ID   IRF7_MOUSE              Reviewed;         457 AA.
AC   P70434;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Interferon regulatory factor 7;
DE            Short=IRF-7;
GN   Name=Irf7;
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=Spleen;
RA   Grossman A., Nicholl J., Antonio L., Luethy R., Suggs S., Sutherland G.R.,
RA   Mak T.W.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVIEW ON FUNCTION.
RX   PubMed=11846980; DOI=10.1089/107999002753452700;
RA   Zhang L., Pagano J.S.;
RT   "Structure and function of IRF-7.";
RL   J. Interferon Cytokine Res. 22:95-101(2002).
RN   [3]
RP   FUNCTION, PHOSPHORYLATION AT SER-425; SER-426; SER-429; SER-431; SER-437;
RP   SER-438 AND SER-441, AND MUTAGENESIS OF SER-425; SER-426; LEU-427;
RP   429-SER--SER-431; SER-437; SER-438 AND SER-441.
RX   PubMed=15743772; DOI=10.1074/jbc.m411389200;
RA   Caillaud A., Hovanessian A.G., Levy D.E., Marie I.J.;
RT   "Regulatory serine residues mediate phosphorylation-dependent and
RT   phosphorylation-independent activation of interferon regulatory factor 7.";
RL   J. Biol. Chem. 280:17671-17677(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, AND
RP   INTERACTION WITH MYD88 AND TRAF6.
RX   PubMed=15361868; DOI=10.1038/ni1118;
RA   Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K.,
RA   Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.;
RT   "Interferon-alpha induction through Toll-like receptors involves a direct
RT   interaction of IRF7 with MyD88 and TRAF6.";
RL   Nat. Immunol. 5:1061-1068(2004).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   ERRATUM OF PUBMED:16979567.
RA   Honda K., Takaoka A., Taniguchi T.;
RL   Immunity 25:849-849(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=18562536; DOI=10.1128/jvi.00918-08;
RA   Daffis S., Samuel M.A., Suthar M.S., Keller B.C., Gale M. Jr.,
RA   Diamond M.S.;
RT   "Interferon regulatory factor IRF-7 induces the antiviral alpha interferon
RT   response and protects against lethal West Nile virus infection.";
RL   J. Virol. 82:8465-8475(2008).
RN   [10]
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   [11]
RP   REVIEW ON FUNCTION.
RX   PubMed=21490621; DOI=10.1038/gene.2011.21;
RA   Ning S., Pagano J.S., Barber G.N.;
RT   "IRF7: activation, regulation, modification and function.";
RL   Genes Immun. 12:399-414(2011).
RN   [12]
RP   INTERACTION WITH NMI, UBIQUITINATION, REGION, AND MUTAGENESIS OF
RP   1-MET--GLU-237; 1-MET--VAL-132; 238-ARG--PRO-457; 238-ARG--TRP-410 AND
RP   411-VAL--PRO-457.
RX   PubMed=23956435; DOI=10.4049/jimmunol.1300740;
RA   Wang J., Yang B., Hu Y., Zheng Y., Zhou H., Wang Y., Ma Y., Mao K.,
RA   Yang L., Lin G., Ji Y., Wu X., Sun B.;
RT   "Negative regulation of Nmi on virus-triggered type I IFN production by
RT   targeting IRF7.";
RL   J. Immunol. 191:3393-3399(2013).
RN   [13]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=27129230; DOI=10.1074/jbc.m116.718080;
RA   Ren Y., Zhao Y., Lin D., Xu X., Zhu Q., Yao J., Shu H.B., Zhong B.;
RT   "The Type I Interferon-IRF7 Axis Mediates Transcriptional Expression of
RT   Usp25 Gene.";
RL   J. Biol. Chem. 291:13206-13215(2016).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH GBP4.
RX   PubMed=22095711; DOI=10.4049/jimmunol.1003691;
RA   Hu Y., Wang J., Yang B., Zheng N., Qin M., Ji Y., Lin G., Tian L., Wu X.,
RA   Wu L., Sun B.;
RT   "Guanylate binding protein 4 negatively regulates virus-induced type I IFN
RT   and antiviral response by targeting IFN regulatory factor 7.";
RL   J. Immunol. 187:6456-6462(2011).
CC   -!- FUNCTION: Key transcriptional regulator of type I interferon (IFN)-
CC       dependent immune responses and plays a critical role in the innate
CC       immune response against DNA and RNA viruses (PubMed:27129230,
CC       PubMed:22095711). Regulates the transcription of type I IFN genes (IFN-
CC       alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an
CC       interferon-stimulated response element (ISRE) in their promoters. Can
CC       efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA)
CC       genes and mediate their induction via both the virus-activated, MyD88-
CC       independent pathway and the TLR-activated, MyD88-dependent pathway.
CC       Induces transcription of ubiquitin hydrolase USP25 mRNA in response to
CC       lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent
CC       manner (PubMed:27129230). Required during both the early and late
CC       phases of the IFN gene induction but is more critical for the late than
CC       for the early phase. Exists in an inactive form in the cytoplasm of
CC       uninfected cells and following viral infection, double-stranded RNA
CC       (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated
CC       by IKBKE and TBK1 kinases. This induces a conformational change,
CC       leading to its dimerization and nuclear localization where along with
CC       other coactivators it can activate transcription of the type I IFN and
CC       ISG genes. Can also play a role in regulating adaptive immune responses
CC       by inducing PSMB9/LMP2 expression, either directly or through induction
CC       of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a
CC       (EBNA1) and may play a role in the regulation of EBV latency. Can
CC       activate distinct gene expression programs in macrophages and regulate
CC       the anti-tumor properties of primary macrophages.
CC       {ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:15743772,
CC       ECO:0000269|PubMed:15800576, ECO:0000269|PubMed:18562536,
CC       ECO:0000269|PubMed:22095711, ECO:0000269|PubMed:27129230}.
CC   -!- ACTIVITY REGULATION: In the absence of viral infection, maintained as a
CC       monomer in an autoinhibited state and phosphorylation disrupts this
CC       autoinhibition leading to the liberation of the DNA-binding and
CC       dimerization activities and its nuclear localization where it can
CC       activate type I IFN and ISG genes.
CC   -!- SUBUNIT: Monomer. Homodimer; phosphorylation-induced. Heterodimer with
CC       IRF3. Interacts with TICAM1 and TICAM2. Interacts with MYD88 and TRAF6.
CC       Interacts with NMI; the interaction is direct and leads to the
CC       inhibition of IRF7-mediated type I IFN production (PubMed:23956435).
CC       Interacts with GBP4; preventing interaction between TRAF6 and IRF7,
CC       resulting in impaired TRAF6-mediated IRF7 ubiquitination
CC       (PubMed:22095711). Interacts with TARBP2; this interaction prevents
CC       IRF7 phosphorylation and activation (By similarity).
CC       {ECO:0000250|UniProtKB:Q92985, ECO:0000269|PubMed:15361868,
CC       ECO:0000269|PubMed:22095711, ECO:0000269|PubMed:23956435}.
CC   -!- INTERACTION:
CC       P70434; Q60680: Chuk; NbExp=3; IntAct=EBI-997907, EBI-646245;
CC       P70434; Q8C006: Trim35; NbExp=2; IntAct=EBI-997907, EBI-2536044;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15361868}. Cytoplasm
CC       {ECO:0000269|PubMed:15361868}. Note=The phosphorylated and active form
CC       accumulates selectively in the nucleus.
CC   -!- INDUCTION: Induced by lipopolysaccharide (LPS) (PubMed:27129230).
CC       Induced by type I interferon (IFN) and viruses (HIV-1 and SeV viruses)
CC       (PubMed:27129230). {ECO:0000269|PubMed:27129230}.
CC   -!- PTM: Acetylation inhibits its DNA-binding ability and activity.
CC       {ECO:0000250}.
CC   -!- PTM: In response to a viral infection, phosphorylated by TBK1 and
CC       IKBKE1. Phosphorylation, and subsequent activation is inhibited by
CC       vaccinia virus protein E3. In TLR7- and TLR9-mediated signaling
CC       pathway, phosphorylated by IRAK1 (By similarity). {ECO:0000250}.
CC   -!- PTM: TRAF6-mediated ubiquitination is required for IRF7 activation
CC       (PubMed:15361868, PubMed:22095711). TRIM35 mediates IRF7 'Lys-48'-
CC       linked polyubiquitination and subsequent proteasomal degradation (By
CC       similarity). 'Lys-48'-linked polyubiquitination and subsequent
CC       proteasomal degradation is NMI-dependent in response to Sendai virus
CC       infection (PubMed:23956435). Ubiquitinated by UBE3C, leading to its
CC       degradation (By similarity). {ECO:0000250|UniProtKB:Q92985,
CC       ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:22095711,
CC       ECO:0000269|PubMed:23956435}.
CC   -!- PTM: Sumoylated by TRIM28, which inhibits its transactivation activity.
CC       {ECO:0000250}.
CC   -!- PTM: 'Lys-63'-linked ubiquitination by NEURL3 promotes IRF7 activation.
CC       {ECO:0000250|UniProtKB:Q92985}.
CC   -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00840}.
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DR   EMBL; U73037; AAB18626.1; -; mRNA.
DR   CCDS; CCDS22005.1; -.
DR   RefSeq; NP_058546.1; NM_016850.3.
DR   PDB; 3QU3; X-ray; 1.30 A; A/B/C=1-134.
DR   PDBsum; 3QU3; -.
DR   AlphaFoldDB; P70434; -.
DR   SMR; P70434; -.
DR   BioGRID; 207563; 12.
DR   DIP; DIP-37903N; -.
DR   IntAct; P70434; 8.
DR   MINT; P70434; -.
DR   STRING; 10090.ENSMUSP00000026571; -.
DR   iPTMnet; P70434; -.
DR   PhosphoSitePlus; P70434; -.
DR   PaxDb; 10090-ENSMUSP00000026571; -.
DR   ProteomicsDB; 269505; -.
DR   Antibodypedia; 4325; 716 antibodies from 41 providers.
DR   DNASU; 54123; -.
DR   Ensembl; ENSMUST00000026571.11; ENSMUSP00000026571.5; ENSMUSG00000025498.16.
DR   GeneID; 54123; -.
DR   KEGG; mmu:54123; -.
DR   UCSC; uc009kkg.2; mouse.
DR   AGR; MGI:1859212; -.
DR   CTD; 3665; -.
DR   MGI; MGI:1859212; Irf7.
DR   VEuPathDB; HostDB:ENSMUSG00000025498; -.
DR   eggNOG; ENOG502R2I9; Eukaryota.
DR   GeneTree; ENSGT00940000160931; -.
DR   InParanoid; P70434; -.
DR   OMA; HEIAQME; -.
DR   OrthoDB; 3740806at2759; -.
DR   PhylomeDB; P70434; -.
DR   TreeFam; TF328512; -.
DR   Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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-936964; Activation of IRF3, IRF7 mediated by TBK1, IKBKE.
DR   Reactome; R-MMU-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR   BioGRID-ORCS; 54123; 1 hit in 83 CRISPR screens.
DR   PRO; PR:P70434; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P70434; Protein.
DR   Bgee; ENSMUSG00000025498; Expressed in small intestine Peyer's patch and 108 other cell types or tissues.
DR   ExpressionAtlas; P70434; baseline and differential.
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:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProt.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO: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:0016064; P:immunoglobulin mediated immune response; IMP: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; ISO:MGI.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProt.
DR   GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
DR   GO; GO:0034124; P:regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0034127; P:regulation of MyD88-independent toll-like receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:SF2; INTERFERON REGULATORY FACTOR 7; 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.
DR   Genevisible; P70434; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Cytoplasm; DNA-binding; Immunity;
KW   Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..457
FT                   /note="Interferon regulatory factor 7"
FT                   /id="PRO_0000154563"
FT   DNA_BIND        9..126
FT                   /note="IRF tryptophan pentad repeat"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT   REGION          238..410
FT                   /note="Necessary for the interaction with NMI"
FT                   /evidence="ECO:0000269|PubMed:23956435"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine; by KAT2A and KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:Q92985"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   MOD_RES         426
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   MOD_RES         429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   MOD_RES         431
FT                   /note="Phosphoserine; by TBK1 and IKKE"
FT                   /evidence="ECO:0000250|UniProtKB:Q92985"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:15743772"
FT   CROSSLNK        329
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        398
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        400
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         425
FT                   /note="S->A: Strongly decreased transcriptional activation
FT                   in response to viral infection; when associated with
FT                   A-426."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         425
FT                   /note="S->D: Strongly decreased transcriptional activation
FT                   in response to viral infection; when associated with
FT                   D-426."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         426
FT                   /note="S->A: Strongly decreased transcriptional activation
FT                   in response to viral infection; when associated with
FT                   A-425."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         426
FT                   /note="S->D: Strongly decreased transcriptional activation
FT                   in response to viral infection; when associated with
FT                   D-425."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         427
FT                   /note="L->A: Strongly decreased transcriptional activation
FT                   in response to viral infection."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         427
FT                   /note="L->D: No effect on transcriptional activation in
FT                   response to viral infection."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         429..431
FT                   /note="SSS->AAA: Almost no effect on transcriptional
FT                   activation in response to viral infection."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         429..431
FT                   /note="SSS->DDD: Strongly increased transcriptional
FT                   activation in response to viral infection."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         437
FT                   /note="S->A: Almost complete loss of transcriptional
FT                   activation; when associated with A-438."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         437
FT                   /note="S->D: Increased transcriptional activation; when
FT                   associated with D-438."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         438
FT                   /note="S->A: Almost complete loss of transcriptional
FT                   activation; when associated with A-437."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         438
FT                   /note="S->D: Increased transcriptional activation; when
FT                   associated with D-437."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   MUTAGEN         441
FT                   /note="S->A: Almost no effect on transcriptional activation
FT                   in response to viral infection."
FT                   /evidence="ECO:0000269|PubMed:15743772"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   HELIX           56..64
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   HELIX           77..85
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   HELIX           88..100
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:3QU3"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:3QU3"
SQ   SEQUENCE   457 AA;  51222 MW;  30B102C668F56142 CRC64;
     MAEVRGVQRV LFGDWLLGEV SSGQYEGLQW LNEARTVFRV PWKHFGRRDL DEEDAQIFKA
     WAVARGRWPP SGVNLPPPEA EAAERRERRG WKTNFRCALH STGRFILRQD NSGDPVDPHK
     VYELSRELGS TVGPATENRE EVSLSNALPT QGVSPGSFLA RENAGLQTPS PLLSSDAGDL
     LLQVLQYSHI LESESGADPV PPQAPGQEQD RVYEEPYAAW QVEAVPSPRP QQPALTERSL
     GFLDVTIMYK GRTVLQAVVG HPRCVFLYSP MAPAVRTSEP QPVIFPSPAE LPDQKQLHYT
     ETLLQHVSPG LQLELRGPSL WALRMGKCKV YWEVGSPMGT TGPSTPPQLL ERNRHTPIFD
     FSTFFRELEE FRARRRQGSP HYTIYLGFGQ DLSAGRPKEK TLILVKLEPW VCKAYLEGVQ
     REGVSSLDSS SLGLCLSSTN SLYEDIEHFL MDLGQWP
//