ID IRF5_HUMAN Reviewed; 498 AA.
AC Q13568; A4D1J8; A8DUA8; A8DUA9; E7EQ16; E7EW54; Q64GA9; Q64GB1;
AC Q64GB2; Q6RCM8; Q9BQF0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 01-MAY-2013, entry version 117.
DE RecName: Full=Interferon regulatory factor 5;
DE Short=IRF-5;
GN Name=IRF5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
RX PubMed=11303025; DOI=10.1074/jbc.M101216200;
RA Barnes B.J., Moore P.A., Pitha P.M.;
RT "Virus-specific activation of a novel interferon regulatory factor,
RT IRF-5, results in the induction of distinct interferon alpha genes.";
RL J. Biol. Chem. 276:23382-23390(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
RX PubMed=15695821; DOI=10.1074/jbc.M412584200;
RA Schoenemeyer A., Barnes B.J., Mancl M.E., Latz E., Goutagny N.,
RA Pitha P.M., Fitzgerald K.A., Golenbock D.T.;
RT "The interferon regulatory factor, IRF5, is a central mediator of
RT toll-like receptor 7 signaling.";
RL J. Biol. Chem. 280:17005-17012(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), AND ALTERNATIVE
RP SPLICING.
RX PubMed=15805103; DOI=10.1074/jbc.M500543200;
RA Mancl M.E., Hu G., Sangster-Guity N., Olshalsky S.L., Hoops K.,
RA Fitzgerald-Bocarsly P., Pitha P.M., Pinder K., Barnes B.J.;
RT "Two discrete promoters regulate the alternatively spliced human
RT interferon regulatory factor-5 isoforms. Multiple isoforms with
RT distinct cell type-specific expression, localization, regulation, and
RT function.";
RL J. Biol. Chem. 280:21078-21090(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=16642019; DOI=10.1038/ng1782;
RA Graham R.R., Kozyrev S.V., Baechler E.C., Reddy M.V., Plenge R.M.,
RA Bauer J.W., Ortmann W.A., Koeuth T., Escribano M.F.,
RA Collaborative Groups T.A., Pons-Estel B., Petri M., Daly M.,
RA Gregersen P.K., Martin J., Altshuler D., Behrens T.W.,
RA Alarcon-Riquelme M.E.;
RT "A common haplotype of interferon regulatory factor 5 (IRF5) regulates
RT splicing and expression and is associated with increased risk of
RT systemic lupus erythematosus.";
RL Nat. Genet. 38:550-555(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Grossman A., Mittrucker H.W., Lantonio L., Mak T.W.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-253 (ISOFORMS 2 AND 3).
RA Kozyrev S.V., Lewen S., Linga-Reddy P.M.V., Alarcon-Riquelme M.E.;
RT "Structural indel variation in IRF5 is associated with a risk
RT haplotype and defines the precise IRF5 isoforms expressed in SLE.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=12138184; DOI=10.1128/MCB.22.16.5721-5740.2002;
RA Barnes B.J., Kellum M.J., Field A.E., Pitha P.M.;
RT "Multiple regulatory domains of IRF-5 control activation, cellular
RT localization, and induction of chemokines that mediate recruitment of
RT T lymphocytes.";
RL Mol. Cell. Biol. 22:5721-5740(2002).
RN [13]
RP INVOLVEMENT IN SUSCEPTIBILITY TO SLEB10.
RX PubMed=15657875; DOI=10.1086/428480;
RA Sigurdsson S., Nordmark G., Goering H.H.H., Lindroos K., Wiman A.-C.,
RA Sturfelt G., Joensen A., Rantapaeae-Dahlqvist S., Moeller B., Kere J.,
RA Koskenmies S., Widen E., Eloranta M.-L., Julkunen H.,
RA Kristjansdottir H., Steinsson K., Alm G., Roennblom L.,
RA Syvaenen A.-C.;
RT "Polymorphisms in the tyrosine kinase 2 and interferon regulatory
RT factor 5 genes are associated with systemic lupus erythematosus.";
RL Am. J. Hum. Genet. 76:528-537(2005).
RN [14]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=15556946; DOI=10.1074/jbc.M408452200;
RA Lin R., Yang L., Arguello M., Penafuerte C., Hiscott J.;
RT "A CRM1-dependent nuclear export pathway is involved in the regulation
RT of IRF-5 subcellular localization.";
RL J. Biol. Chem. 280:3088-3095(2005).
RN [15]
RP INVOLVEMENT IN SUSCEPTIBILITY TO RHEUMATOID ARTHRITIS.
RX PubMed=17599733; DOI=10.1002/art.22704;
RA Sigurdsson S., Padyukov L., Kurreeman F.A., Liljedahl U., Wiman A.C.,
RA Alfredsson L., Toes R., Ronnelid J., Klareskog L., Huizinga T.W.,
RA Alm G., Syvanen A.C., Ronnblom L.;
RT "Association of a haplotype in the promoter region of the interferon
RT regulatory factor 5 gene with rheumatoid arthritis.";
RL Arthritis Rheum. 56:2202-2210(2007).
RN [16]
RP INVOLVEMENT IN SUSCEPTIBILITY TO IBD14.
RX PubMed=17881657; DOI=10.1093/hmg/ddm259;
RA Dideberg V., Kristjansdottir G., Milani L., Libioulle C.,
RA Sigurdsson S., Louis E., Wiman A.-C., Vermeire S., Rutgeerts P.,
RA Belaiche J., Franchimont D., Van Gossum A., Bours V., Syvaenen A.-C.;
RT "An insertion-deletion polymorphism in the interferon regulatory
RT Factor 5 (IRF5) gene confers risk of inflammatory bowel diseases.";
RL Hum. Mol. Genet. 16:3008-3016(2007).
RN [17]
RP UBIQUITINATION AT LYS-411 AND LYS-412 BY TRAF6.
RX PubMed=18824541; DOI=10.1128/MCB.00662-08;
RA Balkhi M.Y., Fitzgerald K.A., Pitha P.M.;
RT "Functional regulation of MyD88-activated interferon regulatory factor
RT 5 by K63-linked polyubiquitination.";
RL Mol. Cell. Biol. 28:7296-7308(2008).
RN [18]
RP PHOSPHORYLATION AT THR-10; SER-158; SER-293; SER-301; SER-435 AND
RP SER-446, AND SUBCELLULAR LOCATION.
RX PubMed=22412986; DOI=10.1371/journal.pone.0033098;
RA Chang Foreman H.C., Van Scoy S., Cheng T.F., Reich N.C.;
RT "Activation of interferon regulatory factor 5 by site specific
RT phosphorylation.";
RL PLoS ONE 7:E33098-E33098(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 232-477 OF MUTANT ASP-440,
RP SUBUNIT, AND PHOSPHORYLATION AT SER-435; SER-437; SER-440 AND SER-446.
RX PubMed=18836453; DOI=10.1038/nsmb.1496;
RA Chen W., Lam S.S., Srinath H., Jiang Z., Correia J.J., Schiffer C.A.,
RA Fitzgerald K.A., Lin K., Royer W.E. Jr.;
RT "Insights into interferon regulatory factor activation from the
RT crystal structure of dimeric IRF5.";
RL Nat. Struct. Mol. Biol. 15:1213-1220(2008).
CC -!- FUNCTION: Transcription factor involved in the induction of
CC interferons IFNA and INFB and inflammatory cytokines upon virus
CC infection. Activated by TLR7 or TLR8 signaling.
CC -!- SUBUNIT: Homodimer, when phosphorylated.
CC -!- INTERACTION:
CC Q7Z434:MAVS; NbExp=2; IntAct=EBI-3931258, EBI-995373;
CC O43765:SGTA; NbExp=3; IntAct=EBI-3931258, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q13568-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13568-2; Sequence=VSP_041375;
CC Name=3;
CC IsoId=Q13568-3; Sequence=VSP_043924;
CC Name=4;
CC IsoId=Q13568-4; Sequence=VSP_043925;
CC Name=5;
CC IsoId=Q13568-5; Sequence=VSP_044822;
CC -!- PTM: Phosphorylation of serine and threonine residues in a C-
CC terminal autoinhibitory region, stimulates dimerization, transport
CC into the nucleus, assembly with the coactivator CBP/p300 and
CC initiation of transcription.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for
CC activation.
CC -!- DISEASE: Inflammatory bowel disease 14 (IBD14) [MIM:612245]: A
CC chronic, relapsing inflammation of the gastrointestinal tract with
CC a complex etiology. It is subdivided into Crohn disease and
CC ulcerative colitis phenotypes. Crohn disease may affect any part
CC of the gastrointestinal tract from the mouth to the anus, but most
CC frequently it involves the terminal ileum and colon. Bowel
CC inflammation is transmural and discontinuous; it may contain
CC granulomas or be associated with intestinal or perianal fistulas.
CC In contrast, in ulcerative colitis, the inflammation is continuous
CC and limited to rectal and colonic mucosal layers; fistulas and
CC granulomas are not observed. Both diseases include extraintestinal
CC inflammation of the skin, eyes, or joints. Note=Disease
CC susceptibility is associated with variations affecting the gene
CC represented in this entry.
CC -!- DISEASE: Systemic lupus erythematosus 10 (SLEB10) [MIM:612251]: A
CC chronic, relapsing, inflammatory, and often febrile multisystemic
CC disorder of connective tissue, characterized principally by
CC involvement of the skin, joints, kidneys and serosal membranes. It
CC is of unknown etiology, but is thought to represent a failure of
CC the regulatory mechanisms of the autoimmune system. The disease is
CC marked by a wide range of system dysfunctions, an elevated
CC erythrocyte sedimentation rate, and the formation of LE cells in
CC the blood or bone marrow. Note=Disease susceptibility is
CC associated with variations affecting the gene represented in this
CC entry.
CC -!- DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory
CC disease with autoimmune features and a complex genetic component.
CC It primarily affects the joints and is characterized by
CC inflammatory changes in the synovial membranes and articular
CC structures, widespread fibrinoid degeneration of the collagen
CC fibers in mesenchymal tissues, and by atrophy and rarefaction of
CC bony structures. Note=Disease susceptibility is associated with
CC variations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the IRF family.
CC -!- SIMILARITY: Contains 1 IRF tryptophan pentad repeat DNA-binding
CC domain.
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DR EMBL; AY504947; AAR90326.1; -; mRNA.
DR EMBL; AY504946; AAR90325.1; -; mRNA.
DR EMBL; AY693665; AAU12877.1; -; mRNA.
DR EMBL; AY693666; AAU12878.1; -; mRNA.
DR EMBL; AY693668; AAU12880.1; -; mRNA.
DR EMBL; DQ277633; ABB88960.1; -; mRNA.
DR EMBL; U51127; AAA96056.1; -; mRNA.
DR EMBL; EF064718; ABK41901.1; -; Genomic_DNA.
DR EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24107.1; -; Genomic_DNA.
DR EMBL; CH236950; EAL24108.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83703.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83705.1; -; Genomic_DNA.
DR EMBL; BC004201; AAH04201.1; -; mRNA.
DR EMBL; BC004139; AAH04139.1; -; mRNA.
DR EMBL; DQ995495; ABL96293.1; -; Genomic_DNA.
DR EMBL; DQ995496; ABL96294.1; -; Genomic_DNA.
DR IPI; IPI00220220; -.
DR IPI; IPI00396061; -.
DR IPI; IPI00746140; -.
DR IPI; IPI00940314; -.
DR PIR; G02474; G02474.
DR RefSeq; NP_001092097.2; NM_001098627.2.
DR RefSeq; NP_001092099.1; NM_001098629.1.
DR RefSeq; NP_001092100.1; NM_001098630.1.
DR RefSeq; NP_001229381.1; NM_001242452.1.
DR RefSeq; NP_116032.1; NM_032643.3.
DR UniGene; Hs.521181; -.
DR PDB; 3DSH; X-ray; 2.00 A; A=232-477.
DR PDBsum; 3DSH; -.
DR ProteinModelPortal; Q13568; -.
DR DIP; DIP-46348N; -.
DR IntAct; Q13568; 11.
DR STRING; 9606.ENSP00000349770; -.
DR PhosphoSite; Q13568; -.
DR DMDM; 20178305; -.
DR PaxDb; Q13568; -.
DR PRIDE; Q13568; -.
DR DNASU; 3663; -.
DR Ensembl; ENST00000249375; ENSP00000249375; ENSG00000128604.
DR Ensembl; ENST00000357234; ENSP00000349770; ENSG00000128604.
DR Ensembl; ENST00000402030; ENSP00000385352; ENSG00000128604.
DR Ensembl; ENST00000473745; ENSP00000419149; ENSG00000128604.
DR Ensembl; ENST00000477535; ENSP00000419950; ENSG00000128604.
DR GeneID; 3663; -.
DR KEGG; hsa:3663; -.
DR UCSC; uc003vog.3; human.
DR UCSC; uc003voh.3; human.
DR CTD; 3663; -.
DR GeneCards; GC07P128577; -.
DR HGNC; HGNC:6120; IRF5.
DR HPA; HPA046700; -.
DR MIM; 180300; phenotype.
DR MIM; 607218; gene.
DR MIM; 612245; phenotype.
DR MIM; 612251; phenotype.
DR neXtProt; NX_Q13568; -.
DR Orphanet; 206; Crohn disease.
DR Orphanet; 186; Primary biliary cirrhosis.
DR Orphanet; 771; Ulcerative colitis.
DR PharmGKB; PA29919; -.
DR eggNOG; NOG45024; -.
DR HOGENOM; HOG000037433; -.
DR HOVERGEN; HBG105715; -.
DR KO; K09446; -.
DR OMA; EDVKWPP; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q13568; -.
DR GenomeRNAi; 3663; -.
DR NextBio; 14327; -.
DR ArrayExpress; Q13568; -.
DR Bgee; Q13568; -.
DR CleanEx; HS_IRF5; -.
DR Genevestigator; Q13568; -.
DR GermOnline; ENSG00000128604; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0000975; F:regulatory region DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IC:BHF-UCL.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IC:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
DR GO; GO:0032494; P:response to peptidoglycan; IDA:BHF-UCL.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
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; IPR017855; SMAD_dom-like.
DR InterPro; IPR008984; SMAD_FHA_domain.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SUPFAM; SSF49879; SMAD_FHA; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; DNA-binding; Immunity; Innate immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Systemic lupus erythematosus; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1 498 Interferon regulatory factor 5.
FT /FTId=PRO_0000154558.
FT DNA_BIND 14 122 IRF tryptophan pentad repeat.
FT MOTIF 12 18 Nuclear localization signal.
FT MOTIF 150 160 Nuclear export signal.
FT COMPBIAS 142 149 Poly-Glu.
FT MOD_RES 10 10 Phosphothreonine.
FT MOD_RES 158 158 Phosphoserine; by TBK1.
FT MOD_RES 293 293 Phosphoserine; by TBK1.
FT MOD_RES 301 301 Phosphoserine.
FT MOD_RES 435 435 Phosphoserine.
FT MOD_RES 437 437 Phosphoserine.
FT MOD_RES 440 440 Phosphoserine.
FT MOD_RES 446 446 Phosphoserine.
FT CROSSLNK 411 411 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 412 412 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 160 160 T -> TDAVQSGPHMTPYSLLK (in isoform 2).
FT /FTId=VSP_041375.
FT VAR_SEQ 161 247 EDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLA
FT PPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISP
FT HMLPL -> V (in isoform 5).
FT /FTId=VSP_044822.
FT VAR_SEQ 161 175 EDVKWPPTLQPPTLR -> DAVQSGPHMTPYSLLKEDVKW
FT (in isoform 3).
FT /FTId=VSP_043924.
FT VAR_SEQ 166 175 Missing (in isoform 4).
FT /FTId=VSP_043925.
FT CONFLICT 253 253 K -> KK (in Ref. 3; AAU12880).
FT HELIX 235 239
FT TURN 242 244
FT STRAND 250 256
FT STRAND 262 266
FT STRAND 272 275
FT HELIX 283 285
FT HELIX 286 289
FT STRAND 294 298
FT HELIX 308 318
FT STRAND 325 330
FT STRAND 333 338
FT STRAND 340 342
FT STRAND 344 348
FT STRAND 367 371
FT HELIX 372 383
FT STRAND 395 401
FT HELIX 409 411
FT STRAND 413 420
FT HELIX 421 431
FT HELIX 450 465
SQ SEQUENCE 498 AA; 56044 MW; 01B2ED95C28384E8 CRC64;
MNQSIPVAPT PPRRVRLKPW LVAQVNSCQY PGLQWVNGEK KLFCIPWRHA TRHGPSQDGD
NTIFKAWAKE TGKYTEGVDE ADPAKWKANL RCALNKSRDF RLIYDGPRDM PPQPYKIYEV
CSNGPAPTDS QPPEDYSFGA GEEEEEEEEL QRMLPSLSLT EDVKWPPTLQ PPTLRPPTLQ
PPTLQPPVVL GPPAPDPSPL APPPGNPAGF RELLSEVLEP GPLPASLPPA GEQLLPDLLI
SPHMLPLTDL EIKFQYRGRP PRALTISNPH GCRLFYSQLE ATQEQVELFG PISLEQVRFP
SPEDIPSDKQ RFYTNQLLDV LDRGLILQLQ GQDLYAIRLC QCKVFWSGPC ASAHDSCPNP
IQREVKTKLF SLEHFLNELI LFQKGQTNTP PPFEIFFCFG EEWPDRKPRE KKLITVQVVP
VAARLLLEMF SGELSWSADS IRLQISNPDL KDRMVEQFKE LHHIWQSQQR LQPVAQAPPG
AGLGVGQGPW PMHPAGMQ
//
