IRF9_MOUSE
ID IRF9_MOUSE Reviewed; 399 AA.
AC Q61179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Interferon regulatory factor 9;
DE Short=IRF-9;
DE AltName: Full=IFN-alpha-responsive transcription factor subunit;
DE AltName: Full=ISGF3 p48 subunit;
DE AltName: Full=Interferon-stimulated gene factor 3 gamma;
DE Short=ISGF-3 gamma;
DE AltName: Full=Transcriptional regulator ISGF3 subunit gamma;
GN Name=Irf9; Synonyms=Isgf3g;
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=8882710; DOI=10.1093/oxfordjournals.jbchem.a021227;
RA Suhara W., Yoneyama M., Yonekawa H., Takashi F.;
RT "Structure of mouse interferon stimulated gene factor 3 gamma (ISGF3
RT gamma/p48) cDNA and chromosomal localization of the gene.";
RL J. Biochem. 119:231-234(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-87.
RX PubMed=7843405; DOI=10.1016/0014-5793(94)01426-2;
RA Kawakami T., Matsumoto M., Sato M., Harada H., Taniguchi T., Kitagawa M.;
RT "Possible involvement of the transcription factor ISGF3 gamma in virus-
RT induced expression of the IFN-beta gene.";
RL FEBS Lett. 358:225-229(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION IN THE ISGF3 COMPLEX.
RX PubMed=17332413; DOI=10.1126/science.1136567;
RA Tenoever B.R., Ng S.L., Chua M.A., McWhirter S.M., Garcia-Sastre A.,
RA Maniatis T.;
RT "Multiple functions of the IKK-related kinase IKKepsilon in interferon-
RT mediated antiviral immunity.";
RL Science 315:1274-1278(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor that plays an essential role in anti-
CC viral immunity. It mediates signaling by type I IFNs (IFN-alpha and
CC IFN-beta). Following type I IFN binding to cell surface receptors, Jak
CC kinases (TYK2 and JAK1) are activated, leading to tyrosine
CC phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the
CC phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3
CC transcription factor, that enters the nucleus. ISGF3 binds to the IFN
CC stimulated response element (ISRE) to activate the transcription of
CC interferon stimulated genes, which drive the cell in an antiviral
CC state. {ECO:0000250|UniProtKB:Q00978}.
CC -!- SUBUNIT: Interacts with STAT2 in the cytoplasm. Forms the interferon-
CC stimulated gene factor 3 complex (ISGF3) with the heterodimer
CC STAT1:STAT2; upon stimulation. {ECO:0000269|PubMed:17332413}.
CC -!- INTERACTION:
CC Q61179; Q9QXJ2: Stat2; NbExp=10; IntAct=EBI-646653, EBI-646643;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By IFN-alpha and IFN-beta. Upon stimulation the regulatory
CC phosphorylated alpha and beta subunits assemble with the gamma subunit
CC and translocate from the cytoplasm to the nucleus.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U51992; AAC52494.1; -; mRNA.
DR EMBL; BC005435; AAH05435.1; -; mRNA.
DR EMBL; BC012968; AAH12968.1; -; mRNA.
DR CCDS; CCDS27119.1; -.
DR PIR; JC4592; JC4592.
DR RefSeq; NP_001152889.1; NM_001159417.1.
DR RefSeq; NP_001152890.1; NM_001159418.1.
DR RefSeq; NP_032420.1; NM_008394.3.
DR PDB; 5OEM; X-ray; 1.90 A; A=197-385.
DR PDB; 5OEN; X-ray; 2.92 A; A=206-376.
DR PDBsum; 5OEM; -.
DR PDBsum; 5OEN; -.
DR AlphaFoldDB; Q61179; -.
DR SMR; Q61179; -.
DR BioGRID; 200811; 9.
DR IntAct; Q61179; 8.
DR STRING; 10090.ENSMUSP00000120525; -.
DR iPTMnet; Q61179; -.
DR PhosphoSitePlus; Q61179; -.
DR EPD; Q61179; -.
DR jPOST; Q61179; -.
DR MaxQB; Q61179; -.
DR PaxDb; Q61179; -.
DR PRIDE; Q61179; -.
DR ProteomicsDB; 269506; -.
DR Antibodypedia; 663; 294 antibodies from 34 providers.
DR DNASU; 16391; -.
DR Ensembl; ENSMUST00000130697; ENSMUSP00000120359; ENSMUSG00000002325.
DR GeneID; 16391; -.
DR KEGG; mmu:16391; -.
DR UCSC; uc007tzl.2; mouse.
DR CTD; 10379; -.
DR MGI; MGI:107587; Irf9.
DR VEuPathDB; HostDB:ENSMUSG00000002325; -.
DR eggNOG; ENOG502RR4E; Eukaryota.
DR GeneTree; ENSGT00940000162115; -.
DR HOGENOM; CLU_031544_1_2_1; -.
DR InParanoid; Q61179; -.
DR OrthoDB; 648909at2759; -.
DR PhylomeDB; Q61179; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR BioGRID-ORCS; 16391; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Irf9; mouse.
DR PRO; PR:Q61179; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q61179; protein.
DR Bgee; ENSMUSG00000002325; Expressed in granulocyte and 247 other tissues.
DR ExpressionAtlas; Q61179; baseline and differential.
DR Genevisible; Q61179; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070721; C:ISGF3 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; 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 CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR019471; Interferon_reg_factor-3.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SMART; SM01243; IRF-3; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..399
FT /note="Interferon regulatory factor 9"
FT /id="PRO_0000154568"
FT DNA_BIND 9..116
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 118..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:5OEM"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5OEM"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5OEM"
FT STRAND 352..366
FT /evidence="ECO:0007829|PDB:5OEM"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:5OEM"
SQ SEQUENCE 399 AA; 44610 MW; 92F9481ACEB669BD CRC64;
MASGKVRCTR KLRSWIVEQV ESGHFPGVCW DDAAKTMFRI PWKHAGKQDF REDQDAAIFK
AWALFKEKHK DGDIGHPAVW KTRLRCALNK SSEFEEVPER GRMDVAEPYK VYRILPAGTL
PNQPRNQKSP CKRSISCVSP EREENMENGR TNGVVNHSDS GSNIGGGGNG SNRSDSNSNC
NSELEEGAGT TEATIREDPV FLEHQLPLNS DYSLLLTFIY GGRVVGKTQV HSLDCRLVAE
RSDSESSMEQ VEFPKPDPLE PTQHLLNQLD RGVLVASNSR GLFVQRLCPI PISWNAPEAP
PGPGPHLLPS NKCVELFKTT YFCRDLAQYF QGQGPPPKFQ ATLHFWEESP GSSHSQENLI
TVQMEQAFAR HLLEKIPEEE KAALFLLQHT EQSPSALGH
