IRF1_MOUSE
ID IRF1_MOUSE Reviewed; 329 AA.
AC P15314;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Interferon regulatory factor 1;
DE Short=IRF-1;
GN Name=Irf1;
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].
RX PubMed=3409321; DOI=10.1016/s0092-8674(88)91307-4;
RA Miyamoto M., Fujita T., Kimura Y., Maruyama M., Harada H., Sudo Y.,
RA Miyata T., Taniguchi T.;
RT "Regulated expression of a gene encoding a nuclear factor, IRF-1, that
RT specifically binds to IFN-beta gene regulatory elements.";
RL Cell 54:903-913(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 UBIQUITINATION.
RX PubMed=10712599; DOI=10.1046/j.1432-1327.2000.01163.x;
RA Nakagawa K., Yokosawa H.;
RT "Degradation of transcription factor IRF-1 by the ubiquitin-proteasome
RT pathway. The C-terminal region governs the protein stability.";
RL Eur. J. Biochem. 267:1680-1686(2000).
RN [4]
RP REVIEW ON FUNCTION.
RX PubMed=11244049; DOI=10.1146/annurev.immunol.19.1.623;
RA Taniguchi T., Ogasawara K., Takaoka A., Tanaka N.;
RT "IRF family of transcription factors as regulators of host defense.";
RL Annu. Rev. Immunol. 19:623-655(2001).
RN [5]
RP INTERACTION WITH PIAS3, SUMOYLATION, AND FUNCTION.
RX PubMed=12387893; DOI=10.1016/s0014-5793(02)03486-5;
RA Nakagawa K., Yokosawa H.;
RT "PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-
RT 1.";
RL FEBS Lett. 530:204-208(2002).
RN [6]
RP REVIEW ON FUNCTION.
RX PubMed=11846971; DOI=10.1089/107999002753452610;
RA Kroeger A., Koester M., Schroeder K., Hauser H., Mueller P.P.;
RT "Activities of IRF-1.";
RL J. Interferon Cytokine Res. 22:5-14(2002).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=11846974; DOI=10.1089/107999002753452647;
RA Romeo G., Fiorucci G., Chiantore M.V., Percario Z.A., Vannucchi S.,
RA Affabris E.;
RT "IRF-1 as a negative regulator of cell proliferation.";
RL J. Interferon Cytokine Res. 22:39-47(2002).
RN [8]
RP REVIEW ON FUNCTION.
RX PubMed=16932750; DOI=10.1038/nri1900;
RA Honda K., Taniguchi T.;
RT "IRFs: master regulators of signalling by Toll-like receptors and cytosolic
RT pattern-recognition receptors.";
RL Nat. Rev. Immunol. 6:644-658(2006).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH
RP MYD88, AND INDUCTION BY IFN-GAMMA.
RX PubMed=17018642; DOI=10.1073/pnas.0607181103;
RA Negishi H., Fujita Y., Yanai H., Sakaguchi S., Ouyang X., Shinohara M.,
RA Takayanagi H., Ohba Y., Taniguchi T., Honda K.;
RT "Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1
RT transcription factor by MyD88 in Toll-like receptor-dependent gene
RT induction program.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15136-15141(2006).
RN [10]
RP FUNCTION, INDUCTION BY IFN-GAMMA, AND SUMOYLATION.
RX PubMed=18955028; DOI=10.1016/j.bbrc.2008.10.092;
RA Kim E.-J., Park J.-S., Um S.-J.;
RT "Ubc9-mediated sumoylation leads to transcriptional repression of IRF-1.";
RL Biochem. Biophys. Res. Commun. 377:952-956(2008).
RN [11]
RP FUNCTION.
RX PubMed=18641303; DOI=10.4049/jimmunol.181.3.1673;
RA Fragale A., Gabriele L., Stellacci E., Borghi P., Perrotti E., Ilari R.,
RA Lanciotti A., Remoli A.L., Venditti M., Belardelli F., Battistini A.;
RT "IFN regulatory factor-1 negatively regulates CD4+ CD25+ regulatory T cell
RT differentiation by repressing Foxp3 expression.";
RL J. Immunol. 181:1673-1682(2008).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=20308629; DOI=10.4049/jimmunol.0902264;
RA Stirnweiss A., Ksienzyk A., Klages K., Rand U., Grashoff M., Hauser H.,
RA Kroeger A.;
RT "IFN regulatory factor-1 bypasses IFN-mediated antiviral effects through
RT viperin gene induction.";
RL J. Immunol. 184:5179-5185(2010).
RN [14]
RP FUNCTION.
RX PubMed=21909274; DOI=10.1371/journal.ppat.1002230;
RA Brien J.D., Daffis S., Lazear H.M., Cho H., Suthar M.S., Gale M. Jr.,
RA Diamond M.S.;
RT "Interferon regulatory factor-1 (IRF-1) shapes both innate and CD8(+) T
RT cell immune responses against West Nile virus infection.";
RL PLoS Pathog. 7:E1002230-E1002230(2011).
RN [15]
RP FUNCTION, AND INDUCTION BY IFN AND INFLUENZA A VIRUS.
RX PubMed=29321274; DOI=10.4049/jimmunol.1701538;
RA Kuriakose T., Zheng M., Neale G., Kanneganti T.D.;
RT "IRF1 is a transcriptional regulator of ZBP1 promoting NLRP3 inflammasome
RT activation and cell death during influenza virus infection.";
RL J. Immunol. 200:1489-1495(2018).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30635240; DOI=10.1016/j.immuni.2018.11.017;
RA Daniels B.P., Kofman S.B., Smith J.R., Norris G.T., Snyder A.G., Kolb J.P.,
RA Gao X., Locasale J.W., Martinez J., Gale M. Jr., Loo Y.M., Oberst A.;
RT "The nucleotide sensor ZBP1 and kinase RIPK3 induce the enzyme IRG1 to
RT promote an antiviral metabolic state in neurons.";
RL Immunity 50:64-76(2019).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 7-111, AND SUBUNIT.
RX PubMed=9422515; DOI=10.1038/34224;
RA Escalante C.R., Yie J., Thanos D., Aggarwal A.K.;
RT "Structure of IRF-1 with bound DNA reveals determinants of interferon
RT regulation.";
RL Nature 391:103-106(1998).
CC -!- FUNCTION: Transcriptional regulator which displays a remarkable
CC functional diversity in the regulation of cellular responses
CC (PubMed:11244049, PubMed:11846971, PubMed:11846974, PubMed:16932750,
CC PubMed:20049431). Regulates transcription of IFN and IFN-inducible
CC genes, host response to viral and bacterial infections, regulation of
CC many genes expressed during hematopoiesis, inflammation, immune
CC responses and cell proliferation and differentiation, regulation of the
CC cell cycle and induction of growth arrest and programmed cell death
CC following DNA damage (PubMed:11244049, PubMed:11846971,
CC PubMed:11846974, PubMed:16932750, PubMed:20049431). Stimulates both
CC innate and acquired immune responses through the activation of specific
CC target genes and can act as a transcriptional activator and repressor
CC regulating target genes by binding to an interferon-stimulated response
CC element (ISRE) in their promoters (PubMed:11244049, PubMed:11846971,
CC PubMed:11846974, PubMed:16932750, PubMed:20049431). Binds to a
CC consensus sequence in gene promoters (By similarity). Its target genes
CC for transcriptional activation activity are: genes involved in anti-
CC viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL,
CC ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial
CC response, such as NOS2/INOS; anti-proliferative response, such as
CC p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7
CC and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2
CC and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC
CC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B
CC and B2M and MHC class II expression, such as CIITA; metabolic enzymes,
CC such as ACOD1/IRG1 (PubMed:12387893, PubMed:17018642, PubMed:18955028,
CC PubMed:21909274, PubMed:20308629, PubMed:29321274, PubMed:30635240).
CC Represses genes involved in anti-proliferative response, such as
CC BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune
CC response, such as FOXP3, IL4, ANXA2 and TLR4 (PubMed:18641303).
CC Stimulates p53/TP53-dependent transcription through enhanced
CC recruitment of EP300 leading to increased acetylation of p53/TP53 (By
CC similarity). Plays an important role in immune response directly
CC affecting NK maturation and activity, macrophage production of IL12,
CC Th1 development and maturation of CD8+ T-cells (PubMed:11244049,
CC PubMed:11846971, PubMed:11846974, PubMed:16932750, PubMed:20049431).
CC Also implicated in the differentiation and maturation of dendritic
CC cells and in the suppression of regulatory T (Treg) cells development
CC (PubMed:11244049, PubMed:11846971, PubMed:11846974, PubMed:16932750,
CC PubMed:20049431). Acts as a tumor suppressor and plays a role not only
CC in antagonism of tumor cell growth but also in stimulating an immune
CC response against tumor cells (PubMed:11244049, PubMed:11846971,
CC PubMed:11846974, PubMed:16932750, PubMed:20049431).
CC {ECO:0000250|UniProtKB:P10914, ECO:0000269|PubMed:11244049,
CC ECO:0000269|PubMed:11846971, ECO:0000269|PubMed:11846974,
CC ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:16932750,
CC ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:18641303,
CC ECO:0000269|PubMed:18955028, ECO:0000269|PubMed:20049431,
CC ECO:0000269|PubMed:20308629, ECO:0000269|PubMed:21909274,
CC ECO:0000269|PubMed:29321274, ECO:0000269|PubMed:30635240,
CC ECO:0000303|PubMed:11244049, ECO:0000303|PubMed:11846971,
CC ECO:0000303|PubMed:11846974, ECO:0000303|PubMed:16932750,
CC ECO:0000303|PubMed:20049431}.
CC -!- ACTIVITY REGULATION: Activated by MYD88. {ECO:0000269|PubMed:17018642}.
CC -!- SUBUNIT: Monomer (PubMed:9422515). Homodimer (PubMed:9422515).
CC Interacts with EP300 (By similarity). Interacts with MYD88
CC (PubMed:17018642). Interacts with PIAS3 (PubMed:12387893).
CC {ECO:0000250|UniProtKB:P10914, ECO:0000269|PubMed:12387893,
CC ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:9422515}.
CC -!- INTERACTION:
CC P15314; Q14145: KEAP1; Xeno; NbExp=2; IntAct=EBI-6115486, EBI-751001;
CC P15314; Q13114: TRAF3; Xeno; NbExp=2; IntAct=EBI-6115486, EBI-357631;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17018642,
CC ECO:0000269|PubMed:30635240}. Cytoplasm {ECO:0000269|PubMed:17018642}.
CC Note=MYD88-associated IRF1 migrates into the nucleus more efficiently
CC than non-MYD88-associated IRF1. {ECO:0000269|PubMed:17018642}.
CC -!- INDUCTION: Induced by IFN-gamma (PubMed:17018642, PubMed:18955028,
CC PubMed:29321274). Induced by influenza A virus (PubMed:29321274).
CC {ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:18955028,
CC ECO:0000269|PubMed:29321274}.
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 (PubMed:12387893,
CC PubMed:18955028). Sumolyated by UBE2I/UBC9 and SUMO1 (PubMed:18955028).
CC Inactivates the tumor suppressor activity (By similarity). Elevated
CC levels in tumor cells (By similarity). Major site is Lys-276 (By
CC similarity). Sumoylation is enhanced by PIAS3 (PubMed:12387893).
CC Desumoylated by SENP1 in tumor cells and appears to compete with
CC ubiquitination on C-terminal sites (By similarity).
CC {ECO:0000250|UniProtKB:P10914, ECO:0000269|PubMed:12387893,
CC ECO:0000269|PubMed:18955028}.
CC -!- PTM: Ubiquitinated. Appears to compete with sumoylation on C-terminal
CC sites (By similarity). {ECO:0000250|UniProtKB:P10914}.
CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
CC ProRule:PRU00840}.
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DR EMBL; M21065; AAA39334.1; -; mRNA.
DR EMBL; BC003821; AAH03821.1; -; mRNA.
DR CCDS; CCDS24686.1; -.
DR PIR; A31595; A31595.
DR RefSeq; NP_001152868.1; NM_001159396.1.
DR RefSeq; NP_032416.1; NM_008390.2.
DR PDB; 1IF1; X-ray; 3.00 A; A/B=1-113.
DR PDBsum; 1IF1; -.
DR AlphaFoldDB; P15314; -.
DR SMR; P15314; -.
DR BioGRID; 200784; 7.
DR CORUM; P15314; -.
DR DIP; DIP-61281N; -.
DR IntAct; P15314; 6.
DR STRING; 10090.ENSMUSP00000104548; -.
DR iPTMnet; P15314; -.
DR PhosphoSitePlus; P15314; -.
DR EPD; P15314; -.
DR PaxDb; P15314; -.
DR PRIDE; P15314; -.
DR ProteomicsDB; 267152; -.
DR Antibodypedia; 3180; 494 antibodies from 37 providers.
DR DNASU; 16362; -.
DR Ensembl; ENSMUST00000019043; ENSMUSP00000019043; ENSMUSG00000018899.
DR Ensembl; ENSMUST00000108920; ENSMUSP00000104548; ENSMUSG00000018899.
DR GeneID; 16362; -.
DR KEGG; mmu:16362; -.
DR UCSC; uc007iww.2; mouse.
DR CTD; 3659; -.
DR MGI; MGI:96590; Irf1.
DR VEuPathDB; HostDB:ENSMUSG00000018899; -.
DR eggNOG; ENOG502QVVN; Eukaryota.
DR GeneTree; ENSGT00940000156288; -.
DR HOGENOM; CLU_056386_1_0_1; -.
DR InParanoid; P15314; -.
DR OMA; PGLVWIN; -.
DR OrthoDB; 734108at2759; -.
DR PhylomeDB; P15314; -.
DR TreeFam; TF328512; -.
DR BioGRID-ORCS; 16362; 21 hits in 80 CRISPR screens.
DR ChiTaRS; Irf1; mouse.
DR EvolutionaryTrace; P15314; -.
DR PRO; PR:P15314; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P15314; protein.
DR Bgee; ENSMUSG00000018899; Expressed in small intestine Peyer's patch and 255 other tissues.
DR ExpressionAtlas; P15314; baseline and differential.
DR Genevisible; P15314; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA: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; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0002376; P:immune system process; IBA:GO_Central.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB.
DR GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; TAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; TAS:UniProtKB.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; TAS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IMP:UniProtKB.
DR GO; GO:0002819; P:regulation of adaptive immune response; TAS:UniProtKB.
DR GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060416; P:response to growth hormone; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Antiviral defense; Cytoplasm;
KW DNA-binding; Immunity; Innate immunity; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..329
FT /note="Interferon regulatory factor 1"
FT /id="PRO_0000154546"
FT DNA_BIND 5..113
FT /note="IRF tryptophan pentad repeat"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840"
FT REGION 93..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10914"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1IF1"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1IF1"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1IF1"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1IF1"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1IF1"
SQ SEQUENCE 329 AA; 37319 MW; 0E5DD23C0D977B34 CRC64;
MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK DACLFRSWAI
HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPPLTRNQR
KERKSKSSRD TKSKTKRKLC GDVSPDTFSD GLSSSTLPDD HSSYTTQGYL GQDLDMERDI
TPALSPCVVS SSLSEWHMQM DIIPDSTTDL YNLQVSPMPS TSEAATDEDE EGKIAEDLMK
LFEQSEWQPT HIDGKGYLLN EPGTQLSSVY GDFSCKEEPE IDSPRGDIGI GIQHVFTEMK
NMDSIMWMDS LLGNSVRLPP SIQAIPCAP
