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Q8BVZ5

- IL33_MOUSE

UniProt

Q8BVZ5 - IL33_MOUSE

Protein

Interleukin-33

Gene

Il33

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    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. 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.
    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. This form is rapidely lost upon angiogenic or proinflammatory activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei101 – 1022Cleavage; by CTSG and ELANECurated
    Sitei108 – 1092Cleavage; by ELANECurated

    GO - Molecular functioni

    1. cytokine activity Source: BHF-UCL

    GO - Biological processi

    1. extrinsic apoptotic signaling pathway Source: MGI
    2. negative regulation of immunoglobulin secretion Source: BHF-UCL
    3. negative regulation of interferon-gamma production Source: BHF-UCL
    4. negative regulation of leukocyte migration Source: BHF-UCL
    5. negative regulation of T-helper 1 type immune response Source: BHF-UCL
    6. positive regulation of chemokine secretion Source: BHF-UCL
    7. positive regulation of gene expression Source: MGI
    8. positive regulation of immunoglobulin secretion Source: BHF-UCL
    9. positive regulation of inflammatory response Source: BHF-UCL
    10. positive regulation of interleukin-13 production Source: BHF-UCL
    11. positive regulation of interleukin-4 production Source: BHF-UCL
    12. positive regulation of interleukin-5 production Source: BHF-UCL
    13. positive regulation of interleukin-6 production Source: BHF-UCL
    14. positive regulation of macrophage activation Source: BHF-UCL
    15. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
    16. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    17. positive regulation of type 2 immune response Source: BHF-UCL
    18. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Transcription

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-33
    Short name:
    IL-33
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Il33
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1924375. Il33.

    Subcellular locationi

    Nucleus. Chromosome. Cytoplasmic vesiclesecretory vesicle By similarity. 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 By similarity.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. extracellular space Source: UniProtKB-KW
    3. nucleus Source: MGI
    4. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasmic vesicle, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Interleukin-33PRO_0000096791Add
    BLAST
    Propeptidei1 – 101101CuratedPRO_0000430087Add
    BLAST
    Chaini102 – 266165Interleukin-33(102-266)CuratedPRO_0000430088Add
    BLAST
    Chaini109 – 266158Interleukin-33(109-266)CuratedPRO_0000430089Add
    BLAST

    Post-translational modificationi

    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. Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation. 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.3 Publications

    Proteomic databases

    PRIDEiQ8BVZ5.

    PTM databases

    PhosphoSiteiQ8BVZ5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BVZ5.
    BgeeiQ8BVZ5.
    CleanExiMM_IL33.
    GenevestigatoriQ8BVZ5.

    Interactioni

    Subunit structurei

    Forms a 1:1:1 heterotrimeric complex with its primary high-affinity receptor IL1RL1 and the coreceptor IL1RAP.By similarity

    Protein-protein interaction databases

    BioGridi218533. 1 interaction.
    IntActiQ8BVZ5. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BVZ5.
    SMRiQ8BVZ5. Positions 109-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6565Homeodomain-like HTH domainBy similarityAdd
    BLAST
    Regioni66 – 10843Interaction with RELAAdd
    BLAST

    Domaini

    The homeodomain-like HTH domain mediates nuclear localization and heterochromatin association.By similarity

    Sequence similaritiesi

    Belongs to the IL-1 family. Highly divergent.Curated

    Phylogenomic databases

    eggNOGiNOG41297.
    GeneTreeiENSGT00390000005185.
    HOGENOMiHOG000070215.
    HOVERGENiHBG081791.
    InParanoidiQ8BVZ5.
    KOiK12967.
    OMAiDPGVFIG.
    OrthoDBiEOG7TQV1R.
    PhylomeDBiQ8BVZ5.
    TreeFamiTF338120.

    Family and domain databases

    InterProiIPR026145. IL-33.
    [Graphical view]
    PANTHERiPTHR21114. PTHR21114. 1 hit.
    PfamiPF15095. IL33. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8BVZ5-1 [UniParc]FASTAAdd to Basket

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    MRPRMKYSNS KISPAKFSST AGEALVPPCK IRRSQQKTKE FCHVYCMRLR    50
    SGLTIRKETS YFRKEPTKRY SLKSGTKHEE NFSAYPRDSR KRSLLGSIQA 100
    FAASVDTLSI QGTSLLTQSP ASLSTYNDQS VSFVLENGCY VINVDDSGKD 150
    QEQDQVLLRY YESPCPASQS GDGVDGKKLM VNMSPIKDTD IWLHANDKDY 200
    SVELQRGDVS PPEQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE 250
    EKDESCNNIM FKLSKI 266
    Length:266
    Mass (Da):29,991
    Last modified:March 1, 2003 - v1
    Checksum:iE03C2C297EB43E23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 252AL → RS in AAX86999. (PubMed:16286016)Curated
    Sequence conflicti179 – 1791L → V in AAH03847. (PubMed:15489334)Curated
    Sequence conflicti185 – 1851P → S in AAX86999. (PubMed:16286016)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY905582 mRNA. Translation: AAX86999.1.
    AK075849 mRNA. Translation: BAC36003.1.
    AK163464 mRNA. Translation: BAE37352.1.
    BC003847 mRNA. Translation: AAH03847.1.
    CCDSiCCDS29740.1.
    RefSeqiNP_001158196.1. NM_001164724.1.
    NP_598536.2. NM_133775.2.
    XP_006527526.1. XM_006527463.1.
    UniGeneiMm.182359.

    Genome annotation databases

    EnsembliENSMUST00000025724; ENSMUSP00000025724; ENSMUSG00000024810.
    ENSMUST00000120388; ENSMUSP00000113829; ENSMUSG00000024810.
    GeneIDi77125.
    KEGGimmu:77125.
    UCSCiuc008hec.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY905582 mRNA. Translation: AAX86999.1 .
    AK075849 mRNA. Translation: BAC36003.1 .
    AK163464 mRNA. Translation: BAE37352.1 .
    BC003847 mRNA. Translation: AAH03847.1 .
    CCDSi CCDS29740.1.
    RefSeqi NP_001158196.1. NM_001164724.1.
    NP_598536.2. NM_133775.2.
    XP_006527526.1. XM_006527463.1.
    UniGenei Mm.182359.

    3D structure databases

    ProteinModelPortali Q8BVZ5.
    SMRi Q8BVZ5. Positions 109-265.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 218533. 1 interaction.
    IntActi Q8BVZ5. 1 interaction.

    PTM databases

    PhosphoSitei Q8BVZ5.

    Proteomic databases

    PRIDEi Q8BVZ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025724 ; ENSMUSP00000025724 ; ENSMUSG00000024810 .
    ENSMUST00000120388 ; ENSMUSP00000113829 ; ENSMUSG00000024810 .
    GeneIDi 77125.
    KEGGi mmu:77125.
    UCSCi uc008hec.2. mouse.

    Organism-specific databases

    CTDi 90865.
    MGIi MGI:1924375. Il33.

    Phylogenomic databases

    eggNOGi NOG41297.
    GeneTreei ENSGT00390000005185.
    HOGENOMi HOG000070215.
    HOVERGENi HBG081791.
    InParanoidi Q8BVZ5.
    KOi K12967.
    OMAi DPGVFIG.
    OrthoDBi EOG7TQV1R.
    PhylomeDBi Q8BVZ5.
    TreeFami TF338120.

    Miscellaneous databases

    NextBioi 346526.
    PROi Q8BVZ5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BVZ5.
    Bgeei Q8BVZ5.
    CleanExi MM_IL33.
    Genevestigatori Q8BVZ5.

    Family and domain databases

    InterProi IPR026145. IL-33.
    [Graphical view ]
    PANTHERi PTHR21114. PTHR21114. 1 hit.
    Pfami PF15095. IL33. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      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.
      Immunity 23:479-490(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: BALB/c.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina and Gastric mucosa.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. "Interleukin-33 is biologically active independently of caspase-1 cleavage."
      Talabot-Ayer D., Lamacchia C., Gabay C., Palmer G.
      J. Biol. Chem. 284:19420-19426(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
    5. "The dual function cytokine IL-33 interacts with the transcription factor NF-kappaB to dampen NF-kappaB-stimulated gene transcription."
      Ali S., Mohs A., Thomas M., Klare J., Ross R., Schmitz M.L., Martin M.U.
      J. Immunol. 187:1609-1616(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NF-KAPPAB/RELA.
    6. "IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G."
      Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B., Girard J.P., Cayrol C.
      Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, CLEAVAGE AT PHE-101 BY CSTG AND ELANE, CLEAVAGE AT LEU-108 BY ELANE.

    Entry informationi

    Entry nameiIL33_MOUSE
    AccessioniPrimary (citable) accession number: Q8BVZ5
    Secondary accession number(s): Q2YEJ4, Q3TQN0, Q99L46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Intraperitoneal injections of IL-33 induce the expression of IL-4, IL-5, and IL-13 and lead to severe pathological changes in mucosal organs.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3