IRF1_BOVIN
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-AUG-2022, entry version 116.
DE RecName: Full=Interferon regulatory factor 1;
DE Short=IRF-1;
GN Name=IRF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
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.
RN [2]
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 (By
CC similarity). Regulates transcription of IFN and IFN-inducible genes,
CC host response to viral and bacterial infections, regulation of many
CC genes expressed during hematopoiesis, inflammation, immune responses
CC and cell proliferation and differentiation, regulation of the cell
CC cycle and induction of growth arrest and programmed cell death
CC following DNA damage (By similarity). Stimulates both innate and
CC acquired immune responses through the activation of specific target
CC genes and can act as a transcriptional activator and repressor
CC regulating target genes by binding to an interferon-stimulated response
CC element (ISRE) in their promoters (By similarity). Binds to a consensus
CC sequence in gene promoters (By similarity). Its target genes for
CC transcriptional activation activity include: genes involved in anti-
CC viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL,
CC ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial
CC response, such as NOS2/INOS; anti-proliferative response, such as
CC p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7
CC and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2
CC and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC
CC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B
CC and B2M and MHC class II expression, such as CIITA; metabolic enzymes,
CC such as ACOD1/IRG1 (By similarity). Represses genes involved in anti-
CC proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1,
CC CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and
CC TLR4 (By similarity). Stimulates p53/TP53-dependent transcription
CC through enhanced recruitment of EP300 leading to increased acetylation
CC of p53/TP53. Plays an important role in immune response directly
CC affecting NK maturation and activity, macrophage production of IL12,
CC Th1 development and maturation of CD8+ T-cells (By similarity). Also
CC implicated in the differentiation and maturation of dendritic cells and
CC in the suppression of regulatory T (Treg) cells development (By
CC similarity). Acts as a tumor suppressor and plays a role not only in
CC antagonism of tumor cell growth but also in stimulating an immune
CC response against tumor cells (By similarity).
CC {ECO:0000250|UniProtKB:P10914}.
CC -!- ACTIVITY REGULATION: Activated by MYD88.
CC {ECO:0000250|UniProtKB:P15314}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (By similarity). Interacts
CC with EP300 (By similarity). Interacts with MYD88 (By similarity).
CC Interacts with PIAS3 (By similarity). {ECO:0000250|UniProtKB:P10914,
CC ECO:0000250|UniProtKB:P15314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15314}. Cytoplasm
CC {ECO:0000250|UniProtKB:P15314}. Note=MYD88-associated IRF1 migrates
CC into the nucleus more efficiently than non-MYD88-associated IRF1.
CC {ECO:0000250|UniProtKB:P15314}.
CC -!- PTM: Phosphorylated by CK2 and this positively regulates its activity.
CC {ECO:0000250|UniProtKB:P10914}.
CC -!- PTM: Sumoylation represses the transcriptional activity and displays
CC enhanced resistance to protein degradation (By similarity). Sumolyated
CC by UBE2I/UBC9 and SUMO1 (By similarity). Inactivates the tumor
CC suppressor activity (By similarity). Elevated levels in tumor cells.
CC Major site is Lys-276 (By similarity). Sumoylation is enhanced by PIAS3
CC (By similarity). Desumoylated by SENP1 in tumor cells and appears to
CC compete with ubiquitination on C-terminal sites (By similarity).
CC {ECO:0000250|UniProtKB:P10914, ECO:0000250|UniProtKB:P15314}.
CC -!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-terminal
CC sites (By similarity). {ECO:0000250|UniProtKB:P10914}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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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 AlphaFoldDB; Q3SZP0; -.
DR SMR; Q3SZP0; -.
DR STRING; 9913.ENSBTAP00000041732; -.
DR PaxDb; Q3SZP0; -.
DR PRIDE; Q3SZP0; -.
DR GeneID; 789216; -.
DR KEGG; bta:789216; -.
DR CTD; 3659; -.
DR eggNOG; ENOG502QVVN; Eukaryota.
DR HOGENOM; CLU_056386_1_0_1; -.
DR InParanoid; Q3SZP0; -.
DR OrthoDB; 734108at2759; -.
DR TreeFam; TF328512; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
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:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR031215; IRF1.
DR InterPro; IPR017431; IRF1/IRF2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949:SF3; PTHR11949:SF3; 1.
DR Pfam; PF00605; IRF; 1.
DR PIRSF; PIRSF038196; IFN_RF1/2; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Antiviral defense; Cytoplasm; DNA-binding;
KW Immunity; Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..322
FT /note="Interferon regulatory factor 1"
FT /id="PRO_0000223674"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 92..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10914"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 302
FT /note="L -> W (in Ref. 1; AAO46998)"
FT /evidence="ECO:0000305"
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
