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Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]

 IL33_HUMAN              Reviewed;         270 AA.
O95760; B2R8L1; B4DJ35; B4E1Q9; D3DRI5; E7EAX4; Q2YEJ5;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Interleukin-33;
Short=IL-33;
AltName: Full=Interleukin-1 family member 11;
Short=IL-1F11;
AltName: Full=Nuclear factor from high endothelial venules;
Short=NF-HEV;
Contains:
RecName: Full=Interleukin-33 (95-270);
Contains:
RecName: Full=Interleukin-33 (99-270);
Contains:
RecName: Full=Interleukin-33 (109-270);
Flags: Precursor;
Name=IL33; Synonyms=C9orf26, IL1F11, NFHEV;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Endothelial cell;
PubMed=12819012; DOI=10.1016/S0002-9440(10)63631-0;
Baekkevold E.S., Roussigne M., Yamanaka T., Johansen F.-E.,
Jahnsen F.L., Amalric F., Brandtzaeg P., Erard M., Haraldsen G.,
Girard J.-P.;
"Molecular characterization of NF-HEV, a nuclear factor preferentially
expressed in human high endothelial venules.";
Am. J. Pathol. 163:69-79(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10566975; DOI=10.1097/00004647-199911000-00013;
Onda H., Kasuya H., Takakura K., Hori T., Imaizumi T., Takeuchi T.,
Inoue I., Takeda J.;
"Identification of genes differentially expressed in canine
vasospastic cerebral arteries after subarachnoid hemorrhage.";
J. Cereb. Blood Flow Metab. 19:1279-1288(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND PROTEOLYTIC
PROCESSING.
PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015;
Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K.,
Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F.,
Kastelein R.A.;
"IL-33, an interleukin-1-like cytokine that signals via the IL-1
receptor-related protein ST 2 and induces T helper type 2-associated
cytokines.";
Immunity 23:479-490(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=21454686; DOI=10.1074/jbc.M111.219089;
Hong J., Bae S., Jhun H., Lee S., Choi J., Kang T., Kwak A., Hong K.,
Kim E., Jo S., Kim S.;
"Identification of constitutively active interleukin 33 (IL-33) splice
variant.";
J. Biol. Chem. 286:20078-20086(2011).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Adrenal gland, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 95-121, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, PROTEOLYTIC PROCESSING, CLEAVAGE AT PHE-94 AND LEU-108 BY
CSTG, AND CLEAVAGE AT ILE-98 BY ELANE.
PubMed=22307629; DOI=10.1073/pnas.1115884109;
Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A.,
Monsarrat B., Girard J.P., Cayrol C.;
"IL-33 is processed into mature bioactive forms by neutrophil elastase
and cathepsin G.";
Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012).
[11]
FUNCTION.
PubMed=17853410; DOI=10.1002/eji.200737547;
Komai-Koma M., Xu D., Li Y., McKenzie A.N., McInnes I.B., Liew F.Y.;
"IL-33 is a chemoattractant for human Th2 cells.";
Eur. J. Immunol. 37:2779-2786(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR TARGETING DOMAIN.
PubMed=17185418; DOI=10.1073/pnas.0606854104;
Carriere V., Roussel L., Ortega N., Lacorre D.A., Americh L.,
Aguilar L., Bouche G., Girard J.P.;
"IL-33, the IL-1-like cytokine ligand for ST2 receptor, is a
chromatin-associated nuclear factor in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 104:282-287(2007).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18787100; DOI=10.2353/ajpath.2008.080014;
Kuchler A.M., Pollheimer J., Balogh J., Sponheim J., Manley L.,
Sorensen D.R., De Angelis P.M., Scott H., Haraldsen G.;
"Nuclear interleukin-33 is generally expressed in resting endothelium
but rapidly lost upon angiogenic or proinflammatory activation.";
Am. J. Pathol. 173:1229-1242(2008).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18836528; DOI=10.1371/journal.pone.0003331;
Moussion C., Ortega N., Girard J.P.;
"The IL-1-like cytokine IL-33 is constitutively expressed in the
nucleus of endothelial cells and epithelial cells in vivo: a novel
'alarmin'?";
PLoS ONE 3:E3331-E3331(2008).
[15]
PROTEOLYTIC PROCESSING.
PubMed=19596270; DOI=10.1016/j.bbrc.2009.07.018;
Hayakawa M., Hayakawa H., Matsuyama Y., Tamemoto H., Okazaki H.,
Tominaga S.;
"Mature interleukin-33 is produced by calpain-mediated cleavage in
vivo.";
Biochem. Biophys. Res. Commun. 387:218-222(2009).
[16]
PROTEOLYTIC PROCESSING.
PubMed=19559631; DOI=10.1016/j.immuni.2009.05.007;
Luthi A.U., Cullen S.P., McNeela E.A., Duriez P.J., Afonina I.S.,
Sheridan C., Brumatti G., Taylor R.C., Kersse K., Vandenabeele P.,
Lavelle E.C., Martin S.J.;
"Suppression of interleukin-33 bioactivity through proteolysis by
apoptotic caspases.";
Immunity 31:84-98(2009).
[17]
PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
PubMed=19465481; DOI=10.1074/jbc.M901744200;
Talabot-Ayer D., Lamacchia C., Gabay C., Palmer G.;
"Interleukin-33 is biologically active independently of caspase-1
cleavage.";
J. Biol. Chem. 284:19420-19426(2009).
[18]
PROTEOLYTIC PROCESSING.
PubMed=19439663; DOI=10.1073/pnas.0812690106;
Cayrol C., Girard J.P.;
"The IL-1-like cytokine IL-33 is inactivated after maturation by
caspase-1.";
Proc. Natl. Acad. Sci. U.S.A. 106:9021-9026(2009).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21734074; DOI=10.4049/jimmunol.1003080;
Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L.,
Martin M.U.;
"The dual function cytokine IL-33 interacts with the transcription
factor NF-kappaB to dampen NF-kappaB-stimulated gene transcription.";
J. Immunol. 187:1609-1616(2011).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22215666; DOI=10.1074/jbc.M111.298703;
Kakkar R., Hei H., Dobner S., Lee R.T.;
"Interleukin 33 as a mechanically responsive cytokine secreted by
living cells.";
J. Biol. Chem. 287:6941-6948(2012).
[21]
STRUCTURE BY NMR OF 111-270, INTERACTION WITH IL1RL1 AND IL1RAP, AND
SUBUNIT.
PubMed=19836339; DOI=10.1016/j.str.2009.08.009;
Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C.,
Bazan J.F., Fairbrother W.J.;
"Structure of IL-33 and its interaction with the ST2 and IL-1RAcP
receptors--insight into heterotrimeric IL-1 signaling complexes.";
Structure 17:1398-1410(2009).
[22]
X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 112-270 IN COMPLEX WITH
IL1RL1/ST2, AND MUTAGENESIS OF GLU-144; GLU-148; ASP-149; GLU-165 AND
ASP-244.
PubMed=23980170; DOI=10.1073/pnas.1308651110;
Liu X., Hammel M., He Y., Tainer J.A., Jeng U.S., Zhang L., Wang S.,
Wang X.;
"Structural insights into the interaction of IL-33 with its
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 110:14918-14923(2013).
-!- FUNCTION: Cytokine that binds to and signals through the
IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK
signaling pathways in target cells (PubMed:16286016). Involved in
the maturation of Th2 cells inducing the secretion of T-helper
type 2-associated cytokines. Also involved in activation of mast
cells, basophils, eosinophils and natural killer cells. Acts as a
chemoattractant for Th2 cells, and may function as an "alarmin",
that amplifies immune responses during tissue injury
(PubMed:17853410, PubMed:18836528). {ECO:0000269|PubMed:16286016,
ECO:0000269|PubMed:17853410, ECO:0000269|PubMed:18836528}.
-!- FUNCTION: In quiescent endothelia the uncleaved form is
constitutively and abundantly expressed, and acts as a chromatin-
associated nuclear factor with transcriptional repressor
properties, it may sequester nuclear NF-kappaB/RELA, lowering
expression of its targets (PubMed:21734074). This form is rapidely
lost upon angiogenic or proinflammatory activation
(PubMed:18787100). {ECO:0000269|PubMed:18787100,
ECO:0000269|PubMed:21734074}.
-!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary
high-affinity receptor IL1RL1 and the coreceptor IL1RAP.
{ECO:0000269|PubMed:19836339, ECO:0000269|PubMed:23980170}.
-!- INTERACTION:
P0C0S8:HIST1H2AM; NbExp=3; IntAct=EBI-724057, EBI-1390628;
Q01638:IL1RL1; NbExp=2; IntAct=EBI-724057, EBI-993762;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819012,
ECO:0000269|PubMed:17185418, ECO:0000269|PubMed:18787100,
ECO:0000269|PubMed:18836528, ECO:0000269|PubMed:21734074}.
Chromosome {ECO:0000269|PubMed:17185418}. Cytoplasmic vesicle,
secretory vesicle {ECO:0000269|PubMed:22215666}. Secreted
{ECO:0000269|PubMed:19465481}. Note=Associates with
heterochromatin and mitotic chromosomes (PubMed:17185418).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95760-1; Sequence=Displayed;
Name=2;
IsoId=O95760-2; Sequence=VSP_042728;
Note=No experimental confirmation available.;
Name=3; Synonyms=spIL-33;
IsoId=O95760-3; Sequence=VSP_044948;
Note=Constitutively active.;
Name=4;
IsoId=O95760-4; Sequence=VSP_045440;
-!- TISSUE SPECIFICITY: Expressed at high level in high endothelial
venules found in tonsils, Peyer patches and mesenteric lymph
nodes. Almost undetectable in placenta.
{ECO:0000269|PubMed:12819012}.
-!- DOMAIN: The homeodomain-like HTH domain mediates nuclear
localization and heterochromatin association.
-!- PTM: The full-length protein can be released from cells and is
able to signal via the IL1RL1/ST2 receptor. However, proteolytic
processing by CSTG/cathepsin G and ELANE/neutrophil elastase
produces C-terminal peptides that are more active than the
unprocessed full length protein. May also be proteolytically
processed by calpains (PubMed:19596270). Proteolytic cleavage
mediated by apoptotic caspases including CASP3 and CASP7 results
in IL33 inactivation (PubMed:19559631). In vitro proteolytic
cleavage by CASP1 was reported (PubMed:16286016) but could not be
confirmed in vivo (PubMed:19465481) suggesting that IL33 is
probably not a direct substrate for that caspase.
{ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:19439663,
ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:19559631,
ECO:0000269|PubMed:19596270, ECO:0000269|PubMed:22307629}.
-!- SIMILARITY: Belongs to the IL-1 family. Highly divergent.
{ECO:0000305}.
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EMBL; AB024518; BAA75892.1; -; mRNA.
EMBL; AY905581; AAX86998.1; -; mRNA.
EMBL; HQ641439; ADR77828.1; -; mRNA.
EMBL; AK295908; BAG58697.1; -; mRNA.
EMBL; AK303943; BAG64871.1; -; mRNA.
EMBL; AK313414; BAG36208.1; -; mRNA.
EMBL; CR407619; CAG28547.1; -; mRNA.
EMBL; AL353741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58748.1; -; Genomic_DNA.
EMBL; CH471071; EAW58750.1; -; Genomic_DNA.
EMBL; CH471071; EAW58751.1; -; Genomic_DNA.
EMBL; BC047085; AAH47085.1; -; mRNA.
CCDS; CCDS56563.1; -. [O95760-2]
CCDS; CCDS56564.1; -. [O95760-4]
CCDS; CCDS6468.1; -. [O95760-1]
CCDS; CCDS83341.1; -. [O95760-3]
RefSeq; NP_001186569.1; NM_001199640.1. [O95760-2]
RefSeq; NP_001186570.1; NM_001199641.1. [O95760-4]
RefSeq; NP_001300973.1; NM_001314044.1. [O95760-1]
RefSeq; NP_001300974.1; NM_001314045.1. [O95760-1]
RefSeq; NP_001300975.1; NM_001314046.1.
RefSeq; NP_001300976.1; NM_001314047.1.
RefSeq; NP_001300977.1; NM_001314048.1. [O95760-3]
RefSeq; NP_254274.1; NM_033439.3. [O95760-1]
UniGene; Hs.731660; -.
PDB; 2KLL; NMR; -; A=111-270.
PDB; 4KC3; X-ray; 3.27 A; A=112-270.
PDBsum; 2KLL; -.
PDBsum; 4KC3; -.
ProteinModelPortal; O95760; -.
SMR; O95760; -.
BioGrid; 124776; 7.
DIP; DIP-37862N; -.
IntAct; O95760; 6.
MINT; MINT-1423224; -.
STRING; 9606.ENSP00000370842; -.
iPTMnet; O95760; -.
PhosphoSitePlus; O95760; -.
BioMuta; IL33; -.
PaxDb; O95760; -.
PeptideAtlas; O95760; -.
PRIDE; O95760; -.
Ensembl; ENST00000381434; ENSP00000370842; ENSG00000137033. [O95760-1]
Ensembl; ENST00000417746; ENSP00000394039; ENSG00000137033. [O95760-4]
Ensembl; ENST00000456383; ENSP00000414238; ENSG00000137033. [O95760-2]
Ensembl; ENST00000611532; ENSP00000478858; ENSG00000137033. [O95760-3]
GeneID; 90865; -.
KEGG; hsa:90865; -.
UCSC; uc011lmh.3; human. [O95760-1]
CTD; 90865; -.
DisGeNET; 90865; -.
EuPathDB; HostDB:ENSG00000137033.11; -.
GeneCards; IL33; -.
HGNC; HGNC:16028; IL33.
HPA; CAB007057; -.
HPA; HPA024426; -.
HPA; HPA052386; -.
MIM; 608678; gene.
neXtProt; NX_O95760; -.
OpenTargets; ENSG00000137033; -.
PharmGKB; PA162392005; -.
eggNOG; ENOG410J11H; Eukaryota.
eggNOG; ENOG41118MB; LUCA.
GeneTree; ENSGT00390000005185; -.
HOGENOM; HOG000070215; -.
HOVERGEN; HBG081791; -.
InParanoid; O95760; -.
KO; K12967; -.
OMA; DFWLHAN; -.
OrthoDB; EOG091G0F5I; -.
PhylomeDB; O95760; -.
TreeFam; TF338120; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-9014843; Interleukin-33 signaling.
EvolutionaryTrace; O95760; -.
GenomeRNAi; 90865; -.
PRO; PR:O95760; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000137033; -.
CleanEx; HS_IL33; -.
Genevisible; O95760; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0002282; P:microglial cell activation involved in immune response; IEA:Ensembl.
GO; GO:0061518; P:microglial cell proliferation; IEA:Ensembl.
GO; GO:0051025; P:negative regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:BHF-UCL.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0002830; P:positive regulation of type 2 immune response; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0042092; P:type 2 immune response; IBA:GO_Central.
InterPro; IPR026145; IL-33.
PANTHER; PTHR21114; PTHR21114; 1.
Pfam; PF15095; IL33; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
Cytokine; Cytoplasmic vesicle; Direct protein sequencing; Nucleus;
Polymorphism; Reference proteome; Secreted; Transcription.
CHAIN 1 270 Interleukin-33.
/FTId=PRO_0000096790.
PROPEP 1 94 {ECO:0000269|PubMed:22307629}.
/FTId=PRO_0000430083.
CHAIN 95 270 Interleukin-33 (95-270).
/FTId=PRO_0000430084.
CHAIN 99 270 Interleukin-33 (99-270).
/FTId=PRO_0000430085.
CHAIN 109 270 Interleukin-33 (109-270).
/FTId=PRO_0000430086.
REGION 1 65 Homeodomain-like HTH domain.
REGION 66 111 Interaction with RELA. {ECO:0000250}.
SITE 94 95 Cleavage; by CTSG.
SITE 98 99 Cleavage; by ELANE.
SITE 108 109 Cleavage; by CTSG.
VAR_SEQ 31 157 KSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLK
TGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSS
ITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKD
EKKD -> N (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045440.
VAR_SEQ 72 113 Missing (in isoform 3).
{ECO:0000303|PubMed:21454686}.
/FTId=VSP_044948.
VAR_SEQ 115 156 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042728.
VARIANT 263 263 I -> M (in dbSNP:rs16924241).
/FTId=VAR_049576.
MUTAGEN 144 144 E->K: Decreases affinity for IL1RL1.
{ECO:0000269|PubMed:23980170}.
MUTAGEN 148 148 E->K: 7-fold decrease in affinity for
IL1RL1. {ECO:0000269|PubMed:23980170}.
MUTAGEN 149 149 D->K: Almost abolishes binding to IL1RL1.
{ECO:0000269|PubMed:23980170}.
MUTAGEN 165 165 E->K: 8-fold decrease in affinity for
IL1RL1. {ECO:0000269|PubMed:23980170}.
MUTAGEN 244 244 D->K: Decreases affinity for IL1RL1.
{ECO:0000269|PubMed:23980170}.
CONFLICT 139 139 E -> G (in Ref. 5; BAG36208).
{ECO:0000305}.
STRAND 112 115 {ECO:0000244|PDB:2KLL}.
STRAND 119 127 {ECO:0000244|PDB:4KC3}.
TURN 129 131 {ECO:0000244|PDB:2KLL}.
STRAND 133 138 {ECO:0000244|PDB:4KC3}.
STRAND 140 148 {ECO:0000244|PDB:4KC3}.
STRAND 158 169 {ECO:0000244|PDB:4KC3}.
TURN 170 172 {ECO:0000244|PDB:2KLL}.
STRAND 180 189 {ECO:0000244|PDB:4KC3}.
STRAND 193 197 {ECO:0000244|PDB:4KC3}.
TURN 198 201 {ECO:0000244|PDB:4KC3}.
STRAND 202 206 {ECO:0000244|PDB:4KC3}.
HELIX 214 216 {ECO:0000244|PDB:4KC3}.
STRAND 218 224 {ECO:0000244|PDB:4KC3}.
STRAND 228 235 {ECO:0000244|PDB:4KC3}.
STRAND 238 243 {ECO:0000244|PDB:4KC3}.
STRAND 246 251 {ECO:0000244|PDB:4KC3}.
HELIX 261 263 {ECO:0000244|PDB:2KLL}.
STRAND 265 267 {ECO:0000244|PDB:4KC3}.
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


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