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 27-MAR-2024, entry version 181. 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 RT IRF-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. RX PubMed=25774715; DOI=10.1038/ni.3118; RA Man S.M., Karki R., Malireddi R.K., Neale G., Vogel P., Yamamoto M., RA Lamkanfi M., Kanneganti T.D.; RT "The transcription factor IRF1 and guanylate-binding proteins target RT activation of the AIM2 inflammasome by Francisella infection."; RL Nat. Immunol. 16:467-475(2015). RN [16] RP FUNCTION. RX PubMed=27693356; DOI=10.1016/j.cell.2016.09.012; RA Man S.M., Karki R., Sasai M., Place D.E., Kesavardhana S., Temirov J., RA Frase S., Zhu Q., Malireddi R.K.S., Kuriakose T., Peters J.L., Neale G., RA Brown S.A., Yamamoto M., Kanneganti T.D.; RT "IRGB10 liberates bacterial ligands for sensing by the AIM2 and caspase-11- RT NLRP3 inflammasomes."; RL Cell 167:382-396(2016). RN [17] 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 [18] 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 [19] 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, PubMed:25774715). Regulates transcription of IFN and CC IFN-inducible genes, host response to viral and bacterial infections, CC regulation of many genes expressed during hematopoiesis, inflammation, CC immune responses and cell proliferation and differentiation, regulation CC of the cell cycle and induction of growth arrest and programmed cell CC death 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, RIGI, TNFSF10/TRAIL, ZBP1, CC OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial CC response, such as GBP2, GBP5, IRGB10 and NOS2/INOS; anti-proliferative CC response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as CC BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, CC IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA CC repair, such as POLQ/POLH; MHC class I expression, such as TAP1, CC PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II CC expression, such as CIITA; metabolic enzymes, such as ACOD1/IRG1 CC (PubMed:12387893, PubMed:17018642, PubMed:18955028, PubMed:21909274, CC PubMed:20308629, PubMed:25774715, PubMed:27693356, PubMed:29321274, CC PubMed:30635240). Represses genes involved in anti-proliferative CC response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and CC in immune response, such as FOXP3, IL4, ANXA2 and TLR4 CC (PubMed:18641303). Stimulates p53/TP53-dependent transcription through CC enhanced recruitment of EP300 leading to increased acetylation of CC p53/TP53 (By similarity). Plays an important role in immune response CC directly affecting NK maturation and activity, macrophage production of CC IL12, 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:25774715, ECO:0000269|PubMed:27693356, 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). Interacts CC with SPOP (By similarity). {ECO:0000250|UniProtKB:P10914, CC ECO:0000269|PubMed:12387893, ECO:0000269|PubMed:17018642, CC 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: Ubiquitinated in a SPOP-depedent manner. Sumoylation represses the CC transcriptional activity and displays enhanced resistance to protein CC degradation (PubMed:12387893, PubMed:18955028). Sumolyated by CC UBE2I/UBC9 and SUMO1 (PubMed:18955028). Inactivates the tumor CC suppressor activity (By similarity). Elevated levels in tumor cells (By CC similarity). Major site is Lys-276 (By similarity). Sumoylation is CC enhanced by PIAS3 (PubMed:12387893). Desumoylated by SENP1 in tumor CC cells and appears to compete with ubiquitination on C-terminal sites CC (By similarity). {ECO:0000250|UniProtKB:P10914, CC ECO:0000269|PubMed:12387893, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000104548; -. DR ProteomicsDB; 267152; -. DR Antibodypedia; 3180; 611 antibodies from 37 providers. DR DNASU; 16362; -. DR Ensembl; ENSMUST00000019043.13; ENSMUSP00000019043.7; ENSMUSG00000018899.18. DR Ensembl; ENSMUST00000108920.10; ENSMUSP00000104548.3; ENSMUSG00000018899.18. DR GeneID; 16362; -. DR KEGG; mmu:16362; -. DR UCSC; uc007iww.2; mouse. DR AGR; MGI:96590; -. 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; WHIPVEI; -. DR OrthoDB; 3740806at2759; -. DR PhylomeDB; P15314; -. DR TreeFam; TF328512; -. DR BioGRID-ORCS; 16362; 23 hits in 85 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 259 other cell types or tissues. DR ExpressionAtlas; P15314; baseline and differential. 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; IDA: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:0007249; P:canonical NF-kappaB signal transduction; ISO:MGI. 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:0002376; P:immune system process; IBA:GO_Central. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. 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:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA: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: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; ISO:MGI. DR GO; GO:0060416; P:response to growth hormone; ISO:MGI. DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IMP:UniProtKB. DR CDD; cd00103; IRF; 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; IPR017431; IRF1/IRF2. 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:SF3; INTERFERON REGULATORY FACTOR 1; 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; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00601; IRF_1; 1. DR PROSITE; PS51507; IRF_2; 1. DR Genevisible; P15314; MM. 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 //