IRF2_SIGHI
ID IRF2_SIGHI Reviewed; 349 AA.
AC Q8R4E0;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Interferon regulatory factor 2;
DE Short=IRF-2;
GN Name=IRF2;
OS Sigmodon hispidus (Hispid cotton rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Sigmodontinae; Sigmodon.
OX NCBI_TaxID=42415;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Blanco J.C., Pletneva L.M., Prince G.A.;
RT "Cotton rat cytokines, chemokines, and interferons.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically binds to the upstream regulatory region of type
CC I IFN and IFN-inducible MHC class I genes (the interferon consensus
CC sequence (ICS)) and represses those genes. Also acts as an activator
CC for several genes including H4 and IL7. Constitutively binds to the
CC ISRE promoter to activate IL7. Involved in cell cycle regulation
CC through binding the site II (HiNF-M) promoter region of H4 and
CC activating transcription during cell growth. Antagonizes IRF1
CC transcriptional activation.
CC -!- SUBUNIT: Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with
CC CREBBP in growing cells; the interaction acetylates IRF2 and regulates
CC IRF2-dependent H4 promoter activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75
CC is required for stimulation of H4 promoter activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: The major sites of sumoylation are Lys-137 and Lys-293.
CC Sumoylation with SUMO1 increases its transcriptional repressor activity
CC on IRF1 and diminishes its ability to activate ISRE and H4 promoter (By
CC similarity). {ECO:0000250}.
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; AF480857; AAL87198.1; -; mRNA.
DR AlphaFoldDB; Q8R4E0; -.
DR BMRB; Q8R4E0; -.
DR SMR; Q8R4E0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR017431; IRF1/IRF2.
DR InterPro; IPR031218; IRF2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949:SF22; PTHR11949:SF22; 1.
DR Pfam; PF00605; IRF; 1.
DR PIRSF; PIRSF038196; IFN_RF1/2; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..349
FT /note="Interferon regulatory factor 2"
FT /id="PRO_0000154551"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 228..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14316"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 39471 MW; 83E844FCCD25BDE3 CRC64;
MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK DAPLFRNWAI
HTGKHQPGID KPDPKTWKAN FRCAMNSLPD IEEVKDRSIK KGNNAFRVYR MLPLSERPSK
KGKKPKTEKE ERVKHIKQEP VESSLGLSNG VSDLSPEYAV LASTIKTEVD STVNIIVVGQ
SHLDSNIEDQ EIVTNPPDIC QVVEVTTESD DQPVSMSELY PLQISPVSSY AESETTDSVP
SDEEGAEGRP HWRKRNFEGK QFLSNMGTRS TYLLPSMATF VTSNKPDLQV TIKEESCPMP
YNSSWPPFTD LSLPAPVTPT PSSSRPDRET RASVIKKTSD ITQSRVKSC
