Database: UniProt
Entry: A0FIN4
LinkDB: A0FIN4
Original site: A0FIN4 
ID   IRF1_PIG                Reviewed;         322 AA.
AC   A0FIN4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   12-APR-2017, entry version 70.
DE   RecName: Full=Interferon regulatory factor 1;
DE            Short=IRF-1;
GN   Name=IRF1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RA   Liu Y., Zhang Q.;
RT   "Molecular cloning of interferon regulatory factor 1 (IRF1).";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional regulator which displays a remarkable
CC       functional diversity in the regulation of cellular responses.
CC       These include the regulation of IFN and IFN-inducible genes, host
CC       response to viral and bacterial infections, regulation of many
CC       genes expressed during hematopoiesis, inflammation, immune
CC       responses and cell proliferation and differentiation, regulation
CC       of the cell cycle and induction of growth arrest and programmed
CC       cell death following DNA damage. Stimulates both innate and
CC       acquired immune responses through the activation of specific
CC       target genes and can act as a transcriptional activator and
CC       repressor regulating target genes by binding to an interferon-
CC       stimulated response element (ISRE) in their promoters. Its target
CC       genes for transcriptional activation activity include: genes
CC       involved in anti-viral response, such as IFN-alpha/beta,
CC       RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-
CC       proliferative response, such as p53/TP53, LOX and CDKN1A;
CC       apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune
CC       response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA
CC       damage responses and DNA repair, such as POLQ/POLH; MHC class I
CC       expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and
CC       B2M and MHC class II expression, such as CIITA. Represses genes
CC       involved in anti-proliferative response, such as BIRC5/survivin,
CC       CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as
CC       FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent
CC       transcription through enhanced recruitment of EP300 leading to
CC       increased acetylation of p53/TP53. Plays an important role in
CC       immune response directly affecting NK maturation and activity,
CC       macrophage production of IL12, Th1 development and maturation of
CC       CD8+ T-cells. Also implicated in the differentiation and
CC       maturation of dendritic cells and in the suppression of regulatory
CC       T (Treg) cells development. Acts as a tumor suppressor and plays a
CC       role not only in antagonism of tumor cell growth but also in
CC       stimulating an immune response against tumor cells (By
CC       similarity). {ECO:0000250}.
CC   -!- ENZYME REGULATION: Activated by MYD88. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with EP300, PIAS3 and MYD88
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=MYD88-associated IRF1 migrates into the
CC       nucleus more efficiently than non-MYD88-associated IRF1.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CK2 and this positively regulates its
CC       activity. {ECO:0000250}.
CC   -!- PTM: Sumoylation represses the transcriptional activity and
CC       displays enhanced resistance to protein degradation. Inactivates
CC       the tumor suppressor activity. Elevated levels in tumor cells.
CC       Major site is Lys-276. Sumoylation is enhanced by PIAS3.
CC       Desumoylated by SENP1 in tumor cells and appears to compete with
CC       ubiquitination on C-terminal sites (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-
CC       terminal sites (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00840}.
DR   EMBL; EF011020; ABJ98327.1; -; mRNA.
DR   RefSeq; NP_001090882.1; NM_001097413.1.
DR   UniGene; Ssc.19494; -.
DR   ProteinModelPortal; A0FIN4; -.
DR   STRING; 9823.ENSSSCP00000015188; -.
DR   PaxDb; A0FIN4; -.
DR   PRIDE; A0FIN4; -.
DR   Ensembl; ENSSSCT00000015600; ENSSSCP00000015188; ENSSSCG00000014277.
DR   GeneID; 396611; -.
DR   KEGG; ssc:396611; -.
DR   CTD; 3659; -.
DR   eggNOG; ENOG410IER3; Eukaryota.
DR   eggNOG; ENOG4111HM7; LUCA.
DR   GeneTree; ENSGT00760000119093; -.
DR   HOGENOM; HOG000037937; -.
DR   HOVERGEN; HBG003455; -.
DR   InParanoid; A0FIN4; -.
DR   KO; K09444; -.
DR   OrthoDB; EOG091G0CB8; -.
DR   TreeFam; TF328512; -.
DR   Reactome; R-SSC-933541; TRAF6 mediated IRF7 activation.
DR   Reactome; R-SSC-983231; Factors involved in megakaryocyte development and platelet production.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Bgee; ENSSSCG00000014277; -.
DR   ExpressionAtlas; A0FIN4; differential.
DR   Genevisible; A0FIN4; SS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:InterPro.
DR   GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR   GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR   GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR   Gene3D;; -; 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; IPR011991; WHTH_DNA-bd_dom.
DR   PANTHER; PTHR11949; PTHR11949; 1.
DR   PANTHER; PTHR11949:SF37; PTHR11949:SF37; 1.
DR   Pfam; PF00605; IRF; 1.
DR   PIRSF; PIRSF038196; IFN_RF1/2; 1.
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; Antiviral defense; Complete proteome;
KW   Cytoplasm; DNA-binding; Immunity; Innate immunity; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Tumor suppressor; Ubl conjugation.
FT   CHAIN         1    322       Interferon regulatory factor 1.
FT                                /FTId=PRO_0000273191.
FT   DNA_BIND      5    113       IRF tryptophan pentad repeat.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00840}.
FT   MOD_RES      78     78       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P10914}.
FT   CROSSLNK    276    276       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    296    296       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
SQ   SEQUENCE   322 AA;  35999 MW;  47AAE7198EED3B07 CRC64;
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