ID IRF1_BOVIN Reviewed; 322 AA.
AC Q3SZP0; Q865L0;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-SEP-2014, entry version 77.
DE RecName: Full=Interferon regulatory factor 1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Davis J.S., Hou X.;
RT "Molecular cloning of Bos taurus interferon regulatory factor 1.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional regulator which displays a remarkable
CC functional diversity in the regulation of cellular responses.
CC These include the regulation of IFN and IFN-inducible genes, host
CC response to viral and bacterial infections, regulation of many
CC genes expressed during hematopoiesis, inflammation, immune
CC responses and cell proliferation and differentiation, regulation
CC of the cell cycle and induction of growth arrest and programmed
CC cell death following DNA damage. Stimulates both innate and
CC acquired immune responses through the activation of specific
CC target genes and can act as a transcriptional activator and
CC repressor regulating target genes by binding to an interferon-
CC stimulated response element (ISRE) in their promoters. Its target
CC genes for transcriptional activation activity include: genes
CC involved in anti-viral response, such as IFN-alpha/beta,
CC DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and
CC RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-
CC proliferative response, such as p53/TP53, LOX and CDKN1A;
CC apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune
CC response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA
CC damage responses and DNA repair, such as POLQ/POLH; MHC class I
CC expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and
CC B2M and MHC class II expression, such as CIITA. Represses genes
CC involved in anti-proliferative response, such as BIRC5/survivin,
CC CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as
CC FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent
CC transcription through enhanced recruitment of EP300 leading to
CC increased acetylation of p53/TP53. Plays an important role in
CC immune response directly affecting NK maturation and activity,
CC macrophage production of IL12, Th1 development and maturation of
CC CD8+ T-cells. Also implicated in the differentiation and
CC maturation of dendritic cells and in the suppression of regulatory
CC T (Treg) cells development. Acts as a tumor suppressor and plays a
CC role not only in antagonism of tumor cell growth but also in
CC stimulating an immune response against tumor cells (By
CC -!- ENZYME REGULATION: Activated by MYD88 (By similarity).
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with EP300, PIAS3 and MYD88
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Note=MYD88-associated IRF1 migrates into the nucleus
CC more efficiently than non-MYD88-associated IRF1 (By similarity).
CC -!- PTM: Phosphorylated by CK2 and this positively regulates its
CC activity (By similarity).
CC -!- PTM: Sumoylation represses the transcriptional activity and
CC displays enhanced resistance to protein degradation. Inactivates
CC the tumor suppressor activity. Elevated levels in tumor cells.
CC Major site is Lys-276. Sumoylation is enhanced by PIAS3 (By
CC similarity). Desumoylated by SENP1 in tumor cells and appears to
CC compete with ubiquitination on C-terminal sites (By similarity).
CC -!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-
CC terminal sites (By similarity).
CC -!- SIMILARITY: Belongs to the IRF family.
CC -!- SIMILARITY: Contains 1 IRF tryptophan pentad repeat DNA-binding
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DR EMBL; AY204899; AAO46998.1; -; mRNA.
DR EMBL; BC102766; AAI02767.1; -; mRNA.
DR RefSeq; NP_001178190.1; NM_001191261.2.
DR RefSeq; XP_003584774.1; XM_003584726.2.
DR UniGene; Bt.102576; -.
DR UniGene; Bt.87587; -.
DR UniGene; Bt.89067; -.
DR ProteinModelPortal; Q3SZP0; -.
DR SMR; Q3SZP0; 7-111.
DR STRING; 9913.ENSBTAP00000041732; -.
DR PRIDE; Q3SZP0; -.
DR Ensembl; ENSBTAT00000044218; ENSBTAP00000041732; ENSBTAG00000031231.
DR GeneID; 337917; -.
DR GeneID; 789216; -.
DR KEGG; bta:337917; -.
DR KEGG; bta:789216; -.
DR CTD; 3659; -.
DR eggNOG; NOG42582; -.
DR GeneTree; ENSGT00740000114956; -.
DR HOGENOM; HOG000037937; -.
DR HOVERGEN; HBG003455; -.
DR InParanoid; Q3SZP0; -.
DR KO; K09444; -.
DR OrthoDB; EOG72ZCFD; -.
DR TreeFam; TF328512; -.
DR Reactome; REACT_215067; Factors involved in megakaryocyte development and platelet production.
DR Reactome; REACT_218986; TRAF6 mediated IRF7 activation.
DR NextBio; 20929556; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 22.214.171.124; -; 1.
DR InterPro; IPR017431; Interferon_reg_fac-1/2.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00605; IRF; 1.
DR PIRSF; PIRSF038196; IFN_RF1/2; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Antiviral defense; Complete proteome;
KW Cytoplasm; DNA-binding; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1 322 Interferon regulatory factor 1.
FT DNA_BIND 5 113 IRF tryptophan pentad repeat.
FT MOD_RES 78 78 N6-acetyllysine (By similarity).
FT CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO) (By
FT CROSSLNK 296 296 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO) (By
FT CONFLICT 302 302 L -> W (in Ref. 1; AAO46998).
SQ SEQUENCE 322 AA; 36168 MW; 273CA27DAE5DB7BB CRC64;
MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK DACLFRSWAI
HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPPLTKSQR
KERKSKSSRD ARSKAKKKPY GEYSPDTFSD GLSSSTLPDD HSNYTVRSYM GQDLDIERTL
TPALSPCGVS STLPNWSIPV EIVPDSTSDL YNFQVSPMPS TSEAATDEDE EGKLTEDIMK
LLEQTGWQQT SVDGKGYLLN EPGAQPTSVY GEFSCKEEPE VDSPGGYIGL ISSDMKNMDP
SLLDSLLTPV RLPSIQAIPC AP