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Database: UniProt
Entry: P56477
LinkDB: P56477
Original site: P56477 
ID   IRF5_MOUSE              Reviewed;         497 AA.
AC   P56477;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   29-OCT-2014, entry version 106.
DE   RecName: Full=Interferon regulatory factor 5;
DE            Short=IRF-5;
GN   Name=Irf5;
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].
RC   STRAIN=C57BL/6J; TISSUE=Lymph node;
RA   Grossman A., Kondo S., Antonio L., Mak T.W.;
RT   "Generation of mutant mice deficient in IRF5.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   UBIQUITINATION AT LYS-410 AND LYS-411 BY TRAF6, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18824541; DOI=10.1128/MCB.00662-08;
RA   Balkhi M.Y., Fitzgerald K.A., Pitha P.M.;
RT   "Functional regulation of MyD88-activated interferon regulatory factor
RT   5 by K63-linked polyubiquitination.";
RL   Mol. Cell. Biol. 28:7296-7308(2008).
CC   -!- FUNCTION: Transcription factor involved in the induction of
CC       interferons IFNA and INFB and inflammatory cytokines upon virus
CC       infection. Activated by TLR7 or TLR8 signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer, when phosphorylated. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18824541}.
CC       Nucleus {ECO:0000269|PubMed:18824541}. Note=Shuttles between the
CC       nucleus and the cytoplasm.
CC   -!- PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for
CC       activation. {ECO:0000269|PubMed:18824541}.
CC   -!- PTM: Phosphorylation of serine and threonine residues in a C-
CC       terminal autoinhibitory region, stimulates dimerization, transport
CC       into the nucleus, assembly with the coactivator CBP/p300 and
CC       initiation of transcription. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00840}.
CC   -!- SIMILARITY: Contains 1 IRF tryptophan pentad repeat DNA-binding
CC       domain. {ECO:0000255|PROSITE-ProRule:PRU00840}.
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DR   EMBL; AF028725; AAB81997.1; -; mRNA.
DR   CCDS; CCDS19962.1; -.
DR   RefSeq; NP_001239311.1; NM_001252382.1.
DR   RefSeq; NP_036187.1; NM_012057.4.
DR   RefSeq; XP_006505160.1; XM_006505097.1.
DR   UniGene; Mm.6479; -.
DR   ProteinModelPortal; P56477; -.
DR   SMR; P56477; 19-119, 231-466.
DR   BioGrid; 205111; 4.
DR   IntAct; P56477; 1.
DR   MINT; MINT-1565953; -.
DR   STRING; 10090.ENSMUSP00000004392; -.
DR   PhosphoSite; P56477; -.
DR   PaxDb; P56477; -.
DR   PRIDE; P56477; -.
DR   DNASU; 27056; -.
DR   Ensembl; ENSMUST00000004392; ENSMUSP00000004392; ENSMUSG00000029771.
DR   Ensembl; ENSMUST00000163511; ENSMUSP00000127021; ENSMUSG00000029771.
DR   GeneID; 27056; -.
DR   KEGG; mmu:27056; -.
DR   UCSC; uc009bdu.2; mouse.
DR   CTD; 3663; -.
DR   MGI; MGI:1350924; Irf5.
DR   eggNOG; NOG45024; -.
DR   HOGENOM; HOG000037433; -.
DR   HOVERGEN; HBG105715; -.
DR   InParanoid; P56477; -.
DR   KO; K09446; -.
DR   OMA; YDGPRDM; -.
DR   OrthoDB; EOG7CCBR1; -.
DR   PhylomeDB; P56477; -.
DR   TreeFam; TF328512; -.
DR   Reactome; REACT_198660; Interferon gamma signaling.
DR   NextBio; 305003; -.
DR   PRO; PR:P56477; -.
DR   Bgee; P56477; -.
DR   CleanEx; MM_IRF5; -.
DR   ExpressionAtlas; P56477; baseline and differential.
DR   Genevestigator; P56477; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0000975; F:regulatory region DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR   GO; GO:0032494; P:response to peptidoglycan; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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; SSF49879; 1.
DR   PROSITE; PS00601; IRF_1; 1.
DR   PROSITE; PS51507; IRF_2; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Complete proteome; Cytoplasm; DNA-binding;
KW   Immunity; Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1    497       Interferon regulatory factor 5.
FT                                /FTId=PRO_0000154559.
FT   DNA_BIND     14    122       IRF tryptophan pentad repeat.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00840}.
FT   MOTIF        12     18       Nuclear localization signal.
FT                                {ECO:0000250}.
FT   MOTIF       149    159       Nuclear export signal. {ECO:0000250}.
FT   COMPBIAS      9     12       Poly-Pro.
FT   COMPBIAS    140    148       Poly-Glu.
FT   MOD_RES     157    157       Phosphoserine; by TBK1. {ECO:0000250}.
FT   MOD_RES     300    300       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     434    434       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     436    436       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     439    439       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     445    445       Phosphoserine. {ECO:0000250}.
FT   CROSSLNK    410    410       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:18824541}.
FT   CROSSLNK    411    411       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:18824541}.
SQ   SEQUENCE   497 AA;  56005 MW;  D8BD54DB946E354F CRC64;
     MNHSAPGIPP PPRRVRLKPW LVAQVNSCQY PGLQWVNGEK KLFYIPWRHA TRHGPSQDGD
     NTIFKAWAKE TGKYTEGVDE ADPAKWKANL RCALNKSRDF QLFYDGPRDM PPQPYKIYEV
     CSNGPAPTES QPTDDYVLGE EEEEEEEELQ RMLPGLSITE PALPGPPNAP YSLPKEDTKW
     PPALQPPVGL GPPVPDPNLL APPSGNPAGF RQLLPEVLEP GPLASSQPPT EPLLPDLLIS
     PHMLPLTDLE IKFQYRGRAP RTLTISNPQG CRLFYSQLEA TQEQVELFGP VTLEQVRFPS
     PEDIPSDKQR FYTNQLLDVL DRGLILQLQG QDLYAIRLCQ CKVFWSGPCA LAHGSCPNPI
     QREVKTKLFS LEQFLNELIL FQKGQTNTPP PFEIFFCFGE EWPDVKPREK KLITVQVVPV
     AARLLLEMFS GELSWSADSI RLQISNPDLK DHMVEQFKEL HHLWQSQQQL QPMVQAPPVA
     GLDASQGPWP MHPVGMQ
//
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