ID IL33_MOUSE Reviewed; 266 AA. AC Q8BVZ5; Q2YEJ4; Q3TQN0; Q99L46; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 142. DE RecName: Full=Interleukin-33; DE Short=IL-33; DE Contains: DE RecName: Full=Interleukin-33(102-266); DE Contains: DE RecName: Full=Interleukin-33(109-266); DE Flags: Precursor; GN Name=Il33 {ECO:0000312|MGI:MGI:1924375}; 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], AND FUNCTION. RC STRAIN=BALB/cJ; RX PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015; RA Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K., RA Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F., RA Kastelein R.A.; RT "IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor- RT related protein ST 2 and induces T helper type 2-associated cytokines."; RL Immunity 23:479-490(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Gastric mucosa; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] 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 [4] RP FUNCTION, PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION. RX PubMed=19465481; DOI=10.1074/jbc.m901744200; RA Talabot-Ayer D., Lamacchia C., Gabay C., Palmer G.; RT "Interleukin-33 is biologically active independently of caspase-1 RT cleavage."; RL J. Biol. Chem. 284:19420-19426(2009). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NF-KAPPAB/RELA. RX PubMed=21734074; DOI=10.4049/jimmunol.1003080; RA Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L., Martin M.U.; RT "The dual function cytokine IL-33 interacts with the transcription factor RT NF-kappaB to dampen NF-kappaB-stimulated gene transcription."; RL J. Immunol. 187:1609-1616(2011). RN [6] RP PROTEOLYTIC CLEAVAGE AT PHE-101 BY CSTG AND ELANE, AND PROTEOLYTIC CLEAVAGE RP AT LEU-108 BY ELANE. RX PubMed=22307629; DOI=10.1073/pnas.1115884109; RA Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B., RA Girard J.P., Cayrol C.; RT "IL-33 is processed into mature bioactive forms by neutrophil elastase and RT cathepsin G."; RL Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012). RN [7] RP FUNCTION, INTERACTION WITH H.POLYGYRUS ARI, SUBCELLULAR LOCATION, AND RP INDUCTION BY A.ALTERNATA AND H.POLYGYRUS. RX PubMed=29045903; DOI=10.1016/j.immuni.2017.09.015; RA Osbourn M., Soares D.C., Vacca F., Cohen E.S., Scott I.C., Gregory W.F., RA Smyth D.J., Toivakka M., Kemter A.M., le Bihan T., Wear M., Hoving D., RA Filbey K.J., Hewitson J.P., Henderson H., Gonzalez-Ciscar A., Errington C., RA Vermeren S., Astier A.L., Wallace W.A., Schwarze J., Ivens A.C., RA Maizels R.M., McSorley H.J.; RT "HpARI Protein Secreted by a Helminth Parasite Suppresses Interleukin-33."; RL Immunity 47:739-751(2017). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=34644537; DOI=10.1016/j.immuni.2021.09.010; RA Faas M., Ipseiz N., Ackermann J., Culemann S., Grueneboom A., Schroeder F., RA Rothe T., Scholtysek C., Eberhardt M., Boettcher M., Kirchner P., Stoll C., RA Ekici A., Fuchs M., Kunz M., Weigmann B., Wirtz S., Lang R., Hofmann J., RA Vera J., Voehringer D., Michelucci A., Mougiakakos D., Uderhardt S., RA Schett G., Kroenke G.; RT "IL-33-induced metabolic reprogramming controls the differentiation of RT alternatively activated macrophages and the resolution of inflammation."; RL Immunity 54:2531-2546.e5(2021). RN [9] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=35794369; DOI=10.1038/s41590-022-01255-6; RA Chen W., Chen S., Yan C., Zhang Y., Zhang R., Chen M., Zhong S., Fan W., RA Zhu S., Zhang D., Lu X., Zhang J., Huang Y., Zhu L., Li X., Lv D., Fu Y., RA Iv H., Ling Z., Ma L., Jiang H., Long G., Zhu J., Wu D., Wu B., Sun B.; RT "Allergen protease-activated stress granule assembly and gasdermin D RT fragmentation control interleukin-33 secretion."; RL Nat. Immunol. 23:1021-1030(2022). RN [10] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=35749514; DOI=10.1126/sciimmunol.abl7209; RA Yamagishi R., Kamachi F., Nakamura M., Yamazaki S., Kamiya T., Takasugi M., RA Cheng Y., Nonaka Y., Yukawa-Muto Y., Thuy L.T.T., Harada Y., Arai T., RA Loo T.M., Yoshimoto S., Ando T., Nakajima M., Taguchi H., Ishikawa T., RA Akiba H., Miyake S., Kubo M., Iwakura Y., Fukuda S., Chen W.Y., Kawada N., RA Rudensky A., Nakae S., Hara E., Ohtani N.; RT "Gasdermin D-mediated release of IL-33 from senescent hepatic stellate RT cells promotes obesity-associated hepatocellular carcinoma."; RL Sci. Immunol. 7:eabl7209-eabl7209(2022). CC -!- FUNCTION: Cytokine that binds to and signals through the IL1RL1/ST2 CC receptor which in turn activates NF-kappa-B and MAPK signaling pathways CC in target cells (PubMed:29045903). Involved in the maturation of Th2 CC cells inducing the secretion of T-helper type 2-associated cytokines CC (By similarity). Also involved in activation of mast cells, basophils, CC eosinophils and natural killer cells (By similarity). Acts as an CC enhancer of polarization of alternatively activated macrophages (By CC similarity). Acts as a chemoattractant for Th2 cells, and may function CC as an 'alarmin', that amplifies immune responses during tissue injury CC (By similarity). Induces rapid UCP2-dependent mitochondrial rewiring CC that attenuates the generation of reactive oxygen species and preserves CC the integrity of Krebs cycle required for persistent production of CC itaconate and subsequent GATA3-dependent differentiation of CC inflammation-resolving alternatively activated macrophages CC (PubMed:34644537). {ECO:0000250|UniProtKB:O95760, CC ECO:0000269|PubMed:29045903, ECO:0000269|PubMed:34644537}. CC -!- FUNCTION: In quiescent endothelia the uncleaved form is constitutively CC and abundantly expressed, and acts as a chromatin-associated nuclear CC factor with transcriptional repressor properties, it may sequester CC nuclear NF-kappaB/RELA, lowering expression of its targets (By CC similarity). This form is rapidely lost upon angiogenic or pro- CC inflammatory activation (By similarity). CC {ECO:0000250|UniProtKB:O95760}. CC -!- SUBUNIT: (Microbial infection) Interacts (in reduced form) with CC H.polygyrus ARI; the interaction abolishes the interaction with its CC primary receptor IL1RL1. {ECO:0000269|PubMed:29045903}. CC -!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary high- CC affinity receptor IL1RL1 and the coreceptor IL1RAP. Interacts with CC cargo receptor TMED10; the interaction mediates the translocation from CC the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate CC compartment) and thereby secretion. {ECO:0000250|UniProtKB:O95760}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34644537}. Chromosome CC {ECO:0000250|UniProtKB:O95760}. Cytoplasm CC {ECO:0000250|UniProtKB:O95760}. Cytoplasmic vesicle, secretory vesicle CC {ECO:0000250|UniProtKB:O95760}. Secreted {ECO:0000269|PubMed:35749514, CC ECO:0000269|PubMed:35794369}. Note=Secreted and released in the CC extracellular milieu by passing through the gasdermin-D (GSDMD) pore CC following cleavage by CELA1 (PubMed:35794369, PubMed:35749514). CC Associates with heterochromatin and mitotic chromosomes (By CC similarity). The secretion is dependent on protein unfolding and CC facilitated by the cargo receptor TMED10; it results in protein CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum- CC Golgi intermediate compartment) followed by vesicle entry and secretion CC (By similarity). {ECO:0000250|UniProtKB:O95760, CC ECO:0000269|PubMed:35749514, ECO:0000269|PubMed:35794369}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29045903}. CC Note=(Microbial infection) Upon infection with H.polygyrus, tethered to CC the nucleus by the H.polygyrus parasitic protein ARI. CC {ECO:0000269|PubMed:29045903}. CC -!- INDUCTION: By cold stress, and by infection with the fungus A.alternata CC and the parasite H.polygyrus. {ECO:0000269|PubMed:29045903}. CC -!- DOMAIN: The homeodomain-like HTH domain mediates nuclear localization CC and heterochromatin association. {ECO:0000250}. CC -!- PTM: The full-length protein can be released from cells and is able to CC signal via the IL1RL1/ST2 receptor (PubMed:16286016). However, CC proteolytic processing by CELA1, CSTG/cathepsin G and ELANE/neutrophil CC elastase produces C-terminal peptides that are more active than the CC unprocessed full-length protein (PubMed:22307629, PubMed:35749514). May CC also be proteolytically processed by calpains. Proteolytic cleavage CC mediated by apoptotic caspases including CASP3 and CASP7 results in CC IL33 inactivation (PubMed:16286016, PubMed:19465481). In vitro CC proteolytic cleavage by CASP1 was reported (PubMed:16286016) but could CC not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is CC probably not a direct substrate for that caspase (PubMed:16286016, CC PubMed:19465481). {ECO:0000269|PubMed:16286016, CC ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:22307629, CC ECO:0000269|PubMed:35749514}. CC -!- MISCELLANEOUS: Intraperitoneal injections of IL-33 induce the CC expression of IL-4, IL-5, and IL-13 and lead to severe pathological CC changes in mucosal organs. CC -!- SIMILARITY: Belongs to the IL-1 family. Highly divergent. CC {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; AY905582; AAX86999.1; -; mRNA. DR EMBL; AK075849; BAC36003.1; -; mRNA. DR EMBL; AK163464; BAE37352.1; -; mRNA. DR EMBL; BC003847; AAH03847.1; -; mRNA. DR CCDS; CCDS29740.1; -. DR RefSeq; NP_001158196.1; NM_001164724.1. DR RefSeq; NP_598536.2; NM_133775.2. DR RefSeq; XP_006527526.1; XM_006527463.3. DR RefSeq; XP_011245701.1; XM_011247399.2. DR PDB; 5VI4; X-ray; 2.79 A; A/D=109-266. DR PDBsum; 5VI4; -. DR AlphaFoldDB; Q8BVZ5; -. DR SMR; Q8BVZ5; -. DR BioGRID; 218533; 1. DR IntAct; Q8BVZ5; 1. DR STRING; 10090.ENSMUSP00000025724; -. DR iPTMnet; Q8BVZ5; -. DR PhosphoSitePlus; Q8BVZ5; -. DR MaxQB; Q8BVZ5; -. DR PaxDb; 10090-ENSMUSP00000025724; -. DR ProteomicsDB; 269549; -. DR Antibodypedia; 3362; 1482 antibodies from 44 providers. DR DNASU; 77125; -. DR Ensembl; ENSMUST00000025724.9; ENSMUSP00000025724.9; ENSMUSG00000024810.17. DR Ensembl; ENSMUST00000120388.9; ENSMUSP00000113829.3; ENSMUSG00000024810.17. DR GeneID; 77125; -. DR KEGG; mmu:77125; -. DR UCSC; uc008hec.2; mouse. DR AGR; MGI:1924375; -. DR CTD; 90865; -. DR MGI; MGI:1924375; Il33. DR VEuPathDB; HostDB:ENSMUSG00000024810; -. DR eggNOG; ENOG502RW83; Eukaryota. DR GeneTree; ENSGT00390000005185; -. DR InParanoid; Q8BVZ5; -. DR OMA; KTACYFR; -. DR OrthoDB; 4642349at2759; -. DR PhylomeDB; Q8BVZ5; -. DR TreeFam; TF338120; -. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-9014843; Interleukin-33 signaling. DR BioGRID-ORCS; 77125; 2 hits in 77 CRISPR screens. DR ChiTaRS; Il33; mouse. DR PRO; PR:Q8BVZ5; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q8BVZ5; Protein. DR Bgee; ENSMUSG00000024810; Expressed in ciliary body and 214 other cell types or tissues. DR ExpressionAtlas; Q8BVZ5; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005615; C:extracellular space; IDA:UniProt. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL. DR GO; GO:0002112; F:interleukin-33 receptor binding; IPI:UniProtKB. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IDA:MGI. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:MGI. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0038172; P:interleukin-33-mediated signaling pathway; IDA:ARUK-UCL. DR GO; GO:0002281; P:macrophage activation involved in immune response; IDA:UniProtKB. DR GO; GO:0030225; P:macrophage differentiation; IDA:UniProtKB. DR GO; GO:0002282; P:microglial cell activation involved in immune response; IDA:UniProtKB. DR GO; GO:0061518; P:microglial cell proliferation; IDA:UniProtKB. DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IGI:BHF-UCL. DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; IDA:UniProt. DR GO; GO:0002686; P:negative regulation of leukocyte migration; IGI:BHF-UCL. DR GO; GO:0120042; P:negative regulation of macrophage proliferation; IDA:ARUK-UCL. DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IGI:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0032689; P:negative regulation of type II interferon production; IGI:BHF-UCL. DR GO; GO:0150145; P:positive regulation of CD80 production; IDA:ARUK-UCL. DR GO; GO:0150142; P:positive regulation of CD86 production; IDA:ARUK-UCL. DR GO; GO:0010186; P:positive regulation of cellular defense response; IMP:ARUK-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL. DR GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IGI:BHF-UCL. DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL. DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IGI:BHF-UCL. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IGI:BHF-UCL. DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IGI:BHF-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:ARUK-UCL. DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL. DR GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; IDA:ARUK-UCL. DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IDA:ARUK-UCL. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:ARUK-UCL. DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:ARUK-UCL. DR GO; GO:0002830; P:positive regulation of type 2 immune response; IDA:MGI. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR GO; GO:0042092; P:type 2 immune response; IDA:MGI. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR026145; IL-33. DR PANTHER; PTHR21114; DVS27 PROTEIN; 1. DR PANTHER; PTHR21114:SF0; INTERLEUKIN-33; 1. DR Pfam; PF15095; IL33; 1. DR Genevisible; Q8BVZ5; MM. PE 1: Evidence at protein level; KW 3D-structure; Chromosome; Cytokine; Cytoplasm; Cytoplasmic vesicle; KW Nucleus; Reference proteome; Secreted; Transcription. FT CHAIN 1..266 FT /note="Interleukin-33" FT /id="PRO_0000096791" FT PROPEP 1..101 FT /evidence="ECO:0000305" FT /id="PRO_0000430087" FT CHAIN 102..266 FT /note="Interleukin-33(102-266)" FT /evidence="ECO:0000305" FT /id="PRO_0000430088" FT CHAIN 109..266 FT /note="Interleukin-33(109-266)" FT /evidence="ECO:0000305" FT /id="PRO_0000430089" FT REGION 1..67 FT /note="Homeodomain-like HTH domain" FT /evidence="ECO:0000250|UniProtKB:O95760" FT REGION 66..108 FT /note="Interaction with RELA" FT /evidence="ECO:0000269|PubMed:21734074" FT SITE 101..102 FT /note="Cleavage; by CTSG and ELANE" FT /evidence="ECO:0000269|PubMed:22307629" FT SITE 108..109 FT /note="Cleavage; by ELANE" FT /evidence="ECO:0000269|PubMed:22307629" FT CONFLICT 24..25 FT /note="AL -> RS (in Ref. 1; AAX86999)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="L -> V (in Ref. 3; AAH03847)" FT /evidence="ECO:0000305" FT CONFLICT 185 FT /note="P -> S (in Ref. 1; AAX86999)" FT /evidence="ECO:0000305" FT STRAND 117..125 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 156..166 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 177..187 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:5VI4" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:5VI4" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 227..234 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:5VI4" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:5VI4" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:5VI4" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:5VI4" SQ SEQUENCE 266 AA; 29991 MW; E03C2C297EB43E23 CRC64; MRPRMKYSNS KISPAKFSST AGEALVPPCK IRRSQQKTKE FCHVYCMRLR SGLTIRKETS YFRKEPTKRY SLKSGTKHEE NFSAYPRDSR KRSLLGSIQA FAASVDTLSI QGTSLLTQSP ASLSTYNDQS VSFVLENGCY VINVDDSGKD QEQDQVLLRY YESPCPASQS GDGVDGKKLM VNMSPIKDTD IWLHANDKDY SVELQRGDVS PPEQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE EKDESCNNIM FKLSKI //