IRF2_MOUSE
ID IRF2_MOUSE Reviewed; 349 AA.
AC P23906;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Interferon regulatory factor 2;
DE Short=IRF-2;
GN Name=Irf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2475256; DOI=10.1016/0092-8674(89)90107-4;
RA Harada H., Fujita T., Miyamoto M., Kimura Y., Maruyama M., Furia A.,
RA Miyata T., Taniguchi T.;
RT "Structurally similar but functionally distinct factors, IRF-1 and IRF-2,
RT bind to the same regulatory elements of IFN and IFN-inducible genes.";
RL Cell 58:729-739(1989).
RN [2]
RP PROTEIN SEQUENCE OF 108-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP STRUCTURE BY NMR OF 2-113.
RX PubMed=9562558; DOI=10.1016/s0969-2126(98)00050-1;
RA Furui J., Uegaki K., Yamazaki T., Shirakawa M., Swindells M.B., Harada H.,
RA Taniguchi T., Kyogoku Y.;
RT "Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of
RT the winged helix-turn-helix family.";
RL Structure 6:491-500(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-113.
RX PubMed=10487755; DOI=10.1093/emboj/18.18.5028;
RA Fujii Y., Shimizu T., Kusumoto M., Kyogoku Y., Taniguchi T., Hakoshima T.;
RT "Crystal structure of an IRF-DNA complex reveals novel DNA recognition and
RT cooperative binding to a tandem repeat of core sequences.";
RL EMBO J. 18:5028-5041(1999).
CC -!- FUNCTION: Specifically binds to the upstream regulatory region of type
CC I IFN and IFN-inducible MHC class I genes (the interferon consensus
CC sequence (ICS)) and represses those genes. Also acts as an activator
CC for several genes including H4 and IL7. Constitutively binds to the
CC ISRE promoter to activate IL7. Involved in cell cycle regulation
CC through binding the site II (HiNF-M) promoter region of H4 and
CC activating transcription during cell growth. Antagonizes IRF1
CC transcriptional activation.
CC -!- SUBUNIT: Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with
CC CREBBP in growing cells; the interaction acetylates IRF2 and regulates
CC IRF2-dependent H4 promoter activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By viruses and IFN.
CC -!- PTM: Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75
CC is required for stimulation of H4 promoter activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: The major sites of sumoylation are Lys-137 and Lys-293.
CC Sumoylation with SUMO1 increases its transcriptional repressor activity
CC on IRF1 and diminishes its ability to activate ISRE and H4 promoter (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; J03168; AAA39333.1; -; mRNA.
DR CCDS; CCDS22295.1; -.
DR RefSeq; NP_032417.3; NM_008391.4.
DR RefSeq; XP_006509351.1; XM_006509288.3.
DR RefSeq; XP_006509352.1; XM_006509289.3.
DR PDB; 1IRF; NMR; -; A=2-113.
DR PDB; 1IRG; NMR; -; A=2-113.
DR PDB; 2IRF; X-ray; 2.20 A; G/H/I/J/K/L=1-113.
DR PDBsum; 1IRF; -.
DR PDBsum; 1IRG; -.
DR PDBsum; 2IRF; -.
DR AlphaFoldDB; P23906; -.
DR BMRB; P23906; -.
DR SMR; P23906; -.
DR BioGRID; 200785; 4.
DR STRING; 10090.ENSMUSP00000034041; -.
DR iPTMnet; P23906; -.
DR PhosphoSitePlus; P23906; -.
DR jPOST; P23906; -.
DR PaxDb; P23906; -.
DR PeptideAtlas; P23906; -.
DR PRIDE; P23906; -.
DR ProteomicsDB; 267006; -.
DR Antibodypedia; 17374; 542 antibodies from 45 providers.
DR DNASU; 16363; -.
DR Ensembl; ENSMUST00000034041; ENSMUSP00000034041; ENSMUSG00000031627.
DR GeneID; 16363; -.
DR KEGG; mmu:16363; -.
DR UCSC; uc009lqo.2; mouse.
DR CTD; 3660; -.
DR MGI; MGI:96591; Irf2.
DR VEuPathDB; HostDB:ENSMUSG00000031627; -.
DR eggNOG; ENOG502QW7C; Eukaryota.
DR GeneTree; ENSGT00940000159063; -.
DR HOGENOM; CLU_056386_0_0_1; -.
DR InParanoid; P23906; -.
DR OMA; NAEGRPH; -.
DR OrthoDB; 734108at2759; -.
DR PhylomeDB; P23906; -.
DR TreeFam; TF328512; -.
DR BioGRID-ORCS; 16363; 10 hits in 76 CRISPR screens.
DR ChiTaRS; Irf2; mouse.
DR EvolutionaryTrace; P23906; -.
DR PRO; PR:P23906; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P23906; protein.
DR Bgee; ENSMUSG00000031627; Expressed in granulocyte and 205 other tissues.
DR ExpressionAtlas; P23906; baseline and differential.
DR Genevisible; P23906; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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; IPR017431; IRF1/IRF2.
DR InterPro; IPR031218; IRF2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949:SF22; PTHR11949:SF22; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..349
FT /note="Interferon regulatory factor 2"
FT /id="PRO_0000154550"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 230..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2IRF"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2IRF"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:2IRF"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2IRF"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1IRF"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2IRF"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:2IRF"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2IRF"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2IRF"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2IRF"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2IRF"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1IRG"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:2IRF"
SQ SEQUENCE 349 AA; 39453 MW; 8738B082FB40FB11 CRC64;
MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK DAPLFRNWAI
HTGKHQPGID KPDPKTWKAN FRCAMNSLPD IEEVKDRSIK KGNNAFRVYR MLPLSERPSK
KGKKPKTEKE ERVKHIKQEP VESSLGLSNG VSGFSPEYAV LTSAIKNEVD STVNIIVVGQ
SHLDSNIEDQ EIVTNPPDIC QVVEVTTESD DQPVSMSELY PLQISPVSSY AESETTDSVA
SDEENAEGRP HWRKRSIEGK QYLSNMGTRN TYLLPSMATF VTSNKPDLQV TIKEDSCPMP
YNSSWPPFTD LPLPAPVTPT PSSSRPDRET RASVIKKTSD ITQARVKSC
