IRF1_CHICK
ID IRF1_CHICK Reviewed; 313 AA.
AC Q90876; Q5W4T4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Interferon regulatory factor 1;
DE Short=IRF-1;
GN Name=IRF1;
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].
RX PubMed=7536924; DOI=10.1073/pnas.92.8.3105;
RA Jungwirth C., Rebbert M., Ozato K., Degen H.J., Schultz U., Dawid I.B.;
RT "Chicken interferon consensus sequence-binding protein (ICSBP) and
RT interferon regulatory factor (IRF) 1 genes reveal evolutionary conservation
RT in the IRF gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3105-3109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15626157; DOI=10.1089/jir.2004.24.600;
RA Avery S., Rothwell L., Degen W.D.J., Schijns V.E.J.C., Young J.,
RA Kaufman J., Kaiser P.;
RT "Characterization of the first nonmammalian T2 cytokine gene cluster: the
RT cluster contains functional single-copy genes for IL-3, IL-4, IL-13, and
RT GM-CSF, a gene for IL-5 that appears to be a pseudogene, and a gene
RT encoding another cytokinelike transcript, KK34.";
RL J. Interferon Cytokine Res. 24:600-610(2004).
CC -!- FUNCTION: Transcriptional regulator that specifically binds to the
CC upstream regulatory region of type I IFN and IFN-inducible MHC class I
CC genes (the interferon consensus sequence (ICS)) and activates those
CC genes (By similarity). Acts as a tumor suppressor (By similarity).
CC {ECO:0000250|UniProtKB:P10914}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15314}. Cytoplasm
CC {ECO:0000250|UniProtKB:P15314}.
CC -!- PTM: Phosphorylated by CK2 and this positively regulates its activity.
CC {ECO:0000250|UniProtKB:P10914}.
CC -!- PTM: Sumoylation represses the transcriptional activity and displays
CC enhanced resistance to protein degradation. Inactivates the tumor
CC suppressor activity. Elevated levels in tumor cells. Major site is Lys-
CC 271. Sumoylation is enhanced by PIAS3. Desumoylated by SENP1 in tumor
CC cells and appears to compete with ubiquitination on C-terminal sites
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-terminal
CC sites (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; L39766; AAA62160.1; -; mRNA.
DR EMBL; AJ621385; CAF18545.1; -; Genomic_DNA.
DR RefSeq; NP_990746.1; NM_205415.1.
DR AlphaFoldDB; Q90876; -.
DR SMR; Q90876; -.
DR STRING; 9031.ENSGALP00000002242; -.
DR PaxDb; Q90876; -.
DR Ensembl; ENSGALT00000002244; ENSGALP00000002242; ENSGALG00000006785.
DR GeneID; 396384; -.
DR KEGG; gga:396384; -.
DR CTD; 3659; -.
DR VEuPathDB; HostDB:geneid_396384; -.
DR eggNOG; ENOG502QVVN; Eukaryota.
DR GeneTree; ENSGT00940000156288; -.
DR HOGENOM; CLU_056386_1_0_1; -.
DR InParanoid; Q90876; -.
DR OrthoDB; 734108at2759; -.
DR PhylomeDB; Q90876; -.
DR PRO; PR:Q90876; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000006785; Expressed in granulocyte and 12 other tissues.
DR ExpressionAtlas; Q90876; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
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; IPR031215; IRF1.
DR InterPro; IPR017431; IRF1/IRF2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949:SF3; PTHR11949:SF3; 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 Activator; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..313
FT /note="Interferon regulatory factor 1"
FT /id="PRO_0000154548"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 110..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 36010 MW; 0895FA3736FA7463 CRC64;
MPVSRMRMRP WLEMQINSNQ IPGLIWINKD KMIFQIPWKH AAKHGWDMEK DACLFRSWAI
HTGRYKVGEK DPDPKTWKAN FRCAMNSLPD IEEVKDKSIN KGSSAVRVYR MLPPLTKDQK
KERKSKSSRE ARNKSKRKLY EDMRMEESAE RLTSTPLPDD HSSYTAHDYT GQEVEVENTS
ITLDLSSCEV SGSLTDWRMP MEIAMADSTN DIYQLQVSPL GSSSEDEDEM KSNIIKLLEP
TQDWHTTSVE GKGFFTNEPG TQTMCSTFGY KEQDGEIDTS SAELEFRMMD QKSSLDFSWL
DTVRPMQAIS CSL
