ID IRF8_MOUSE Reviewed; 424 AA.
AC P23611;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 01-MAY-2013, entry version 112.
DE RecName: Full=Interferon regulatory factor 8;
DE Short=IRF-8;
DE AltName: Full=Interferon consensus sequence-binding protein;
DE Short=ICSBP;
GN Name=Irf8; Synonyms=Icsbp, Icsbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2111015; DOI=10.1073/pnas.87.10.3743;
RA Driggers P.H., Ennist D.L., Gleason S.L., Mak W.-H., Marks M.S.,
RA Levi B.-Z., Flanagan J.R., Appella E., Ozato K.;
RT "An interferon gamma-regulated protein that binds the interferon-
RT inducible enhancer element of major histocompatibility complex class I
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3743-3747(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH TRIM21, UBIQUITINATION, INDUCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17579016;
RA Kong H.J., Anderson D.E., Lee C.H., Jang M.K., Tamura T., Tailor P.,
RA Cho H.K., Cheong J., Xiong H., Morse H.C. III, Ozato K.;
RT "Autoantigen Ro52 is an interferon inducible E3 ligase that
RT ubiquitinates IRF-8 and enhances cytokine expression in macrophages.";
RL J. Immunol. 179:26-30(2007).
RN [5]
RP FUNCTION, AND INTERACTION WITH BATF.
RX PubMed=22992524; DOI=10.1038/nature11531;
RA Tussiwand R., Lee W.L., Murphy T.L., Mashayekhi M., Kc W.,
RA Albring J.C., Satpathy A.T., Rotondo J.A., Edelson B.T., Kretzer N.M.,
RA Wu X., Weiss L.A., Glasmacher E., Li P., Liao W., Behnke M., Lam S.S.,
RA Aurthur C.T., Leonard W.J., Singh H., Stallings C.L., Sibley L.D.,
RA Schreiber R.D., Murphy K.M.;
RT "Compensatory dendritic cell development mediated by BATF-IRF
RT interactions.";
RL Nature 490:502-507(2012).
CC -!- FUNCTION: Specifically binds to the upstream regulatory region of
CC type I IFN and IFN-inducible MHC class I genes (the interferon
CC consensus sequence (ICS)). Plays a regulatory role in cells of the
CC immune system. Involved in CD8(+) dendritic cell differentiation
CC by forming a complex with the BATF-JUNB heterodimer in immune
CC cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-
CC 3'), an immune-specific regulatory element, followed by
CC cooperative binding of BATF and IRF8 and activation of genes.
CC -!- SUBUNIT: Interacts with COPS2 (By similarity). Interacts (via C-
CC terminus) with TRIM21 (via C-terminus). Interacts with the BATF-
CC JUNB heterodimer. Interacts with BATF (via bZIP domain); the
CC interaction is direct.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Predominantly in lymphoid tissues.
CC -!- INDUCTION: By interferon gamma.
CC -!- PTM: Ubiquitinated. Ubiquitination by TRIM21 in macrophages, a
CC process that is strongly increased upon interferon gamma
CC stimulation, leds to the enhanced transcriptional activity of
CC target cytokine genes.
CC -!- SIMILARITY: Belongs to the IRF family.
CC -!- SIMILARITY: Contains 1 IRF tryptophan pentad repeat DNA-binding
CC domain.
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DR EMBL; M32489; AAA37878.1; -; mRNA.
DR EMBL; AK018533; BAB31258.1; -; mRNA.
DR EMBL; BC005450; AAH05450.1; -; mRNA.
DR IPI; IPI00134564; -.
DR PIR; A35861; A35861.
DR RefSeq; NP_032346.1; NM_008320.3.
DR UniGene; Mm.334861; -.
DR ProteinModelPortal; P23611; -.
DR SMR; P23611; 9-115, 198-377.
DR IntAct; P23611; 1.
DR PhosphoSite; P23611; -.
DR PaxDb; P23611; -.
DR PRIDE; P23611; -.
DR Ensembl; ENSMUST00000047737; ENSMUSP00000040245; ENSMUSG00000041515.
DR Ensembl; ENSMUST00000162001; ENSMUSP00000125029; ENSMUSG00000041515.
DR GeneID; 15900; -.
DR KEGG; mmu:15900; -.
DR CTD; 3394; -.
DR MGI; MGI:96395; Irf8.
DR eggNOG; NOG42878; -.
DR HOGENOM; HOG000010107; -.
DR HOVERGEN; HBG003072; -.
DR InParanoid; P23611; -.
DR KO; K10155; -.
DR OMA; RELQQFY; -.
DR OrthoDB; EOG434W5Z; -.
DR NextBio; 288616; -.
DR ArrayExpress; P23611; -.
DR Bgee; P23611; -.
DR CleanEx; MM_IRF8; -.
DR Genevestigator; P23611; -.
DR GermOnline; ENSMUSG00000041515; Mus musculus.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000975; F:regulatory region DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
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_dom-like.
DR InterPro; IPR008984; SMAD_FHA_domain.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SUPFAM; SSF49879; SMAD_FHA; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW Activator; Complete proteome; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1 424 Interferon regulatory factor 8.
FT /FTId=PRO_0000154565.
FT DNA_BIND 7 114 IRF tryptophan pentad repeat.
SQ SEQUENCE 424 AA; 48237 MW; FBE79A76846E8EB2 CRC64;
MCDRNGGRRL RQWLIEQIDS SMYPGLIWEN DEKTMFRIPW KHAGKQDYNQ EVDASIFKAW
AVFKGKFKEG DKAEPATWKT RLRCALNKSP DFEEVTDRSQ LDISEPYKVY RIVPEEEQKC
KLGVAPAGCM SEVPEMECGR SEIEELIKEP SVDEYMGMTK RSPSPPEACR SQILPDWWVQ
QPSAGLPLVT GYAAYDTHHS AFSQMVISFY YGGKLVGQAT TTCLEGCRLS LSQPGLPKLY
GPDGLEPVCF PTADTIPSER QRQVTRKLFG HLERGVLLHS NRKGVFVKRL CQGRVFCSGN
AVVCKGRPNK LERDEVVQVF DTNQFIRELQ QFYATQSRLP DSRVVLCFGE EFPDTVPLRS
KLILVQVEQL YARQLVEEAG KSCGAGSLMP ALEEPQPDQA FRMFPDICTS HQRPFFRENQ
QITV
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