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   24-JAN-2024, entry version 185.
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; 10090-ENSMUSP00000034041; -.
DR   PeptideAtlas; P23906; -.
DR   ProteomicsDB; 267006; -.
DR   Pumba; P23906; -.
DR   Antibodypedia; 17374; 614 antibodies from 45 providers.
DR   DNASU; 16363; -.
DR   Ensembl; ENSMUST00000034041.9; ENSMUSP00000034041.8; ENSMUSG00000031627.10.
DR   GeneID; 16363; -.
DR   KEGG; mmu:16363; -.
DR   UCSC; uc009lqo.2; mouse.
DR   AGR; MGI:96591; -.
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; SSWPPFA; -.
DR   OrthoDB; 3740806at2759; -.
DR   PhylomeDB; P23906; -.
DR   TreeFam; TF328512; -.
DR   BioGRID-ORCS; 16363; 12 hits in 81 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 207 other cell types or tissues.
DR   ExpressionAtlas; P23906; baseline and differential.
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; IMP: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: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:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
DR   CDD; cd00103; IRF; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR019817; Interferon_reg_fac_CS.
DR   InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR   InterPro; IPR017431; IRF1/IRF2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11949; INTERFERON REGULATORY FACTOR; 1.
DR   PANTHER; PTHR11949:SF22; INTERFERON REGULATORY FACTOR 2; 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; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00601; IRF_1; 1.
DR   PROSITE; PS51507; IRF_2; 1.
DR   Genevisible; P23906; MM.
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
//