IL1B_MOUSE
ID IL1B_MOUSE Reviewed; 269 AA.
AC P10749; Q2M4J6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Interleukin-1 beta;
DE Short=IL-1 beta;
DE Flags: Precursor;
GN Name=Il1b;
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=3491144;
RA Gray P.W., Glaister D., Chen E., Goeddel D.V., Pennica D.;
RT "Two interleukin 1 genes in the mouse: cloning and expression of the cDNA
RT for murine interleukin 1 beta.";
RL J. Immunol. 137:3644-3648(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3492706; DOI=10.1093/nar/14.24.9955;
RA Telford J.L., Macchia G., Massone A., Carinci V., Palla E., Melli M.;
RT "The murine interleukin 1 beta gene: structure and evolution.";
RL Nucleic Acids Res. 14:9955-9963(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ; TISSUE=Spleen;
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Characterization of quantitative trait loci influencing growth and
RT adiposity using congenic mouse strains.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [6]
RP PROTEIN SEQUENCE OF 118-139.
RX PubMed=2967326;
RA Huang J.J., Newton R.C., Rutledge S.J., Horuk R., Matthew J.B.,
RA Covington M., Lin Y.;
RT "Characterization of murine IL-1 beta. Isolation, expression, and
RT purification.";
RL J. Immunol. 140:3838-3843(1988).
RN [7]
RP TISSUE SPECIFICITY, INDUCTION BY LPS, AND MISCELLANEOUS.
RX PubMed=16407890; DOI=10.1038/nature04515;
RA Mariathasan S., Weiss D.S., Newton K., McBride J., O'Rourke K.,
RA Roose-Girma M., Lee W.P., Weinrauch Y., Monack D.M., Dixit V.M.;
RT "Cryopyrin activates the inflammasome in response to toxins and ATP.";
RL Nature 440:228-232(2006).
RN [8]
RP SUBCELLULAR LOCATION, INDUCTION BY LPS, AND MISCELLANEOUS.
RX PubMed=17284521; DOI=10.1242/jcs.03377;
RA Brough D., Rothwell N.J.;
RT "Caspase-1-dependent processing of pro-interleukin-1beta is cytosolic and
RT precedes cell death.";
RL J. Cell Sci. 120:772-781(2007).
RN [9]
RP SUBCELLULAR LOCATION, INDUCTION BY LPS, AND MISCELLANEOUS.
RX PubMed=17641058; DOI=10.4049/jimmunol.179.3.1913;
RA Qu Y., Franchi L., Nunez G., Dubyak G.R.;
RT "Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent
RT on inflammasome activation and correlated with exosome release in murine
RT macrophages.";
RL J. Immunol. 179:1913-1925(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1807351; DOI=10.1016/1047-8477(91)90021-n;
RA van Oostrum J., Priestle J.P., Gruetter M.G., Schmitz A.;
RT "The structure of murine interleukin-1 beta at 2.8-A resolution.";
RL J. Struct. Biol. 107:189-195(1991).
CC -!- FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the
CC major endogenous pyrogen, induces prostaglandin synthesis, neutrophil
CC influx and activation, T-cell activation and cytokine production, B-
CC cell activation and antibody production, and fibroblast proliferation
CC and collagen production. Promotes Th17 differentiation of T-cells.
CC Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-
CC helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF
CC production synergistically with TNF and IL6. Involved in transduction
CC of inflammation downstream of pyroptosis: its mature form is
CC specifically released in the extracellular milieu by passing through
CC the gasdermin-D (GSDMD) pore. {ECO:0000250|UniProtKB:P01584}.
CC -!- SUBUNIT: Monomer. Interacts with MEFV. Interacts with integrins
CC ITGAV:ITGBV and ITGA5:ITGB1; integrin-binding is required for IL1B
CC signaling. Interacts with cargo receptor TMED10; the interaction is
CC direct and is required for the secretion of IL1B mature form (By
CC similarity). Interacts with HSP90AB1; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity). Interacts with HSP90B1;
CC the interaction facilitates cargo translocation into the ERGIC (By
CC similarity). {ECO:0000250|UniProtKB:P01584}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17284521}.
CC Secreted {ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}.
CC Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular
CC exosome {ECO:0000269|PubMed:17641058}. Note=The precursor is cytosolic.
CC In response to inflammasome-activating signals, such as ATP for NLRP3
CC inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and
CC secreted. Mature form is secreted and released in the extracellular
CC milieu by passing through the gasdermin-D (GSDMD) pore. In contrast,
CC the precursor form is not released, due to the presence of an acidic
CC region that is proteolytically removed by CASP1 during maturation. The
CC secretion is dependent on protein unfolding and facilitated by the
CC cargo receptor TMED10. {ECO:0000250|UniProtKB:P01584}.
CC -!- TISSUE SPECIFICITY: Expressed in activated macrophages (at protein
CC level). {ECO:0000269|PubMed:16407890, ECO:0000269|PubMed:17284521,
CC ECO:0000269|PubMed:17641058}.
CC -!- INDUCTION: By LPS. {ECO:0000269|PubMed:16407890,
CC ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}.
CC -!- MISCELLANEOUS: IL1B production occurs in 2 steps, each being controlled
CC by different stimuli. First, inflammatory signals, such as LPS,
CC stimulate the synthesis and promote the accumulation of cytosolic
CC stores of pro-IL1B (priming). Then additional signals are required for
CC inflammasome assembly, leading to CASP1 activation, pro-IL1B processing
CC and eventually secretion of the active cytokine. IL1B processing and
CC secretion are temporarily associated. {ECO:0000269|PubMed:17284521,
CC ECO:0000269|PubMed:17641058}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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DR EMBL; M15131; AAA39276.1; -; mRNA.
DR EMBL; X04964; CAA28637.1; -; Genomic_DNA.
DR EMBL; AY902319; AAX90604.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL28238.1; -; Genomic_DNA.
DR EMBL; BC011437; AAH11437.1; -; mRNA.
DR CCDS; CCDS16726.1; -.
DR PIR; I55969; I55969.
DR RefSeq; NP_032387.1; NM_008361.4.
DR PDB; 2MIB; X-ray; 2.84 A; A=118-269.
DR PDB; 8I1B; X-ray; 2.40 A; A=118-269.
DR PDBsum; 2MIB; -.
DR PDBsum; 8I1B; -.
DR AlphaFoldDB; P10749; -.
DR SMR; P10749; -.
DR BioGRID; 200624; 8.
DR IntAct; P10749; 1.
DR STRING; 10090.ENSMUSP00000028881; -.
DR iPTMnet; P10749; -.
DR PhosphoSitePlus; P10749; -.
DR PaxDb; P10749; -.
DR PRIDE; P10749; -.
DR ProteomicsDB; 266968; -.
DR TopDownProteomics; P10749; -.
DR ABCD; P10749; 1 sequenced antibody.
DR Antibodypedia; 771; 2277 antibodies from 49 providers.
DR DNASU; 16176; -.
DR Ensembl; ENSMUST00000028881; ENSMUSP00000028881; ENSMUSG00000027398.
DR GeneID; 16176; -.
DR KEGG; mmu:16176; -.
DR UCSC; uc008mht.1; mouse.
DR CTD; 3553; -.
DR MGI; MGI:96543; Il1b.
DR VEuPathDB; HostDB:ENSMUSG00000027398; -.
DR eggNOG; ENOG502S3E9; Eukaryota.
DR GeneTree; ENSGT00950000182943; -.
DR HOGENOM; CLU_083639_0_0_1; -.
DR InParanoid; P10749; -.
DR OMA; QHYSKGF; -.
DR OrthoDB; 1243742at2759; -.
DR PhylomeDB; P10749; -.
DR TreeFam; TF300203; -.
DR Reactome; R-MMU-448706; Interleukin-1 processing.
DR Reactome; R-MMU-5620971; Pyroptosis.
DR Reactome; R-MMU-5660668; CLEC7A/inflammasome pathway.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR BioGRID-ORCS; 16176; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Il1b; mouse.
DR EvolutionaryTrace; P10749; -.
DR PRO; PR:P10749; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P10749; protein.
DR Bgee; ENSMUSG00000027398; Expressed in granulocyte and 64 other tissues.
DR Genevisible; P10749; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0048143; P:astrocyte activation; IDA:MGI.
DR GO; GO:0097398; P:cellular response to interleukin-17; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IGI:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; ISO:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0050900; P:leukocyte migration; IDA:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0070487; P:monocyte aggregation; ISO:MGI.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:BHF-UCL.
DR GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:1903597; P:negative regulation of gap junction assembly; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IMP:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:MGI.
DR GO; GO:0045917; P:positive regulation of complement activation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; ISO:MGI.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:MGI.
DR GO; GO:0035505; P:positive regulation of myosin light chain kinase activity; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IGI:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1902680; P:positive regulation of RNA biosynthetic process; ISO:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS: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; ISO:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:MGI.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IDA:CAFA.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:MGI.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0033198; P:response to ATP; IDA:MGI.
DR GO; GO:0009743; P:response to carbohydrate; IDA:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0030730; P:sequestering of triglyceride; ISO:MGI.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
DR InterPro; IPR003296; IL-1_beta.
DR InterPro; IPR020877; IL-1_CS.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003502; IL-1_propep.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF30; PTHR10078:SF30; 1.
DR Pfam; PF00340; IL1; 1.
DR Pfam; PF02394; IL1_propep; 1.
DR PRINTS; PR00264; INTERLEUKIN1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00253; INTERLEUKIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Cytoplasm; Direct protein sequencing;
KW Inflammatory response; Lysosome; Mitogen; Pyrogen; Reference proteome;
KW Secreted.
FT PROPEP 1..117
FT /evidence="ECO:0000269|PubMed:2967326"
FT /id="PRO_0000015311"
FT CHAIN 118..269
FT /note="Interleukin-1 beta"
FT /id="PRO_0000015312"
FT SITE 172
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 180
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 182
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 191
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 205
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:8I1B"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:8I1B"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:8I1B"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:8I1B"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:8I1B"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2MIB"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:8I1B"
SQ SEQUENCE 269 AA; 30931 MW; 734FA17B02ED87EE CRC64;
MATVPELNCE MPPFDSDEND LFFEVDGPQK MKGCFQTFDL GCPDESIQLQ ISQQHINKSF
RQAVSLIVAV EKLWQLPVSF PWTFQDEDMS TFFSFIFEEE PILCDSWDDD DNLLVCDVPI
RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK
GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS
TSQAEHKPVF LGNNSGQDII DFTMESVSS
