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Database: UniProt
Entry: P23611
LinkDB: P23611
Original site: P23611 
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   30-AUG-2017, entry version 152.
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; Myomorpha;
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; DOI=10.4049/jimmunol.179.1.26;
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   IDENTIFICATION BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
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: Plays a role as a transcriptional activator or repressor
CC       (By similarity). Specifically binds to the upstream regulatory
CC       region of type I IFN and IFN-inducible MHC class I genes (the
CC       interferon consensus sequence (ICS)). Plays a negative regulatory
CC       role in cells of the immune system. Involved in CD8(+) dendritic
CC       cell differentiation by forming a complex with the BATF-JUNB
CC       heterodimer in immune cells, leading to recognition of AICE
CC       sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory
CC       element, followed by cooperative binding of BATF and IRF8 and
CC       activation of genes (PubMed:22992524).
CC       {ECO:0000250|UniProtKB:Q02556, ECO:0000269|PubMed:22992524}.
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. {ECO:0000250, ECO:0000269|PubMed:17579016,
CC       ECO:0000269|PubMed:22992524}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17579016}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q02556}. Note=In resting
CC       macrophages, localizes in the cytoplasm. Translocated in the
CC       nucleus upon IFN-gamma induction. {ECO:0000250|UniProtKB:Q02556}.
CC   -!- TISSUE SPECIFICITY: Predominantly in lymphoid tissues.
CC   -!- INDUCTION: By interferon gamma. {ECO:0000269|PubMed:17579016}.
CC   -!- PTM: Ubiquitinated (PubMed:17579016). Ubiquitination by TRIM21 in
CC       macrophages, a process that is strongly increased upon interferon
CC       gamma stimulation, leds to the enhanced transcriptional activity
CC       of target cytokine genes (PubMed:17579016). Ubiquitination leads
CC       to its degradation by the proteasome (By similarity).
CC       {ECO:0000250|UniProtKB:Q02556, ECO:0000269|PubMed:17579016}.
CC   -!- PTM: Sumoylated with SUMO3. Desumoylated by SENP1.
CC       {ECO:0000250|UniProtKB:Q02556}.
CC   -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00840}.
DR   EMBL; M32489; AAA37878.1; -; mRNA.
DR   EMBL; AK018533; BAB31258.1; -; mRNA.
DR   EMBL; BC005450; AAH05450.1; -; mRNA.
DR   CCDS; CCDS22721.1; -.
DR   PIR; A35861; A35861.
DR   RefSeq; NP_001288740.1; NM_001301811.1.
DR   RefSeq; NP_032346.1; NM_008320.4.
DR   UniGene; Mm.334861; -.
DR   ProteinModelPortal; P23611; -.
DR   SMR; P23611; -.
DR   BioGrid; 200504; 6.
DR   IntAct; P23611; 1.
DR   STRING; 10090.ENSMUSP00000040245; -.
DR   iPTMnet; P23611; -.
DR   PhosphoSitePlus; P23611; -.
DR   EPD; P23611; -.
DR   PaxDb; P23611; -.
DR   PeptideAtlas; P23611; -.
DR   PRIDE; P23611; -.
DR   Ensembl; ENSMUST00000047737; ENSMUSP00000040245; ENSMUSG00000041515.
DR   Ensembl; ENSMUST00000162001; ENSMUSP00000125029; ENSMUSG00000041515.
DR   GeneID; 15900; -.
DR   KEGG; mmu:15900; -.
DR   UCSC; uc009nrk.2; mouse.
DR   CTD; 3394; -.
DR   MGI; MGI:96395; Irf8.
DR   eggNOG; ENOG410IED8; Eukaryota.
DR   eggNOG; ENOG410XNYR; LUCA.
DR   GeneTree; ENSGT00760000119093; -.
DR   HOGENOM; HOG000010107; -.
DR   HOVERGEN; HBG003072; -.
DR   InParanoid; P23611; -.
DR   KO; K10155; -.
DR   OMA; CPEGCRL; -.
DR   OrthoDB; EOG091G067P; -.
DR   PhylomeDB; P23611; -.
DR   TreeFam; TF328512; -.
DR   PRO; PR:P23611; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000041515; -.
DR   CleanEx; MM_IRF8; -.
DR   ExpressionAtlas; P23611; baseline and differential.
DR   Genevisible; P23611; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:MGI.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; ISS:UniProtKB.
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:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI: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:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IPI:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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_dom-like.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   PANTHER; PTHR11949; PTHR11949; 1.
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   Activator; Complete proteome; Cytoplasm; DNA-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    424       Interferon regulatory factor 8.
FT                                /FTId=PRO_0000154565.
FT   DNA_BIND      7    114       IRF tryptophan pentad repeat.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00840}.
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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