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Interleukin-33 (IL-33) [Cleaved into: Interleukin-33(102-266); Interleukin-33(109-266)]

 IL33_MOUSE              Reviewed;         266 AA.
Q8BVZ5; Q2YEJ4; Q3TQN0; Q99L46;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
22-NOV-2017, entry version 108.
RecName: Full=Interleukin-33;
Short=IL-33;
Contains:
RecName: Full=Interleukin-33(102-266);
Contains:
RecName: Full=Interleukin-33(109-266);
Flags: Precursor;
Name=Il33;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=BALB/cJ;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Gastric mucosa;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[4]
FUNCTION, 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).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NF-KAPPAB/RELA.
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).
[6]
PROTEOLYTIC PROCESSING, CLEAVAGE AT PHE-101 BY CSTG AND ELANE, AND
CLEAVAGE AT LEU-108 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).
-!- 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. 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.
-!- 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. This form is rapidely lost upon
angiogenic or proinflammatory activation.
-!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary
high-affinity receptor IL1RL1 and the coreceptor IL1RAP.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465481}.
Chromosome {ECO:0000250|UniProtKB:O95760}. Cytoplasmic vesicle,
secretory vesicle {ECO:0000250|UniProtKB:O95760}. Secreted
{ECO:0000269|PubMed:19465481}. Note=Associates with
heterochromatin and mitotic chromosomes.
{ECO:0000250|UniProtKB:O95760}.
-!- DOMAIN: The homeodomain-like HTH domain mediates nuclear
localization and heterochromatin association. {ECO:0000250}.
-!- 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. 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. {ECO:0000269|PubMed:16286016,
ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:22307629}.
-!- 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.
-!- SIMILARITY: Belongs to the IL-1 family. Highly divergent.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY905582; AAX86999.1; -; mRNA.
EMBL; AK075849; BAC36003.1; -; mRNA.
EMBL; AK163464; BAE37352.1; -; mRNA.
EMBL; BC003847; AAH03847.1; -; mRNA.
CCDS; CCDS29740.1; -.
RefSeq; NP_001158196.1; NM_001164724.1.
RefSeq; NP_598536.2; NM_133775.2.
RefSeq; XP_006527526.1; XM_006527463.3.
RefSeq; XP_011245701.1; XM_011247399.2.
UniGene; Mm.182359; -.
PDB; 5VI4; X-ray; 2.79 A; A/D=109-266.
PDBsum; 5VI4; -.
ProteinModelPortal; Q8BVZ5; -.
SMR; Q8BVZ5; -.
BioGrid; 218533; 1.
IntAct; Q8BVZ5; 1.
STRING; 10090.ENSMUSP00000025724; -.
iPTMnet; Q8BVZ5; -.
PhosphoSitePlus; Q8BVZ5; -.
MaxQB; Q8BVZ5; -.
PaxDb; Q8BVZ5; -.
PRIDE; Q8BVZ5; -.
Ensembl; ENSMUST00000025724; ENSMUSP00000025724; ENSMUSG00000024810.
Ensembl; ENSMUST00000120388; ENSMUSP00000113829; ENSMUSG00000024810.
GeneID; 77125; -.
KEGG; mmu:77125; -.
UCSC; uc008hec.2; mouse.
CTD; 90865; -.
MGI; MGI:1924375; Il33.
eggNOG; ENOG410J11H; Eukaryota.
eggNOG; ENOG41118MB; LUCA.
GeneTree; ENSGT00390000005185; -.
HOGENOM; HOG000070215; -.
HOVERGEN; HBG081791; -.
InParanoid; Q8BVZ5; -.
KO; K12967; -.
OMA; DFWLHAN; -.
OrthoDB; EOG091G0F5I; -.
PhylomeDB; Q8BVZ5; -.
TreeFam; TF338120; -.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-9014843; Interleukin-33 signaling.
PRO; PR:Q8BVZ5; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024810; -.
CleanEx; MM_IL33; -.
ExpressionAtlas; Q8BVZ5; baseline and differential.
Genevisible; Q8BVZ5; MM.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
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; IDA:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:0002281; P:macrophage activation involved in immune response; IDA:UniProtKB.
GO; GO:0002282; P:microglial cell activation involved in immune response; IDA:UniProtKB.
GO; GO:0061518; P:microglial cell proliferation; IDA:UniProtKB.
GO; GO:0051025; P:negative regulation of immunoglobulin secretion; IGI:BHF-UCL.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IGI:BHF-UCL.
GO; GO:0002686; P:negative regulation of leukocyte migration; IGI:BHF-UCL.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IGI:BHF-UCL.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IGI:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IGI:BHF-UCL.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IGI:BHF-UCL.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IGI:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:BHF-UCL.
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; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0002830; P:positive regulation of type 2 immune response; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026145; IL-33.
PANTHER; PTHR21114; PTHR21114; 1.
Pfam; PF15095; IL33; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome; Cytokine;
Cytoplasmic vesicle; Nucleus; Reference proteome; Secreted;
Transcription.
CHAIN 1 266 Interleukin-33.
/FTId=PRO_0000096791.
PROPEP 1 101 {ECO:0000305}.
/FTId=PRO_0000430087.
CHAIN 102 266 Interleukin-33(102-266). {ECO:0000305}.
/FTId=PRO_0000430088.
CHAIN 109 266 Interleukin-33(109-266). {ECO:0000305}.
/FTId=PRO_0000430089.
REGION 1 65 Homeodomain-like HTH domain.
{ECO:0000250}.
REGION 66 108 Interaction with RELA.
SITE 101 102 Cleavage; by CTSG and ELANE.
{ECO:0000305}.
SITE 108 109 Cleavage; by ELANE. {ECO:0000305}.
CONFLICT 24 25 AL -> RS (in Ref. 1; AAX86999).
{ECO:0000305}.
CONFLICT 179 179 L -> V (in Ref. 3; AAH03847).
{ECO:0000305}.
CONFLICT 185 185 P -> S (in Ref. 1; AAX86999).
{ECO:0000305}.
SEQUENCE 266 AA; 29991 MW; E03C2C297EB43E23 CRC64;
MRPRMKYSNS KISPAKFSST AGEALVPPCK IRRSQQKTKE FCHVYCMRLR SGLTIRKETS
YFRKEPTKRY SLKSGTKHEE NFSAYPRDSR KRSLLGSIQA FAASVDTLSI QGTSLLTQSP
ASLSTYNDQS VSFVLENGCY VINVDDSGKD QEQDQVLLRY YESPCPASQS GDGVDGKKLM
VNMSPIKDTD IWLHANDKDY SVELQRGDVS PPEQAFFVLH KKSSDFVSFE CKNLPGTYIG
VKDNQLALVE EKDESCNNIM FKLSKI


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