ID IRF3_MOUSE Reviewed; 419 AA.
AC P70671;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Interferon regulatory factor 3;
DE Short=IRF-3;
GN Name=Irf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Hakem R., Grossman A., Antonio L., Suggs S., Mak T.W.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=15800576; DOI=10.1038/nature03464;
RA Honda K., Yanai H., Negishi H., Asagiri M., Sato M., Mizutani T.,
RA Shimada N., Ohba Y., Takaoka A., Yoshida N., Taniguchi T.;
RT "IRF-7 is the master regulator of type-I interferon-dependent immune
RT responses.";
RL Nature 434:772-777(2005).
RN [4]
RP REVIEW ON FUNCTION.
RX PubMed=16846591; DOI=10.1016/j.bcp.2006.06.002;
RA Solis M., Goubau D., Romieu-Mourez R., Genin P., Civas A., Hiscott J.;
RT "Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and
RT control of anti-tumor activity in primary macrophages.";
RL Biochem. Pharmacol. 72:1469-1476(2006).
RN [5]
RP REVIEW ON FUNCTION.
RX PubMed=16979567; DOI=10.1016/j.immuni.2006.08.009;
RA Honda K., Takaoka A., Taniguchi T.;
RT "Type I interferon gene induction by the interferon regulatory factor
RT family of transcription factors.";
RL Immunity 25:349-360(2006).
RN [6]
RP ERRATUM OF PUBMED:16979567.
RA Honda K., Takaoka A., Taniguchi T.;
RL Immunity 25:849-849(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=18724932; DOI=10.1016/j.cell.2008.06.032;
RA Stetson D.B., Ko J.S., Heidmann T., Medzhitov R.;
RT "Trex1 prevents cell-intrinsic initiation of autoimmunity.";
RL Cell 134:587-598(2008).
RN [8]
RP REVIEW ON FUNCTION.
RX PubMed=20049431; DOI=10.1007/s00262-009-0804-6;
RA Savitsky D., Tamura T., Yanai H., Taniguchi T.;
RT "Regulation of immunity and oncogenesis by the IRF transcription factor
RT family.";
RL Cancer Immunol. Immunother. 59:489-510(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP PHOSPHORYLATION UPON SSRNA VIRAL INFECTION.
RX PubMed=22065572; DOI=10.1074/jbc.m111.285205;
RA Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.;
RT "Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2
RT proteins define novel innate immune effector pathway against West Nile
RT virus infection.";
RL J. Biol. Chem. 286:44412-44423(2011).
CC -!- FUNCTION: Key transcriptional regulator of type I interferon (IFN)-
CC dependent immune responses which plays a critical role in the innate
CC immune response against DNA and RNA viruses (PubMed:15800576).
CC Regulates the transcription of type I IFN genes (IFN-alpha and IFN-
CC beta) and IFN-stimulated genes (ISG) by binding to an interferon-
CC stimulated response element (ISRE) in their promoters
CC (PubMed:15800576). Acts as a more potent activator of the IFN-beta
CC (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in
CC both the early and late phases of the IFNA/B gene induction
CC (PubMed:16846591, PubMed:16979567, PubMed:20049431). Found in an
CC inactive form in the cytoplasm of uninfected cells and following viral
CC infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR)
CC signaling, is phosphorylated by IKBKE and TBK1 kinases
CC (PubMed:16846591, PubMed:16979567, PubMed:20049431). This induces a
CC conformational change, leading to its dimerization and nuclear
CC localization and association with CREB binding protein (CREBBP) to form
CC dsRNA-activated factor 1 (DRAF1), a complex which activates the
CC transcription of the type I IFN and ISG genes (PubMed:16846591,
CC PubMed:16979567, PubMed:20049431). Can activate distinct gene
CC expression programs in macrophages and can induce significant apoptosis
CC in primary macrophages (PubMed:16846591, PubMed:16979567,
CC PubMed:20049431). {ECO:0000269|PubMed:15800576,
CC ECO:0000303|PubMed:16846591, ECO:0000303|PubMed:16979567,
CC ECO:0000303|PubMed:20049431}.
CC -!- ACTIVITY REGULATION: In the absence of viral infection, maintained as a
CC monomer in an autoinhibited state. Phosphorylation by TBK1 and IKBKE
CC disrupts this autoinhibition leading to the liberation of the DNA-
CC binding and dimerization activities and its nuclear localization where
CC it can activate type I IFN and ISG genes. Phosphorylation and
CC activation follow the following steps: innate adapter proteins, such as
CC MAVS, STING1 or TICAM1, are first activated by viral RNA, cytosolic DNA
CC and bacterial lipopolysaccharide (LPS), respectively, leading to
CC activation of the kinases TBK1 and IKBKE. These kinases then
CC phosphorylate the adapter proteins on their pLxIS motif, leading to
CC recruitment of IRF3, thereby licensing IRF3 for phosphorylation by
CC TBK1. Phosphorylated IRF3 dissociates from the adapter proteins,
CC dimerizes, and then enters the nucleus to induce IFNs.
CC {ECO:0000250|UniProtKB:Q14653}.
CC -!- SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Interacts (when
CC phosphorylated) with CREBBP. Interacts with MAVS (via phosphorylated
CC pLxIS motif). Interacts with TICAM1 (via phosphorylated pLxIS motif).
CC Interacts with STING1 (via phosphorylated pLxIS motif). Interacts with
CC IKBKE and TBK1. Interacts with TICAM2. Interacts with RBCK1. Interacts
CC with HERC5. Interacts with DDX3X; the interaction allows the
CC phosphorylation and activation of IRF3 by IKBKE. Interacts with TRIM21
CC and ULK1, in the presence of TRIM21; this interaction leads to IRF3
CC degradation by autophagy. Interacts with RIOK3; RIOK3 probably mediates
CC the interaction of TBK1 with IRF3. Interacts with ILRUN; the
CC interaction inhibits IRF3 binding to its DNA consensus sequence.
CC Interacts with LYAR; this interaction impairs IRF3 DNA-binding
CC activity. Interacts with TRAF3. Interacts with ZDHHC11; ZDHHC11
CC recruits IRF3 to STING1 upon DNA virus infection and thereby promotes
CC IRF3 activation (By similarity). Interacts with HSP90AA1; the
CC interaction mediates IRF3 association with TOMM70. Interacts with BCL2;
CC the interaction decreases upon Sendai virus infection. Interacts with
CC BAX; the interaction is direct, increases upon virus infection and
CC mediates the formation of the apoptosis complex
CC TOMM70:HSP90AA1:IRF3:BAX (By similarity). Interacts with DDX56 (By
CC similarity). Interacts with NBR1 (By similarity).
CC {ECO:0000250|UniProtKB:Q14653}.
CC -!- INTERACTION:
CC P70671; P70671: Irf3; NbExp=3; IntAct=EBI-7947049, EBI-7947049;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14653}. Nucleus
CC {ECO:0000250|UniProtKB:Q14653}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q14653}. Note=Shuttles between cytoplasmic and
CC nuclear compartments, with export being the prevailing effect. When
CC activated, IRF3 interaction with CREBBP prevents its export to the
CC cytoplasm. Recruited to mitochondria via TOMM70:HSP90AA1 upon Sendai
CC virus infection. {ECO:0000250|UniProtKB:Q14653}.
CC -!- PTM: Constitutively phosphorylated on many Ser/Thr residues
CC (PubMed:22065572). Activated following phosphorylation by TBK1 and
CC IKBKE (By similarity). Innate adapter proteins, such as MAVS, STING1 or
CC TICAM1, are first activated by viral RNA, cytosolic DNA, and bacterial
CC lipopolysaccharide (LPS), respectively, leading to activation of the
CC kinases TBK1 and IKBKE (By similarity). These kinases then
CC phosphorylate the adapter proteins on the pLxIS motif, leading to
CC recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1
CC (By similarity). Phosphorylation at Ser-379 is followed by
CC pyrophosphorylation at the same residue, promoting phosphorylation at
CC Ser-388 (By similarity). Phosphorylated IRF3 dissociates from the
CC adapter proteins, dimerizes, and then enters the nucleus to induce IFNs
CC (By similarity). {ECO:0000250|UniProtKB:Q14653,
CC ECO:0000269|PubMed:22065572}.
CC -!- PTM: Pyrophosphorylated by UAP1 following phosphorylation at Ser-379 by
CC TBK1 (By similarity). Pyrophosphorylation promotes subsequent
CC phosphorylation at Ser-388, leading to homodimerization of IRF3 (By
CC similarity). {ECO:0000250|UniProtKB:Q14653}.
CC -!- PTM: Ubiquitinated; ubiquitination involves RBCK1 leading to
CC proteasomal degradation. Polyubiquitinated; ubiquitination involves
CC TRIM21 leading to proteasomal degradation. Ubiquitinated by UBE3C,
CC leading to its degradation. {ECO:0000250|UniProtKB:Q14653}.
CC -!- PTM: ISGylated by HERC5 resulting in sustained IRF3 activation and in
CC the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The
CC phosphorylation state of IRF3 does not alter ISGylation.
CC {ECO:0000250|UniProtKB:Q14653}.
CC -!- PTM: Proteolytically cleaved by apoptotic caspases during apoptosis,
CC leading to its inactivation. Cleavage by CASP3 during virus-induced
CC apoptosis inactivates it, preventing cytokine overproduction.
CC {ECO:0000250|UniProtKB:Q14653}.
CC -!- DISRUPTION PHENOTYPE: Double knockout with TREX1 does not show a
CC visible phenotype. {ECO:0000269|PubMed:18724932}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; U75839; AAB36924.1; -; mRNA.
DR EMBL; U75840; AAB36925.1; -; mRNA.
DR EMBL; BC050882; AAH50882.1; -; mRNA.
DR CCDS; CCDS21224.1; -.
DR RefSeq; NP_058545.1; NM_016849.4.
DR RefSeq; XP_006541058.1; XM_006540995.3.
DR RefSeq; XP_006541059.1; XM_006540996.2.
DR PDB; 7JFM; X-ray; 2.23 A; A/B=184-390.
DR PDBsum; 7JFM; -.
DR AlphaFoldDB; P70671; -.
DR SMR; P70671; -.
DR BioGRID; 207570; 12.
DR DIP; DIP-29881N; -.
DR IntAct; P70671; 3.
DR MINT; P70671; -.
DR STRING; 10090.ENSMUSP00000003284; -.
DR ChEMBL; CHEMBL4105802; -.
DR iPTMnet; P70671; -.
DR PhosphoSitePlus; P70671; -.
DR EPD; P70671; -.
DR jPOST; P70671; -.
DR PaxDb; 10090-ENSMUSP00000003284; -.
DR PeptideAtlas; P70671; -.
DR ProteomicsDB; 268992; -.
DR Pumba; P70671; -.
DR Antibodypedia; 1283; 1663 antibodies from 46 providers.
DR DNASU; 54131; -.
DR Ensembl; ENSMUST00000003284.16; ENSMUSP00000003284.9; ENSMUSG00000003184.16.
DR Ensembl; ENSMUST00000107834.2; ENSMUSP00000103465.2; ENSMUSG00000003184.16.
DR Ensembl; ENSMUST00000209066.2; ENSMUSP00000146773.2; ENSMUSG00000003184.16.
DR GeneID; 54131; -.
DR KEGG; mmu:54131; -.
DR UCSC; uc009gsm.2; mouse.
DR AGR; MGI:1859179; -.
DR CTD; 3661; -.
DR MGI; MGI:1859179; Irf3.
DR VEuPathDB; HostDB:ENSMUSG00000003184; -.
DR eggNOG; ENOG502QTRR; Eukaryota.
DR GeneTree; ENSGT00940000160569; -.
DR HOGENOM; CLU_031544_2_0_1; -.
DR InParanoid; P70671; -.
DR OMA; DRGVMGY; -.
DR OrthoDB; 3740806at2759; -.
DR PhylomeDB; P70671; -.
DR TreeFam; TF328512; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-1606341; IRF3 mediated activation of type 1 IFN.
DR Reactome; R-MMU-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-MMU-3270619; IRF3-mediated induction of type I IFN.
DR Reactome; R-MMU-9013973; TICAM1-dependent activation of IRF3/IRF7.
DR Reactome; R-MMU-918233; TRAF3-dependent IRF activation pathway.
DR Reactome; R-MMU-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-MMU-936964; Activation of IRF3, IRF7 mediated by TBK1, IKBKE.
DR BioGRID-ORCS; 54131; 4 hits in 80 CRISPR screens.
DR ChiTaRS; Irf3; mouse.
DR PRO; PR:P70671; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70671; Protein.
DR Bgee; ENSMUSG00000003184; Expressed in retinal neural layer and 270 other cell types or tissues.
DR ExpressionAtlas; P70671; baseline and differential.
DR Genevisible; P70671; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; IDA:MGI.
DR GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR GO; GO:0009299; P:mRNA transcription; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR GO; GO:0097300; P:programmed necrotic cell death; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IDA:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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-like_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949; INTERFERON REGULATORY FACTOR; 1.
DR PANTHER; PTHR11949:SF1; INTERFERON REGULATORY FACTOR 3; 1.
DR Pfam; PF00605; IRF; 1.
DR Pfam; PF10401; IRF-3; 1.
DR PRINTS; PR00267; INTFRNREGFCT.
DR SMART; SM00348; IRF; 1.
DR SMART; SM01243; IRF-3; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Antiviral defense; Cytoplasm; DNA-binding;
KW Immunity; Innate immunity; Isopeptide bond; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..419
FT /note="Interferon regulatory factor 3"
FT /id="PRO_0000154554"
FT DNA_BIND 5..111
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 140..419
FT /note="Mediates interaction with ZDHHC11"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT REGION 194..353
FT /note="Interaction with HERC5"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT SITE 121..122
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT SITE 125..126
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 379
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 379
FT /note="Phosphoserine; by TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 388
FT /note="Phosphoserine; by IKKE"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:Q14653"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:7JFM"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:7JFM"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:7JFM"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:7JFM"
SQ SEQUENCE 419 AA; 46852 MW; 1FF67C4E0FC7F027 CRC64;
METPKPRILP WLVSQLDLGQ LEGVAWLDES RTRFRIPWKH GLRQDAQMAD FGIFQAWAEA
SGAYTPGKDK PDVSTWKRNF RSALNRKEVL RLAADNSKDP YDPHKVYEFV TPGARDFVHL
GASPDTNGKS SLPHSQENLP KLFDGLILGP LKDEGSSDLA IVSDPSQQLP SPNVNNFLNP
APQENPLKQL LAEEQWEFEV TAFYRGRQVF QQTLFCPGGL RLVGSTADMT LPWQPVTLPD
PEGFLTDKLV KEYVGQVLKG LGNGLALWQA GQCLWAQRLG HSHAFWALGE ELLPDSGRGP
DGEVHKDKDG AVFDLRPFVA DLIAFMEGSG HSPRYTLWFC MGEMWPQDQP WVKRLVMVKV
VPTCLKELLE MAREGGASSL KTVDLHISNS QPISLTSDQY KAYLQDLVED MDFQATGNI
//
