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Interferon regulatory factor 1 (IRF-1)

 IRF1_MOUSE              Reviewed;         329 AA.
P15314;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
05-DEC-2018, entry version 153.
RecName: Full=Interferon regulatory factor 1;
Short=IRF-1;
Name=Irf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3409321; DOI=10.1016/S0092-8674(88)91307-4;
Miyamoto M., Fujita T., Kimura Y., Maruyama M., Harada H., Sudo Y.,
Miyata T., Taniguchi T.;
"Regulated expression of a gene encoding a nuclear factor, IRF-1, that
specifically binds to IFN-beta gene regulatory elements.";
Cell 54:903-913(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
UBIQUITINATION.
PubMed=10712599; DOI=10.1046/j.1432-1327.2000.01163.x;
Nakagawa K., Yokosawa H.;
"Degradation of transcription factor IRF-1 by the ubiquitin-proteasome
pathway. The C-terminal region governs the protein stability.";
Eur. J. Biochem. 267:1680-1686(2000).
[4]
REVIEW ON FUNCTION.
PubMed=11244049; DOI=10.1146/annurev.immunol.19.1.623;
Taniguchi T., Ogasawara K., Takaoka A., Tanaka N.;
"IRF family of transcription factors as regulators of host defense.";
Annu. Rev. Immunol. 19:623-655(2001).
[5]
INTERACTION WITH PIAS3, SUMOYLATION, AND FUNCTION.
PubMed=12387893; DOI=10.1016/S0014-5793(02)03486-5;
Nakagawa K., Yokosawa H.;
"PIAS3 induces SUMO-1 modification and transcriptional repression of
IRF-1.";
FEBS Lett. 530:204-208(2002).
[6]
REVIEW ON FUNCTION.
PubMed=11846971; DOI=10.1089/107999002753452610;
Kroeger A., Koester M., Schroeder K., Hauser H., Mueller P.P.;
"Activities of IRF-1.";
J. Interferon Cytokine Res. 22:5-14(2002).
[7]
REVIEW ON FUNCTION.
PubMed=11846974; DOI=10.1089/107999002753452647;
Romeo G., Fiorucci G., Chiantore M.V., Percario Z.A., Vannucchi S.,
Affabris E.;
"IRF-1 as a negative regulator of cell proliferation.";
J. Interferon Cytokine Res. 22:39-47(2002).
[8]
REVIEW ON FUNCTION.
PubMed=16932750; DOI=10.1038/nri1900;
Honda K., Taniguchi T.;
"IRFs: master regulators of signalling by Toll-like receptors and
cytosolic pattern-recognition receptors.";
Nat. Rev. Immunol. 6:644-658(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYD88.
PubMed=17018642; DOI=10.1073/pnas.0607181103;
Negishi H., Fujita Y., Yanai H., Sakaguchi S., Ouyang X.,
Shinohara M., Takayanagi H., Ohba Y., Taniguchi T., Honda K.;
"Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1
transcription factor by MyD88 in Toll-like receptor-dependent gene
induction program.";
Proc. Natl. Acad. Sci. U.S.A. 103:15136-15141(2006).
[10]
SUMOYLATION, AND FUNCTION.
PubMed=18955028; DOI=10.1016/j.bbrc.2008.10.092;
Kim E.-J., Park J.-S., Um S.-J.;
"Ubc9-mediated sumoylation leads to transcriptional repression of IRF-
1.";
Biochem. Biophys. Res. Commun. 377:952-956(2008).
[11]
FUNCTION.
PubMed=18641303; DOI=10.4049/jimmunol.181.3.1673;
Fragale A., Gabriele L., Stellacci E., Borghi P., Perrotti E.,
Ilari R., Lanciotti A., Remoli A.L., Venditti M., Belardelli F.,
Battistini A.;
"IFN regulatory factor-1 negatively regulates CD4+ CD25+ regulatory T
cell differentiation by repressing Foxp3 expression.";
J. Immunol. 181:1673-1682(2008).
[12]
REVIEW ON FUNCTION.
PubMed=20049431; DOI=10.1007/s00262-009-0804-6;
Savitsky D., Tamura T., Yanai H., Taniguchi T.;
"Regulation of immunity and oncogenesis by the IRF transcription
factor family.";
Cancer Immunol. Immunother. 59:489-510(2010).
[13]
FUNCTION.
PubMed=20308629; DOI=10.4049/jimmunol.0902264;
Stirnweiss A., Ksienzyk A., Klages K., Rand U., Grashoff M.,
Hauser H., Kroeger A.;
"IFN regulatory factor-1 bypasses IFN-mediated antiviral effects
through viperin gene induction.";
J. Immunol. 184:5179-5185(2010).
[14]
FUNCTION.
PubMed=21909274; DOI=10.1371/journal.ppat.1002230;
Brien J.D., Daffis S., Lazear H.M., Cho H., Suthar M.S., Gale M. Jr.,
Diamond M.S.;
"Interferon regulatory factor-1 (IRF-1) shapes both innate and CD8(+)
T cell immune responses against West Nile virus infection.";
PLoS Pathog. 7:E1002230-E1002230(2011).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 7-111.
PubMed=9422515; DOI=10.1038/34224;
Escalante C.R., Yie J., Thanos D., Aggarwal A.K.;
"Structure of IRF-1 with bound DNA reveals determinants of interferon
regulation.";
Nature 391:103-106(1998).
-!- FUNCTION: Transcriptional regulator which displays a remarkable
functional diversity in the regulation of cellular responses.
These include the regulation of IFN and IFN-inducible genes, host
response to viral and bacterial infections, regulation of many
genes expressed during hematopoiesis, inflammation, immune
responses and cell proliferation and differentiation, regulation
of the cell cycle and induction of growth arrest and programmed
cell death following DNA damage. Stimulates both innate and
acquired immune responses through the activation of specific
target genes and can act as a transcriptional activator and
repressor regulating target genes by binding to an interferon-
stimulated response element (ISRE) in their promoters. Its target
genes for transcriptional activation activity are: genes involved
in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I,
TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin;
antibacterial response, such as NOS2/INOS; anti-proliferative
response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as
BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7,
IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and
DNA repair, such as POLQ/POLH; MHC class I expression, such as
TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class
II expression, such as CIITA. Represses genes involved in anti-
proliferative response, such as BIRC5/survivin, CCNB1, CCNE1,
CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4,
ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription
through enhanced recruitment of EP300 leading to increased
acetylation of p53/TP53. Plays an important role in immune
response directly affecting NK maturation and activity, macrophage
production of IL12, Th1 development and maturation of CD8+ T-
cells. Also implicated in the differentiation and maturation of
dendritic cells and in the suppression of regulatory T (Treg)
cells development. Acts as a tumor suppressor and plays a role not
only in antagonism of tumor cell growth but also in stimulating an
immune response against tumor cells. {ECO:0000269|PubMed:12387893,
ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:18641303,
ECO:0000269|PubMed:18955028, ECO:0000269|PubMed:20308629,
ECO:0000269|PubMed:21909274}.
-!- ACTIVITY REGULATION: Activated by MYD88.
-!- SUBUNIT: Monomer. Homodimer. Interacts with EP300 (By similarity).
Interacts with MYD88 and PIAS3. {ECO:0000250,
ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:17018642}.
-!- INTERACTION:
Q14145:KEAP1 (xeno); NbExp=2; IntAct=EBI-6115486, EBI-751001;
P22366:Myd88; NbExp=2; IntAct=EBI-6115486, EBI-525108;
Q13114:TRAF3 (xeno); NbExp=2; IntAct=EBI-6115486, EBI-357631;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17018642}.
Cytoplasm {ECO:0000269|PubMed:17018642}. Note=MYD88-associated
IRF1 migrates into the nucleus more efficiently than non-MYD88-
associated IRF1.
-!- INDUCTION: By viruses and IFN-gamma.
-!- PTM: Phosphorylated by CK2 and this positively regulates its
activity. {ECO:0000250}.
-!- PTM: Sumoylation represses the transcriptional activity and
displays enhanced resistance to protein degradation. Inactivates
the tumor suppressor activity. Elevated levels in tumor cells.
Major site is Lys-276. Sumoylation is enhanced by PIAS3.
Desumoylated by SENP1 in tumor cells and appears to compete with
ubiquitination on C-terminal sites (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-
terminal sites (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-----------------------------------------------------------------------
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EMBL; M21065; AAA39334.1; -; mRNA.
EMBL; BC003821; AAH03821.1; -; mRNA.
CCDS; CCDS24686.1; -.
PIR; A31595; A31595.
RefSeq; NP_001152868.1; NM_001159396.1.
RefSeq; NP_032416.1; NM_008390.2.
UniGene; Mm.105218; -.
PDB; 1IF1; X-ray; 3.00 A; A/B=1-113.
PDBsum; 1IF1; -.
ProteinModelPortal; P15314; -.
SMR; P15314; -.
BioGrid; 200784; 5.
CORUM; P15314; -.
DIP; DIP-61281N; -.
IntAct; P15314; 6.
STRING; 10090.ENSMUSP00000019043; -.
iPTMnet; P15314; -.
PhosphoSitePlus; P15314; -.
EPD; P15314; -.
PaxDb; P15314; -.
PRIDE; P15314; -.
Ensembl; ENSMUST00000019043; ENSMUSP00000019043; ENSMUSG00000018899.
Ensembl; ENSMUST00000108920; ENSMUSP00000104548; ENSMUSG00000018899.
GeneID; 16362; -.
KEGG; mmu:16362; -.
UCSC; uc007iww.2; mouse.
CTD; 3659; -.
MGI; MGI:96590; Irf1.
eggNOG; ENOG410IER3; Eukaryota.
eggNOG; ENOG4111HM7; LUCA.
GeneTree; ENSGT00940000156288; -.
HOGENOM; HOG000037937; -.
HOVERGEN; HBG003455; -.
InParanoid; P15314; -.
KO; K09444; -.
OMA; CKEEPEV; -.
OrthoDB; EOG091G0CB8; -.
PhylomeDB; P15314; -.
TreeFam; TF328512; -.
EvolutionaryTrace; P15314; -.
PRO; PR:P15314; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018899; Expressed in 280 organ(s), highest expression level in subcutaneous adipose tissue.
CleanEx; MM_IRF1; -.
ExpressionAtlas; P15314; baseline and differential.
Genevisible; P15314; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:InterPro.
GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; TAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IDA:MGI.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; TAS:UniProtKB.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; TAS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:UniProtKB.
GO; GO:0002819; P:regulation of adaptive immune response; TAS:UniProtKB.
GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060416; P:response to growth hormone; ISO:MGI.
CDD; cd00103; IRF; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR019817; Interferon_reg_fac_CS.
InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
InterPro; IPR031215; IRF1.
InterPro; IPR017431; IRF1/IRF2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11949; PTHR11949; 1.
PANTHER; PTHR11949:SF3; PTHR11949:SF3; 1.
Pfam; PF00605; IRF; 1.
PIRSF; PIRSF038196; IFN_RF1/2; 1.
PRINTS; PR00267; INTFRNREGFCT.
SMART; SM00348; IRF; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00601; IRF_1; 1.
PROSITE; PS51507; IRF_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Antiviral defense;
Complete proteome; Cytoplasm; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 329 Interferon regulatory factor 1.
/FTId=PRO_0000154546.
DNA_BIND 5 113 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
MOD_RES 78 78 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10914}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
HELIX 12 20 {ECO:0000244|PDB:1IF1}.
STRAND 21 25 {ECO:0000244|PDB:1IF1}.
STRAND 29 34 {ECO:0000244|PDB:1IF1}.
TURN 48 50 {ECO:0000244|PDB:1IF1}.
STRAND 51 53 {ECO:0000244|PDB:1IF1}.
HELIX 54 61 {ECO:0000244|PDB:1IF1}.
HELIX 74 87 {ECO:0000244|PDB:1IF1}.
STRAND 89 93 {ECO:0000244|PDB:1IF1}.
STRAND 100 102 {ECO:0000244|PDB:1IF1}.
STRAND 107 109 {ECO:0000244|PDB:1IF1}.
SEQUENCE 329 AA; 37319 MW; 0E5DD23C0D977B34 CRC64;
MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK DACLFRSWAI
HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPPLTRNQR
KERKSKSSRD TKSKTKRKLC GDVSPDTFSD GLSSSTLPDD HSSYTTQGYL GQDLDMERDI
TPALSPCVVS SSLSEWHMQM DIIPDSTTDL YNLQVSPMPS TSEAATDEDE EGKIAEDLMK
LFEQSEWQPT HIDGKGYLLN EPGTQLSSVY GDFSCKEEPE IDSPRGDIGI GIQHVFTEMK
NMDSIMWMDS LLGNSVRLPP SIQAIPCAP


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