IRF2_CHICK
ID IRF2_CHICK Reviewed; 348 AA.
AC Q98925;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Interferon regulatory factor 2;
DE Short=IRF-2;
GN Name=IRF2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9142651; DOI=10.1089/jir.1997.17.219;
RA Marienfeld R., Nanda I., Zoeller B., Schmid M., Rebbert M., Jungwirth C.;
RT "Cloning of chicken interferon regulatory factor-2 (IRF-2) cDNA: expression
RT and mapping of the IRF-2 gene.";
RL J. Interferon Cytokine Res. 17:219-227(1997).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CREBBP in growing cells; the interaction
CC acetylates IRF2 and regulates IRF2-dependent H4 promoter activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; X95478; CAA64748.1; -; mRNA.
DR RefSeq; NP_990527.1; NM_205196.1.
DR RefSeq; XP_015131640.1; XM_015276154.1.
DR RefSeq; XP_015131641.1; XM_015276155.1.
DR RefSeq; XP_015131642.1; XM_015276156.1.
DR RefSeq; XP_015131643.1; XM_015276157.1.
DR RefSeq; XP_015131644.1; XM_015276158.1.
DR AlphaFoldDB; Q98925; -.
DR SMR; Q98925; -.
DR STRING; 9031.ENSGALP00000037458; -.
DR PaxDb; Q98925; -.
DR Ensembl; ENSGALT00000038252; ENSGALP00000037458; ENSGALG00000010642.
DR GeneID; 396115; -.
DR KEGG; gga:396115; -.
DR CTD; 3660; -.
DR VEuPathDB; HostDB:geneid_396115; -.
DR eggNOG; ENOG502QW7C; Eukaryota.
DR GeneTree; ENSGT00940000159063; -.
DR HOGENOM; CLU_056386_0_0_1; -.
DR InParanoid; Q98925; -.
DR OrthoDB; 734108at2759; -.
DR PhylomeDB; Q98925; -.
DR PRO; PR:Q98925; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000010642; Expressed in lung and 13 other tissues.
DR ExpressionAtlas; Q98925; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..348
FT /note="Interferon regulatory factor 2"
FT /id="PRO_0000154552"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 348 AA; 39351 MW; C070E381AAD4CD77 CRC64;
MPVERMRMRP WLEEQINSNT IPGLKWINKE KKIFQIPWMH AARHGWDVEK DAPLFRNWAI
HTGKYQSGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIK KGNNAFRVYR MLPLSERPSK
KGKKTKSEKD DKFKQIKQEP VESSFGINGL NDVTSDYFLS SSIKNEVDST VNIVVVGQPH
LDGSSEEQVI VANPPDVCQV VEVTTESDEQ PLSMSQLYPL QISPVSSYAE SETTDSVPSD
EENAEGRLHW QKKNIEGKQY LSNLGMRNTS HMLPSMATFV ANKPDLQVTI KEESCPLPYN
SSWPPFPDIP LPQVVSTAST SSSRPDRETR ASVIKKTSDI TQSRVKSC
