Irf7
entrez
54123
canonical
uniprot
P70434
canonical
ensembl
ENSMUSG00000025498
resolver
ensp
ENSMUSP00000026571
resolver
ensp
ENSMUSP00000095565
resolver
ensp
ENSMUSP00000101644
resolver
ensp
ENSMUSP00000284117
resolver
enst
ENSMUST00000026571
resolver
enst
ENSMUST00000097952
resolver
enst
ENSMUST00000106023
resolver
genesymbol
Irf7
resolver
uniprot
D3Z4U9
resolver
uniprot
F6XAN1
resolver
uniprot
Q3TW14
resolver
uniprot
Q542T3
resolver
uniprot_entry
D3Z4U9_MOUSE
resolver
uniprot_entry
F6XAN1_MOUSE
resolver
uniprot_entry
IRF7_MOUSE
resolver
uniprot_entry
Q3TW14_MOUSE
resolver
uniprot_entry
Q542T3_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: In the absence of viral infection, maintained as a monomer in an autoinhibited state and phosphorylation disrupts this autoinhibition leading to the liberation of the DNA-binding and dimerization activities and its nuclear localization where it can activate type I IFN and ISG genes.
uniprot
proteins
amino_acid_sequence
MAEVRGVQRVLFGDWLLGEVSSGQYEGLQWLNEARTVFRVPWKHFGRRDLDEEDAQIFKAWAVARGRWPPSGVNLPPPEAEAAERRERRGWKTNFRCALHSTGRFILRQDNSGDPVDPHKVYELSRELGSTVGPATENREEVSLSNALPTQGVSPGSFLARENAGLQTPSPLLSSDAGDLLLQVLQYSHILESESGADPVPPQAPGQEQDRVYEEPYAAWQVEAVPSPRPQQPALTERSLGFLDVTIMYKGRTVLQAVVGHPRCVFLYSPMAPAVRTSEPQPVIFPSPAELPDQKQLHYTETLLQHVSPGLQLELRGPSLWALRMGKCKVYWEVGSPMGTTGPSTPPQLLERNRHTPIFDFSTFFRELEEFRARRRQGSPHYTIYLGFGQDLSAGRPKEKTLILVKLEPWVCKAYLEGVQREGVSSLDSSSLGLCLSSTNSLYEDIEHFLMDLGQWP
uniprot
proteins
function
FUNCTION: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22095711, PubMed:27129230). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (PubMed:27129230). Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages. {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15743772, ECO:0000269|PubMed:15800576, ECO:0000269|PubMed:18562536, ECO:0000269|PubMed:22095711, ECO:0000269|PubMed:27129230}.
uniprot
proteins
mass_dalton
51222
uniprot
proteins
mutagenesis
MUTAGEN 425; /note="S->A: Strongly decreased transcriptional activation in response to viral infection; when associated with A-426."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 425; /note="S->D: Strongly decreased transcriptional activation in response to viral infection; when associated with D-426."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 426; /note="S->A: Strongly decreased transcriptional activation in response to viral infection; when associated with A-425."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 426; /note="S->D: Strongly decreased transcriptional activation in response to viral infection; when associated with D-425."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 427; /note="L->A: Strongly decreased transcriptional activation in response to viral infection."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 427; /note="L->D: No effect on transcriptional activation in response to viral infection."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 429..431; /note="SSS->AAA: Almost no effect on transcriptional activation in response to viral infection."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 429..431; /note="SSS->DDD: Strongly increased transcriptional activation in response to viral infection."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 437; /note="S->A: Almost complete loss of transcriptional activation; when associated with A-438."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 437; /note="S->D: Increased transcriptional activation; when associated with D-438."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 438; /note="S->A: Almost complete loss of transcriptional activation; when associated with A-437."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 438; /note="S->D: Increased transcriptional activation; when associated with D-437."; /evidence="ECO:0000269|PubMed:15743772"; MUTAGEN 441; /note="S->A: Almost no effect on transcriptional activation in response to viral infection."; /evidence="ECO:0000269|PubMed:15743772
uniprot
proteins
post_translational_modification
PTM: Acetylation inhibits its DNA-binding ability and activity. {ECO:0000250}.; PTM: In response to a viral infection, phosphorylated by TBK1 and IKBKE1. Phosphorylation, and subsequent activation is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated signaling pathway, phosphorylated by IRAK1 (By similarity). {ECO:0000250}.; PTM: TRAF6-mediated ubiquitination is required for IRF7 activation (PubMed:15361868, PubMed:22095711). TRIM35 mediates IRF7 'Lys-48'-linked polyubiquitination and subsequent proteasomal degradation (By similarity). 'Lys-48'-linked polyubiquitination and subsequent proteasomal degradation is NMI-dependent in response to Sendai virus infection (PubMed:23956435). Ubiquitinated by UBE3C, leading to its degradation (By similarity). {ECO:0000250|UniProtKB:Q92985, ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:22095711, ECO:0000269|PubMed:23956435}.; PTM: Sumoylated by TRIM28, which inhibits its transactivation activity. {ECO:0000250}.; PTM: 'Lys-63'-linked ubiquitination by NEURL3 promotes IRF7 activation. {ECO:0000250|UniProtKB:Q92985}.
uniprot
proteins
protein_family
IRF family
uniprot
proteins
pubmed
11846980
uniprot
proteins
pubmed
15361868
uniprot
proteins
pubmed
15743772
uniprot
proteins
pubmed
15800576
uniprot
proteins
pubmed
16846591
uniprot
proteins
pubmed
16979567
uniprot
proteins
pubmed
18562536
uniprot
proteins
pubmed
20049431
uniprot
proteins
pubmed
21490621
uniprot
proteins
pubmed
22095711
uniprot
proteins
pubmed
23956435
uniprot
proteins
pubmed
27129230
uniprot
proteins
sequence_length
457
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15361868}. Cytoplasm {ECO:0000269|PubMed:15361868}. Note=The phosphorylated and active form accumulates selectively in the nucleus.
uniprot
proteins