IRF5_BOVIN
ID IRF5_BOVIN Reviewed; 499 AA.
AC Q58DJ0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Interferon regulatory factor 5 {ECO:0000250|UniProtKB:Q13568};
DE Short=IRF-5 {ECO:0000250|UniProtKB:Q13568};
GN Name=IRF5 {ECO:0000250|UniProtKB:Q13568};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Transcription factor that plays a critical role in innate
CC immunity by activating expression of type I interferon (IFN) IFNA and
CC INFB and inflammatory cytokines downstream of endolysosomal toll-like
CC receptors TLR7, TLR8 and TLR9. Regulates the transcription of type I
CC IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by
CC binding to an interferon-stimulated response element (ISRE) in their
CC promoters. Can efficiently activate both the IFN-beta (IFNB) and the
CC IFN-alpha (IFNA) genes and mediate their induction downstream of the
CC TLR-activated, MyD88-dependent pathway. {ECO:0000250|UniProtKB:P56477}.
CC -!- ACTIVITY REGULATION: Maintained as a monomer in an autoinhibited state
CC (By similarity). Phosphorylation and activation follow the following
CC steps: innate adapter protein TASL recruits IRF5, thereby licensing
CC IRF5 for phosphorylation by IKBKB (By similarity). Phosphorylated IRF5
CC dissociates from the adapter proteins, dimerizes, and then enters the
CC nucleus to induce IFNs (By similarity). {ECO:0000250|UniProtKB:P56477,
CC ECO:0000250|UniProtKB:Q13568}.
CC -!- SUBUNIT: Homodimer, when phosphorylated (By similarity). Interacts with
CC TASL (via pLxIS motif); interaction takes place downstream of TLR7,
CC TLR8 or TLR9, leading to its activation (By similarity). Interacts with
CC MYD88 and TRAF6 (By similarity). {ECO:0000250|UniProtKB:P56477,
CC ECO:0000250|UniProtKB:Q13568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P56477}. Nucleus
CC {ECO:0000250|UniProtKB:P56477}. Note=Shuttles between the nucleus and
CC the cytoplasm: upon activation by the TLR adapter MYD88 and subsequent
CC phosphorylation, translocates to the nucleus.
CC {ECO:0000250|UniProtKB:P56477}.
CC -!- PTM: Phosphorylation of serine and threonine residues by IKBKB in a C-
CC terminal autoinhibitory region, stimulates dimerization, transport into
CC the nucleus, assembly with the coactivator CBP/EP300 and initiation of
CC transcription. {ECO:0000250|UniProtKB:Q13568}.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for
CC activation. {ECO:0000250|UniProtKB:P56477}.
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; BT021607; AAX46454.1; -; mRNA.
DR RefSeq; NP_001030542.1; NM_001035465.1.
DR AlphaFoldDB; Q58DJ0; -.
DR SMR; Q58DJ0; -.
DR STRING; 9913.ENSBTAP00000006567; -.
DR PaxDb; Q58DJ0; -.
DR PRIDE; Q58DJ0; -.
DR GeneID; 615340; -.
DR KEGG; bta:615340; -.
DR CTD; 3663; -.
DR eggNOG; ENOG502QSKM; Eukaryota.
DR InParanoid; Q58DJ0; -.
DR OrthoDB; 648909at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
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; IPR029838; IRF5.
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 PANTHER; PTHR11949:SF10; PTHR11949:SF10; 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 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; DNA-binding; Immunity; Inflammatory response;
KW Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..499
FT /note="Interferon regulatory factor 5"
FT /id="PRO_0000271387"
FT DNA_BIND 14..122
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOTIF 145..155
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 153
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 294
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56477"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13568"
SQ SEQUENCE 499 AA; 55931 MW; 8978C8CEC005BF12 CRC64;
MNQPAPAALL PPRRVRLKPW LVAQVNSCQY PGLQWVNGEK KLFYIPWRHA TRHGPSHDGD
NTIFKAWAKE TGKYTEGVDE ADPAKWKANL RCALNKSRDF RLIYDGPRDM PPQPYKVYEV
CSNGPAPAES QPSEDNAEEE EEEELQKMLP GLSITEAVQP GPAMAPYSLP KEDVKWPPTL
QPPVVLAPPA PGPNLLVPAP GNAADFGEVF SEVLPSSQPQ PGSLSTSLAP TGEQLLPDLL
ISPHMLPLTD LEIKFQYRGR PPRALTISNP QSCRLLYSQL EATQEQVELF GPVSLEQVRF
PSPEDIPSEK QRFYTNQLLD VLDRGLILQI QGQDLYAIRL CQCKVFWSGP CASAQGSHPN
PIQREVKTKL FSLEDFLNEL ILFQKGQTNT PPPFEIFFCF GEEWPDCKPR EKKLITVQVV
PVAARMLLEM FSGELSWSAD SIRLQISNPD LKDRMVEQFK ELHHIWLSQQ HLQPVAQTPA
MPGLSAAQGP WPMHPVGMQ
