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 01-MAY-2013, entry version 92.
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 -!- SUBUNIT: Homodimer, when phosphorylated (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for
CC activation.
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 (By similarity).
CC -!- SIMILARITY: Belongs to the IRF family.
CC -!- SIMILARITY: Contains 1 IRF tryptophan pentad repeat DNA-binding
CC domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF028725; AAB81997.1; -; mRNA.
DR IPI; IPI00113787; -.
DR RefSeq; NP_001239311.1; NM_001252382.1.
DR RefSeq; NP_036187.1; NM_012057.4.
DR UniGene; Mm.6479; -.
DR ProteinModelPortal; P56477; -.
DR SMR; P56477; 19-119, 231-466.
DR IntAct; P56477; 1.
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 CTD; 3663; -.
DR MGI; MGI:1350924; Irf5.
DR eggNOG; NOG45024; -.
DR HOGENOM; HOG000037433; -.
DR HOVERGEN; HBG105715; -.
DR InParanoid; P56477; -.
DR KO; K09446; -.
DR OMA; EDVKWPP; -.
DR OrthoDB; EOG41C6W2; -.
DR NextBio; 305003; -.
DR ArrayExpress; P56477; -.
DR Bgee; P56477; -.
DR CleanEx; MM_IRF5; -.
DR Genevestigator; P56477; -.
DR GermOnline; ENSMUSG00000029771; Mus musculus.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 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 MOTIF 12 18 Nuclear localization signal (By
FT similarity).
FT MOTIF 149 159 Nuclear export signal (By similarity).
FT COMPBIAS 9 12 Poly-Pro.
FT COMPBIAS 140 148 Poly-Glu.
FT MOD_RES 157 157 Phosphoserine; by TBK1 (By similarity).
FT MOD_RES 300 300 Phosphoserine (By similarity).
FT MOD_RES 434 434 Phosphoserine (By similarity).
FT MOD_RES 436 436 Phosphoserine (By similarity).
FT MOD_RES 439 439 Phosphoserine (By similarity).
FT MOD_RES 445 445 Phosphoserine (By similarity).
FT CROSSLNK 410 410 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 411 411 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
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
//
