ID IL33_HUMAN Reviewed; 270 AA. AC O95760; B4DJ35; B4E1Q9; D3DRI5; E7EAX4; Q2YEJ5; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 22-JAN-2014, entry version 98. DE RecName: Full=Interleukin-33; DE Short=IL-33; DE AltName: Full=Interleukin-1 family member 11; DE Short=IL-1F11; DE AltName: Full=Nuclear factor from high endothelial venules; DE Short=NF-HEV; DE Flags: Precursor; GN Name=IL33; Synonyms=C9orf26, IL1F11, NFHEV; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND RP SUBCELLULAR LOCATION. RC TISSUE=Endothelial cell; RX PubMed=12819012; DOI=10.1016/S0002-9440(10)63631-0; RA Baekkevold E.S., Roussigne M., Yamanaka T., Johansen F.-E., RA Jahnsen F.L., Amalric F., Brandtzaeg P., Erard M., Haraldsen G., RA Girard J.-P.; RT "Molecular characterization of NF-HEV, a nuclear factor preferentially RT expressed in human high endothelial venules."; RL Am. J. Pathol. 163:69-79(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10566975; DOI=10.1097/00004647-199911000-00013; RA Onda H., Kasuya H., Takakura K., Hori T., Imaizumi T., Takeuchi T., RA Inoue I., Takeda J.; RT "Identification of genes differentially expressed in canine RT vasospastic cerebral arteries after subarachnoid hemorrhage."; RL J. Cereb. Blood Flow Metab. 19:1279-1288(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RP PROTEOLYTIC PROCESSING, AND FUNCTION. 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 RT receptor-related protein ST 2 and induces T helper type 2-associated RT cytokines."; RL Immunity 23:479-490(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=21454686; DOI=10.1074/jbc.M111.219089; RA Hong J., Bae S., Jhun H., Lee S., Choi J., Kang T., Kwak A., Hong K., RA Kim E., Jo S., Kim S.; RT "Identification of constitutively active interleukin 33 (IL-33) splice RT variant."; RL J. Biol. Chem. 286:20078-20086(2011). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP FUNCTION. RX PubMed=17853410; DOI=10.1002/eji.200737547; RA Komai-Koma M., Xu D., Li Y., McKenzie A.N., McInnes I.B., Liew F.Y.; RT "IL-33 is a chemoattractant for human Th2 cells."; RL Eur. J. Immunol. 37:2779-2786(2007). RN [11] RP SUBCELLULAR LOCATION, FUNCTION, AND NUCLEAR TARGETING DOMAIN. RX PubMed=17185418; DOI=10.1073/pnas.0606854104; RA Carriere V., Roussel L., Ortega N., Lacorre D.A., Americh L., RA Aguilar L., Bouche G., Girard J.P.; RT "IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a RT chromatin-associated nuclear factor in vivo."; RL Proc. Natl. Acad. Sci. U.S.A. 104:282-287(2007). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18787100; DOI=10.2353/ajpath.2008.080014; RA Kuchler A.M., Pollheimer J., Balogh J., Sponheim J., Manley L., RA Sorensen D.R., De Angelis P.M., Scott H., Haraldsen G.; RT "Nuclear interleukin-33 is generally expressed in resting endothelium RT but rapidly lost upon angiogenic or proinflammatory activation."; RL Am. J. Pathol. 173:1229-1242(2008). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18836528; DOI=10.1371/journal.pone.0003331; RA Moussion C., Ortega N., Girard J.P.; RT "The IL-1-like cytokine IL-33 is constitutively expressed in the RT nucleus of endothelial cells and epithelial cells in vivo: a novel RT 'alarmin'?"; RL PLoS ONE 3:E3331-E3331(2008). RN [14] RP PROTEOLYTIC PROCESSING. RX PubMed=19596270; DOI=10.1016/j.bbrc.2009.07.018; RA Hayakawa M., Hayakawa H., Matsuyama Y., Tamemoto H., Okazaki H., RA Tominaga S.; RT "Mature interleukin-33 is produced by calpain-mediated cleavage in RT vivo."; RL Biochem. Biophys. Res. Commun. 387:218-222(2009). RN [15] RP PROTEOLYTIC PROCESSING. RX PubMed=19559631; DOI=10.1016/j.immuni.2009.05.007; RA Luthi A.U., Cullen S.P., McNeela E.A., Duriez P.J., Afonina I.S., RA Sheridan C., Brumatti G., Taylor R.C., Kersse K., Vandenabeele P., RA Lavelle E.C., Martin S.J.; RT "Suppression of interleukin-33 bioactivity through proteolysis by RT apoptotic caspases."; RL Immunity 31:84-98(2009). RN [16] RP PROTEOLYTIC PROCESSING. RX PubMed=19439663; DOI=10.1073/pnas.0812690106; RA Cayrol C., Girard J.P.; RT "The IL-1-like cytokine IL-33 is inactivated after maturation by RT caspase-1."; RL Proc. Natl. Acad. Sci. U.S.A. 106:9021-9026(2009). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21734074; DOI=10.4049/jimmunol.1003080; RA Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L., RA Martin M.U.; RT "The dual function cytokine IL-33 interacts with the transcription RT factor NF-kappaB to dampen NF-kappaB-stimulated gene transcription."; RL J. Immunol. 187:1609-1616(2011). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22215666; DOI=10.1074/jbc.M111.298703; RA Kakkar R., Hei H., Dobner S., Lee R.T.; RT "Interleukin 33 as a mechanically responsive cytokine secreted by RT living cells."; RL J. Biol. Chem. 287:6941-6948(2012). RN [19] RP PROTEOLYTIC PROCESSING. RX PubMed=22307629; DOI=10.1073/pnas.1115884109; RA Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., RA Monsarrat B., Girard J.P., Cayrol C.; RT "IL-33 is processed into mature bioactive forms by neutrophil elastase RT and cathepsin G."; RL Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012). RN [20] RP STRUCTURE BY NMR OF 111-270, INTERACTION WITH IL1RL1 AND IL1RAP, AND RP SUBUNIT. RX PubMed=19836339; DOI=10.1016/j.str.2009.08.009; RA Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C., RA Bazan J.F., Fairbrother W.J.; RT "Structure of IL-33 and its interaction with the ST2 and IL-1RAcP RT receptors--insight into heterotrimeric IL-1 signaling complexes."; RL Structure 17:1398-1410(2009). CC -!- FUNCTION: Cytokine that binds to and signals through IL1RL1/ST2 CC and its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, CC followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, CC MAPK14, and MAPK8. Induces T-helper type 2-associated cytokines. CC Acts as a chemoattractant tor Th2 cells, and may function as an CC "alarmin", that amplifies immune responses during tissue injury. CC -!- FUNCTION: In quiescent endothelia the uncleaved form is CC constitutively and abundantly expressed, and acts as a chromatin- CC associated nuclear factor with transcriptional repressor CC properties, it may sequester nuclear NF-kappaB/RELA, lowering CC expression of its targets. This form is rapidely lost upon CC angiogenic or proinflammatory activation. CC -!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary CC high-affinity receptor IL1RL1 and the coreceptor IL1RAP. CC -!- INTERACTION: CC P0C0S8:HIST1H2AM; NbExp=3; IntAct=EBI-724057, EBI-1390628; CC Q01638:IL1RL1; NbExp=2; IntAct=EBI-724057, EBI-993762; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Cytoplasmic vesicle, CC secretory vesicle. Secreted. Note=Associates with heterochromatin CC and mitotic chromosomes. Translocation from the nucleus occurs CC upon biomechanical strain, depends on an intact microtubule CC network, and is ATP-dependent. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O95760-1; Sequence=Displayed; CC Name=2; CC IsoId=O95760-2; Sequence=VSP_042728; CC Note=No experimental confirmation available; CC Name=3; Synonyms=spIL-33; CC IsoId=O95760-3; Sequence=VSP_044948; CC Note=Constitutively active; CC Name=4; CC IsoId=O95760-4; Sequence=VSP_045440; CC -!- TISSUE SPECIFICITY: Expressed at high level in high endothelial CC venules found in tonsils, Peyer patches and mesenteric lymph CC nodes. Almost undetectable in placenta. CC -!- DOMAIN: The homeodomain-like HTH domain mediates nuclear CC localization and heterochromatin association. CC -!- PTM: Proteolytically converted to a mature form by CASP1 in vitro CC and calpains in vivo. Caspase-mediated proteolysis, once thought CC to activate IL33, rather acts as a switch to dampen its activity. CC Cathepsin G and elastase can cleave IL33 and generate highly CC active forms in activated neutrophils (IL-33(95-270), IL-33(99- CC 270) and IL-33(109-270)). Proteolysis is not strictly required for CC biological activity. CC -!- SIMILARITY: Belongs to the IL-1 family. Highly divergent. 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; AB024518; BAA75892.1; -; mRNA. DR EMBL; AY905581; AAX86998.1; -; mRNA. DR EMBL; HQ641439; ADR77828.1; -; mRNA. DR EMBL; AK295908; BAG58697.1; -; mRNA. DR EMBL; AK303943; BAG64871.1; -; mRNA. DR EMBL; CR407619; CAG28547.1; -; mRNA. DR EMBL; AL353741; CAI16003.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58748.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58750.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58751.1; -; Genomic_DNA. DR EMBL; BC047085; AAH47085.1; -; mRNA. DR RefSeq; NP_001186569.1; NM_001199640.1. DR RefSeq; NP_001186570.1; NM_001199641.1. DR RefSeq; NP_254274.1; NM_033439.3. DR RefSeq; XP_005251683.1; XM_005251626.1. DR RefSeq; XP_005251684.1; XM_005251627.1. DR UniGene; Hs.731660; -. DR PDB; 2KLL; NMR; -; A=111-270. DR PDB; 4KC3; X-ray; 3.27 A; A=112-270. DR PDBsum; 2KLL; -. DR PDBsum; 4KC3; -. DR ProteinModelPortal; O95760; -. DR SMR; O95760; 111-270. DR IntAct; O95760; 4. DR MINT; MINT-1423224; -. DR STRING; 9606.ENSP00000370842; -. DR PhosphoSite; O95760; -. DR PaxDb; O95760; -. DR PRIDE; O95760; -. DR Ensembl; ENST00000381434; ENSP00000370842; ENSG00000137033. DR Ensembl; ENST00000417746; ENSP00000394039; ENSG00000137033. DR Ensembl; ENST00000456383; ENSP00000414238; ENSG00000137033. DR GeneID; 90865; -. DR KEGG; hsa:90865; -. DR UCSC; uc011lmh.2; human. DR CTD; 90865; -. DR GeneCards; GC09P006206; -. DR HGNC; HGNC:16028; IL33. DR HPA; CAB007057; -. DR HPA; HPA024426; -. DR MIM; 608678; gene. DR neXtProt; NX_O95760; -. DR PharmGKB; PA162392005; -. DR eggNOG; NOG41297; -. DR HOGENOM; HOG000070215; -. DR HOVERGEN; HBG081791; -. DR InParanoid; O95760; -. DR KO; K12967; -. DR OMA; DPGVFIG; -. DR OrthoDB; EOG7TQV1R; -. DR PhylomeDB; O95760; -. DR EvolutionaryTrace; O95760; -. DR GenomeRNAi; 90865; -. DR NextBio; 35499393; -. DR PRO; PR:O95760; -. DR Bgee; O95760; -. DR CleanEx; HS_IL33; -. DR Genevestigator; O95760; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL. DR GO; GO:0051025; P:negative regulation of immunoglobulin secretion; IEA:Ensembl. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl. DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl. DR GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:BHF-UCL. DR GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IEA:Ensembl. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL. DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl. DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl. DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL. DR GO; GO:0002830; P:positive regulation of type 2 immune response; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR InterPro; IPR026145; IL-33. DR PANTHER; PTHR21114; PTHR21114; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Complete proteome; KW Cytokine; Cytoplasmic vesicle; Nucleus; Polymorphism; KW Reference proteome; Secreted; Transcription. FT PROPEP 1 111 FT /FTId=PRO_0000248845. FT CHAIN 112 270 Interleukin-33. FT /FTId=PRO_0000096790. FT REGION 1 65 Homeodomain-like HTH domain. FT REGION 66 111 Interaction with RELA (By similarity). FT VAR_SEQ 31 157 KSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLK FT TGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSS FT ITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKD FT EKKD -> N (in isoform 4). FT /FTId=VSP_045440. FT VAR_SEQ 72 113 Missing (in isoform 3). FT /FTId=VSP_044948. FT VAR_SEQ 115 156 Missing (in isoform 2). FT /FTId=VSP_042728. FT VARIANT 263 263 I -> M (in dbSNP:rs16924241). FT /FTId=VAR_049576. FT STRAND 112 115 FT STRAND 119 127 FT TURN 129 131 FT STRAND 133 138 FT STRAND 140 148 FT STRAND 158 169 FT TURN 170 172 FT STRAND 180 189 FT STRAND 193 197 FT TURN 198 201 FT STRAND 202 206 FT HELIX 214 216 FT STRAND 218 224 FT STRAND 228 235 FT STRAND 238 243 FT STRAND 246 251 FT HELIX 261 263 FT STRAND 265 267 SQ SEQUENCE 270 AA; 30759 MW; 7C158069196EF636 CRC64; MKPKMKYSTN KISTAKWKNT ASKALCFKLG KSQQKAKEVC PMYFMKLRSG LMIKKEACYF RRETTKRPSL KTGRKHKRHL VLAACQQQST VECFAFGISG VQKYTRALHD SSITGISPIT EYLASLSTYN DQSITFALED ESYEIYVEDL KKDEKKDKVL LSYYESQHPS NESGDGVDGK MLMVTLSPTK DFWLHANNKE HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI GVKDNHLALI KVDSSENLCT ENILFKLSET //