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   27-MAR-2024, entry version 215.
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}.
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; 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   BindingDB; P10749; -.
DR   ChEMBL; CHEMBL5069361; -.
DR   iPTMnet; P10749; -.
DR   PhosphoSitePlus; P10749; -.
DR   PaxDb; 10090-ENSMUSP00000028881; -.
DR   ProteomicsDB; 266968; -.
DR   TopDownProteomics; P10749; -.
DR   ABCD; P10749; 1 sequenced antibody.
DR   Antibodypedia; 771; 2657 antibodies from 51 providers.
DR   DNASU; 16176; -.
DR   Ensembl; ENSMUST00000028881.14; ENSMUSP00000028881.8; ENSMUSG00000027398.14.
DR   GeneID; 16176; -.
DR   KEGG; mmu:16176; -.
DR   UCSC; uc008mht.1; mouse.
DR   AGR; MGI:96543; -.
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; QKCLVMS; -.
DR   OrthoDB; 4264279at2759; -.
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 79 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 65 other cell types or tissues.
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:0048018; F:receptor ligand activity; IDA: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: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: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: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:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA: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:0045893; P:positive regulation of DNA-templated transcription; 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: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: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:0050996; P:positive regulation of lipid catabolic process; IDA:BHF-UCL.
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: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:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IGI:ARUK-UCL.
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:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; 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: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   CDD; cd00100; IL1; 1.
DR   Gene3D; 2.80.10.50; -; 1.
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:SF30; INTERLEUKIN-1 BETA; 1.
DR   PANTHER; PTHR10078; INTERLEUKIN-1 FAMILY MEMBER; 1.
DR   Pfam; PF00340; IL1; 1.
DR   Pfam; PF02394; IL1_propep; 1.
DR   PRINTS; PR00262; IL1HBGF.
DR   PRINTS; PR00264; INTERLEUKIN1.
DR   PRINTS; PR01359; INTRLEUKIN1B.
DR   PRINTS; PR01357; INTRLEUKN1AB.
DR   SMART; SM00125; IL1; 1.
DR   SUPFAM; SSF50353; Cytokine; 1.
DR   PROSITE; PS00253; INTERLEUKIN_1; 1.
DR   Genevisible; P10749; MM.
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
//