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Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines (PubMed:17853410, PubMed:18836528). Also involved in activation of mast cells, basophils, eosinophils and natural killer cells (PubMed:17853410, PubMed:18836528). Acts as an enhancer of polarization of alternatively activated macrophages (PubMed:19841166). Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury (PubMed:17853410, PubMed:18836528). Induces rapid UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18787100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21734074"}],"value":"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 pro-inflammatory activation (PubMed:18787100)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19836339"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23980170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272059"}],"value":"Forms a 1:1:1 heterotrimeric complex with its primary high-affinity receptor IL1RL1 and the coreceptor IL1RAP (PubMed:19836339, PubMed:23980170). 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Associates with heterochromatin and mitotic chromosomes (PubMed:17185418). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12819012"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18787100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18836528"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21734074"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17185418"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272059"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22215666"}],"value":"Cytoplasmic vesicle, secretory vesicle","id":"SL-0244"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19465481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35794369"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["O95760-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["O95760-2"],"sequenceIds":["VSP_042728"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"synonyms":[{"value":"spIL-33"}],"isoformIds":["O95760-3"],"sequenceIds":["VSP_044948"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["O95760-4"],"sequenceIds":["VSP_045440"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12819012"}],"value":"Expressed at high level in high endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes. 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However, proteolytic processing by CELA1, CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal peptides that are more active than the unprocessed full length protein (PubMed:22307629, PubMed:35794369). May also be proteolytically processed by calpains (PubMed:19596270, PubMed:22307629). 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, PubMed:19439663) but could not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is probably not a direct substrate for that caspase (PubMed:19439663, PubMed:19465481)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Constitutively active"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the IL-1 family. 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