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Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1)

 IL36A_MOUSE             Reviewed;         160 AA.
Q9JLA2;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 119.
RecName: Full=Interleukin-36 alpha;
AltName: Full=FIL1 epsilon;
AltName: Full=Interleukin-1 epsilon;
Short=IL-1 epsilon;
AltName: Full=Interleukin-1 family member 6;
Short=IL-1F6;
AltName: Full=Interleukin-1 homolog 1;
Short=IL-1H1;
Flags: Precursor;
Name=Il36a; Synonyms=Fil1e, Il1e, Il1f6, Il1h1;
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].
PubMed=10744718; DOI=10.1074/jbc.275.14.10308;
Kumar S., McDonnell P.C., Lehr R., Tierney L., Tzimas M.N.,
Griswold D.E., Capper E.A., Tal-Singer R., Wells G.I., Doyle M.L.,
Young P.R.;
"Identification and initial characterization of four novel members of
the interleukin-1 family.";
J. Biol. Chem. 275:10308-10314(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11466363; DOI=10.4049/jimmunol.167.3.1440;
Debets R., Timans J.C., Homey B., Zurawski S., Sana T.R., Lo S.,
Wagner J., Edwards G., Clifford T., Menon S., Bazan J.F.,
Kastelein R.A.;
"Two novel IL-1 family members, IL-1 delta and IL-1 epsilon, function
as an antagonist and agonist of NF-kappa B activation through the
orphan IL-1 receptor-related protein 2.";
J. Immunol. 167:1440-1446(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[4]
TISSUE SPECIFICITY.
PubMed=20101239; DOI=10.1038/labinvest.2009.148;
Ichii O., Otsuka S., Sasaki N., Yabuki A., Ohta H., Takiguchi M.,
Hashimoto Y., Endoh D., Kon Y.;
"Local overexpression of interleukin-1 family, member 6 relates to the
development of tubulointerstitial lesions.";
Lab. Invest. 90:459-475(2010).
[5]
FUNCTION.
PubMed=21860022; DOI=10.1182/blood-2011-05-356873;
Vigne S., Palmer G., Lamacchia C., Martin P., Talabot-Ayer D.,
Rodriguez E., Ronchi F., Sallusto F., Dinh H., Sims J.E., Gabay C.;
"IL-36R ligands are potent regulators of dendritic and T cells.";
Blood 118:5813-5823(2011).
[6]
FUNCTION, AND PROCESSING.
PubMed=21965679; DOI=10.1074/jbc.M111.267922;
Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M.,
Gabel C.A., Sims J.E.;
"Interleukin-36 (IL-36) ligands require processing for full agonist
(IL-36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra)
activity.";
J. Biol. Chem. 286:42594-42602(2011).
[7]
INDUCTION.
PubMed=21881584; DOI=10.1038/jid.2011.234;
Carrier Y., Ma H.L., Ramon H.E., Napierata L., Small C., O'Toole M.,
Young D.A., Fouser L.A., Nickerson-Nutter C., Collins M.,
Dunussi-Joannopoulos K., Medley Q.G.;
"Inter-regulation of Th17 cytokines and the IL-36 cytokines in vitro
and in vivo: implications in psoriasis pathogenesis.";
J. Invest. Dermatol. 131:2428-2437(2011).
[8]
FUNCTION.
PubMed=23029241; DOI=10.1371/journal.pone.0045784;
Ramadas R.A., Ewart S.L., Iwakura Y., Medoff B.D., LeVine A.M.;
"IL-36alpha exerts pro-inflammatory effects in the lungs of mice.";
PLoS ONE 7:E45784-E45784(2012).
[9]
FUNCTION.
PubMed=24829417; DOI=10.4049/jimmunol.1301481;
Foster A.M., Baliwag J., Chen C.S., Guzman A.M., Stoll S.W.,
Gudjonsson J.E., Ward N.L., Johnston A.;
"IL-36 promotes myeloid cell infiltration, activation, and
inflammatory activity in skin.";
J. Immunol. 192:6053-6061(2014).
-!- FUNCTION: Cytokine that binds to and signals through the
IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK
signaling pathways in target cells linked to a pro-inflammatory
response. Part of the IL-36 signaling system that is thought to be
present in epithelial barriers and to take part in local
inflammatory response; similar to the IL-1 system with which it
shares the coreceptor IL1RAP. Seems to be involved in skin
inflammatory response by acting on keratinocytes, dendritic cells
and indirectly on T-cells to drive tissue infiltration, cell
maturation and cell proliferation. Induces the production of
proinflammatory cytokines, including IL-12, Il-1 beta, IL-6, TNF-
alpha and IL-23 in bone marrow-derived dendritic cells (BMDCs).
Involved in dendritic cell maturation by stimulating the surface
expression of CD80, CD86 and MHC class II. Induces the production
of IFN-gamma, IL-4 and IL-17 by cultured CD4(+) T-cells and
splenocytes. May play a role in proinflammatory effects in the
lung: induces the expression of CXCL1 and CXCL2 in the lung, and
the expression of TNF-alpha, IL-36c, IL-1A, IL-1B, CXCL1 and CXCL2
in isolated splenic CD11c(+) alveolar macrophages. May be involved
in T-cell maturation by stimulating the surface expression of CD40
and modestly CD80 and CD86 in splenic CD11c(+) cells. May be
involved in CD4(+) T-cell proliferation. Induces NF-kappa B
activation in macrophages. {ECO:0000269|PubMed:21860022,
ECO:0000269|PubMed:21965679, ECO:0000269|PubMed:23029241,
ECO:0000269|PubMed:24829417}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in embryonic tissue and in
tissues containing epithelial cells. Elevated expression levels
are detected in chronic kidney disease; expressed inepithelia from
the distal convoluted tubules (DCTs) to the cortical collecting
ducts (CCDs) in single nephrons (at protein level).
{ECO:0000269|PubMed:11466363, ECO:0000269|PubMed:20101239}.
-!- INDUCTION: By IL-22 in normal and psoriasis-like skin.
{ECO:0000269|PubMed:21881584}.
-!- PTM: N-terminal truncation leads to a dramatic enhancement of its
activity (>1000-fold). {ECO:0000269|PubMed:21965679}.
-!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF200493; AAF69249.1; -; mRNA.
EMBL; AF206697; AAG35671.1; -; mRNA.
EMBL; AK004061; BAB23147.1; -; mRNA.
CCDS; CCDS15734.1; -.
RefSeq; NP_062323.1; NM_019450.3.
UniGene; Mm.133095; -.
ProteinModelPortal; Q9JLA2; -.
SMR; Q9JLA2; -.
STRING; 10090.ENSMUSP00000028361; -.
PhosphoSitePlus; Q9JLA2; -.
PaxDb; Q9JLA2; -.
PRIDE; Q9JLA2; -.
Ensembl; ENSMUST00000028361; ENSMUSP00000028361; ENSMUSG00000026984.
GeneID; 54448; -.
KEGG; mmu:54448; -.
UCSC; uc008ioq.1; mouse.
CTD; 54448; -.
MGI; MGI:1859324; Il1f6.
eggNOG; ENOG410JBMR; Eukaryota.
eggNOG; ENOG41118FS; LUCA.
GeneTree; ENSGT00900000141014; -.
HOVERGEN; HBG052100; -.
InParanoid; Q9JLA2; -.
KO; K05484; -.
OMA; PGWFIAV; -.
OrthoDB; EOG091G0V8E; -.
PhylomeDB; Q9JLA2; -.
TreeFam; TF300203; -.
Reactome; R-MMU-9014826; Interleukin-36 pathway.
PRO; PR:Q9JLA2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026984; -.
CleanEx; MM_IL1F6; -.
ExpressionAtlas; Q9JLA2; baseline and differential.
Genevisible; Q9JLA2; MM.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005125; F:cytokine activity; IGI:MGI.
GO; GO:0005149; F:interleukin-1 receptor binding; ISS:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; TAS:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:MGI.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR003297; IL-1RA/IL-36.
InterPro; IPR027163; IL-36_alpha.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR10078:SF25; PTHR10078:SF25; 1.
Pfam; PF00340; IL1; 1.
PRINTS; PR01360; INTRLEUKIN1X.
SUPFAM; SSF50353; SSF50353; 1.
1: Evidence at protein level;
Complete proteome; Cytokine; Immunity; Inflammatory response;
Innate immunity; Nitration; Reference proteome; Secreted.
PROPEP 1 7 {ECO:0000269|PubMed:21965679}.
/FTId=PRO_0000430546.
CHAIN 8 160 Interleukin-36 alpha.
/FTId=PRO_0000153645.
MOD_RES 98 98 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q9UHA7}.
SEQUENCE 160 AA; 18015 MW; AA0434D68FF62F4A CRC64;
MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN
RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF
ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH


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