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Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)

 I36RA_MOUSE             Reviewed;         156 AA.
Q9QYY1; Q9JIG2;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
08-NOV-2002, sequence version 2.
22-NOV-2017, entry version 131.
RecName: Full=Interleukin-36 receptor antagonist protein;
Short=IL-36Ra {ECO:0000303|PubMed:21965679};
AltName: Full=Interleukin-1 HY1;
Short=IL-1HY1;
AltName: Full=Interleukin-1 delta;
Short=IL-1 delta;
AltName: Full=Interleukin-1 family member 5;
Short=IL-1F5;
AltName: Full=Interleukin-1 homolog 3;
Short=IL-1H3;
AltName: Full=Interleukin-1-like protein 1;
Short=IL-1L1;
Name=IL36RN; Synonyms=Fil1d, Il1f5, Il1h3, Il1hy1;
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=11093146;
DOI=10.1002/1521-4141(200011)30:11<3299::AID-IMMU3299>3.0.CO;2-S;
Barton J.L., Herbst R., Bosisio D., Higgins L., Nicklin M.J.H.;
"A tissue specific IL-1 receptor antagonist homolog from the IL-1
cluster lacks IL-1, IL-1ra, IL-18 and IL-18 antagonist activities.";
Eur. J. Immunol. 30:3299-3308(2000).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Stomach, and Tongue;
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).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17908936; DOI=10.1084/jem.20070157;
Blumberg H., Dinh H., Trueblood E.S., Pretorius J., Kugler D.,
Weng N., Kanaly S.T., Towne J.E., Willis C.R., Kuechle M.K.,
Sims J.E., Peschon J.J.;
"Opposing activities of two novel members of the IL-1 ligand family
regulate skin inflammation.";
J. Exp. Med. 204:2603-2614(2007).
[6]
FUNCTION.
PubMed=18284608; DOI=10.1111/j.1471-4159.2008.05304.x;
Costelloe C., Watson M., Murphy A., McQuillan K., Loscher C.,
Armstrong M.E., Garlanda C., Mantovani A., O'Neill L.A., Mills K.H.,
Lynch M.A.;
"IL-1F5 mediates anti-inflammatory activity in the brain through
induction of IL-4 following interaction with SIGIRR/TIR8.";
J. Neurochem. 105:1960-1969(2008).
[7]
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).
[8]
FUNCTION, AND CLEAVAGE OF INITIATOR METHIONINE.
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3-156, AND DISULFIDE BOND.
PubMed=12974628; DOI=10.1021/bi0341197;
Dunn E.F., Gay N.J., Bristow A.F., Gearing D.P., O'Neill L.A.J.,
Pei X.Y.;
"High-resolution structure of murine interleukin 1 homologue IL-1F5
reveals unique loop conformations for receptor binding specificity.";
Biochemistry 42:10938-10944(2003).
-!- FUNCTION: Inhibits the activity of interleukin-36 (IL36A,IL36B and
IL36G) by binding to receptor IL1RL2/IL-36R and preventing its
association with the coreceptor IL1RAP for signaling. 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. Proposed
to play a role in skin inflammation. May be involved in the innate
immune response to fungal pathogens. May activate an anti-
inflammatory signaling pathway by recruiting SIGIRR.
{ECO:0000269|PubMed:17908936, ECO:0000269|PubMed:18284608,
ECO:0000269|PubMed:21860022, ECO:0000269|PubMed:21965679}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly abundant in embryonic tissue and
tissues containing epithelial cells.
-!- PTM: Removal of N-terminal methionine is necessary for full
antagonistic activity. {ECO:0000269|PubMed:21965679}.
-!- DISRUPTION PHENOTYPE: In combination with transgenic IL36A
exacerbates skin abnormalities (acanthosis, hyperkeratosis,
presence of a mixed inflammatory cell infiltrate and increased
cytokine and chemokine expression). {ECO:0000269|PubMed:17908936}.
-!- MISCELLANEOUS: Bioactive (processed) recombinant IL36RN inhibits
effects of IL-36 when used in 100- 1000-fold molar excess.
{ECO:0000269|PubMed:21860022}.
-!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB59831.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AJ250429; CAB59831.1; ALT_INIT; mRNA.
EMBL; AF200495; AAF69251.1; -; mRNA.
EMBL; AF230378; AAF91275.1; -; mRNA.
EMBL; AK008977; BAB26002.1; -; mRNA.
EMBL; AK009741; BAB26471.1; -; mRNA.
CCDS; CCDS50519.1; -.
RefSeq; NP_001139559.1; NM_001146087.1.
RefSeq; NP_001139560.1; NM_001146088.1.
RefSeq; NP_062324.2; NM_019451.2.
UniGene; Mm.29261; -.
PDB; 1MD6; X-ray; 1.60 A; A=3-156.
PDBsum; 1MD6; -.
ProteinModelPortal; Q9QYY1; -.
SMR; Q9QYY1; -.
STRING; 10090.ENSMUSP00000028360; -.
PhosphoSitePlus; Q9QYY1; -.
MaxQB; Q9QYY1; -.
PaxDb; Q9QYY1; -.
PRIDE; Q9QYY1; -.
Ensembl; ENSMUST00000028360; ENSMUSP00000028360; ENSMUSG00000026983.
Ensembl; ENSMUST00000114490; ENSMUSP00000110134; ENSMUSG00000026983.
Ensembl; ENSMUST00000168941; ENSMUSP00000126028; ENSMUSG00000026983.
GeneID; 54450; -.
KEGG; mmu:54450; -.
UCSC; uc008ios.2; mouse.
CTD; 54450; -.
MGI; MGI:1859325; Il1f5.
eggNOG; ENOG410IZIW; Eukaryota.
eggNOG; ENOG41116AA; LUCA.
GeneTree; ENSGT00900000141028; -.
HOVERGEN; HBG052099; -.
InParanoid; Q9QYY1; -.
KO; K05483; -.
OMA; ALCFRMK; -.
OrthoDB; EOG091G0PWA; -.
PhylomeDB; Q9QYY1; -.
TreeFam; TF300203; -.
Reactome; R-MMU-9014826; Interleukin-36 pathway.
EvolutionaryTrace; Q9QYY1; -.
PRO; PR:Q9QYY1; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026983; -.
CleanEx; MM_IL1F5; -.
ExpressionAtlas; Q9QYY1; baseline and differential.
Genevisible; Q9QYY1; MM.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0005152; F:interleukin-1 receptor antagonist activity; IEA:InterPro.
GO; GO:0005149; F:interleukin-1 receptor binding; IBA:GO_Central.
GO; GO:0019732; P:antifungal humoral response; ISO:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; ISO:MGI.
GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IGI:MGI.
InterPro; IPR020877; IL-1_CS.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR003297; IL-1RA/IL-36.
InterPro; IPR027171; IL-36RA.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR45145; PTHR45145; 1.
Pfam; PF00340; IL1; 1.
PRINTS; PR00264; INTERLEUKIN1.
PRINTS; PR01360; INTRLEUKIN1X.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00253; INTERLEUKIN_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytokine; Disulfide bond; Immunity;
Innate immunity; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:21965679}.
CHAIN 2 156 Interleukin-36 receptor antagonist
protein.
/FTId=PRO_0000153643.
DISULFID 9 155 {ECO:0000269|PubMed:12974628}.
CONFLICT 2 2 Missing (in Ref. 3; AAF69251).
{ECO:0000305}.
STRAND 8 14 {ECO:0000244|PDB:1MD6}.
STRAND 19 23 {ECO:0000244|PDB:1MD6}.
STRAND 26 29 {ECO:0000244|PDB:1MD6}.
HELIX 32 35 {ECO:0000244|PDB:1MD6}.
STRAND 43 47 {ECO:0000244|PDB:1MD6}.
HELIX 53 55 {ECO:0000244|PDB:1MD6}.
STRAND 57 62 {ECO:0000244|PDB:1MD6}.
TURN 63 66 {ECO:0000244|PDB:1MD6}.
STRAND 67 70 {ECO:0000244|PDB:1MD6}.
STRAND 73 76 {ECO:0000244|PDB:1MD6}.
STRAND 80 83 {ECO:0000244|PDB:1MD6}.
HELIX 86 91 {ECO:0000244|PDB:1MD6}.
STRAND 92 94 {ECO:0000244|PDB:1MD6}.
HELIX 97 99 {ECO:0000244|PDB:1MD6}.
STRAND 100 105 {ECO:0000244|PDB:1MD6}.
STRAND 110 117 {ECO:0000244|PDB:1MD6}.
STRAND 121 124 {ECO:0000244|PDB:1MD6}.
STRAND 126 131 {ECO:0000244|PDB:1MD6}.
STRAND 133 135 {ECO:0000244|PDB:1MD6}.
STRAND 150 154 {ECO:0000244|PDB:1MD6}.
SEQUENCE 156 AA; 17136 MW; A4D1EE2F93CF77A7 CRC64;
MMVLSGALCF RMKDSALKVL YLHNNQLLAG GLHAEKVIKG EEISVVPNRA LDASLSPVIL
GVQGGSQCLS CGTEKGPILK LEPVNIMELY LGAKESKSFT FYRRDMGLTS SFESAAYPGW
FLCTSPEADQ PVRLTQIPED PAWDAPITDF YFQQCD


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