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Human IL-33  Protein

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Expression host: E. coli  
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IL-33 Summary & Protein Information

IL-33 Related Information

IL-33 Background

Gene Summary: IL-33 (MIM 608678) is a member of the IL1 (see MIM 147760) family that potently drives production of T helper-2 (Th2)-associated cytokines (e.g., IL4; MIM 147780). IL-33 is a ligand for IL-33R (IL1RL1; MIM 601203), an IL1 family receptor that is selectively expressed on Th2 cells and mast cells (summary by Yagami et al., 2010 [PubMed 20926795]).
General information above from NCBI
Subunit structure: 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}.
Domain: The homeodomain-like HTH domain mediates nuclear localization and heterochromatin association.
Subcellular location: Nucleus. Chromosome. Cytoplasmic vesicle, secretory vesicle. Secreted. Note=Associates with heterochromatin and mitotic chromosomes. Translocation from the nucleus occurs upon biomechanical strain, depends on an intact microtubule network, and is ATP-dependent.
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}.
Post-translational: 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}.
Sequence similarity: Belongs to the IL-1 family. Highly divergent. {ECO:0000305}.
General information above from UniProt

Interleukin 33 (IL-33), also known as DVS27 or NF-HEV (Nuclear Factor from High Endothelial enules), is a proinflammatory protein and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 protein is expressed highly and rather selectively by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyers's patches, and lymph nodes. IL-33 protein has transcriptional regulatory properties, and the researches suggested that IL-33 is a dual-function protein that might act both as a cytokine and as an intracellular nuclear factor. As a type 2 cytokines, IL-33 protein also play a pivotal role in helminthic infection and allergic disorders.

IL-33 Alternative Name

DVS27,IL1F11,NF-HEV,NFEHEV,C9orf26, [homo-sapiens]
C9orf26,DKFZp586H0523,DVS27,IL33,IL-33,NFEHEV,NF-HEV,RP11-575C20.2, [human]
Il-33,Il1f11,NF-HEV,9230117N10Rik, [mus-musculus]

IL-33 Related Studies

  • Iikura M, et al. (2007) IL-33 can promote survival, adhesion and cytokine production in human mast cells. Lab Invest. 87(10): 971-8.
  • Lamkanfi M, et al. (2009) IL-33 raises alarm. Immunity. 31(1): 5-7.