. PMC 2194210. PMID 14517278.
  • Lin R, Noyce RS, Collins SE, Everett RD, Mossman KL (February 2004). "The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes". Journal of Virology. 78 (4): 1675–84. doi:10.1128/JVI.78.4.1675-1684.2004. PMC 369457. PMID 14747533.

External links

  • Media related to Interferon regulatory factor-7 at Wikimedia Commons
  • IRF7+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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

  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies


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