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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.
11-DEC-2019, entry version 140.
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=Truncated N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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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.
PDB; 1MD6; X-ray; 1.60 A; A=3-156.
PDBsum; 1MD6; -.
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; ENSGT00950000182943; -.
InParanoid; Q9QYY1; -.
KO; K05483; -.
OMA; NRWLDAR; -.
OrthoDB; 1410755at2759; -.
PhylomeDB; Q9QYY1; -.
TreeFam; TF300203; -.
Reactome; R-MMU-9014826; Interleukin-36 pathway.
EvolutionaryTrace; Q9QYY1; -.
PRO; PR:Q9QYY1; -.
Proteomes; UP000000589; Chromosome 2.
RNAct; Q9QYY1; protein.
Bgee; ENSMUSG00000026983; Expressed in 55 organ(s), highest expression level in skin of back.
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:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
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.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IBA:GO_Central.
GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
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; PTHR10078:SF32; PTHR10078:SF32; 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; Cytokine; Disulfide bond; Immunity; Innate immunity;
Reference proteome; Secreted.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:21965679"
CHAIN 2..156
/note="Interleukin-36 receptor antagonist protein"
/id="PRO_0000153643"
DISULFID 9..155
/evidence="ECO:0000269|PubMed:12974628"
CONFLICT 2
/note="Missing (in Ref. 3; AAF69251)"
/evidence="ECO:0000305"
STRAND 8..14
/evidence="ECO:0000244|PDB:1MD6"
STRAND 19..23
/evidence="ECO:0000244|PDB:1MD6"
STRAND 26..29
/evidence="ECO:0000244|PDB:1MD6"
HELIX 32..35
/evidence="ECO:0000244|PDB:1MD6"
STRAND 43..47
/evidence="ECO:0000244|PDB:1MD6"
HELIX 53..55
/evidence="ECO:0000244|PDB:1MD6"
STRAND 57..62
/evidence="ECO:0000244|PDB:1MD6"
TURN 63..66
/evidence="ECO:0000244|PDB:1MD6"
STRAND 67..70
/evidence="ECO:0000244|PDB:1MD6"
STRAND 73..76
/evidence="ECO:0000244|PDB:1MD6"
STRAND 80..83
/evidence="ECO:0000244|PDB:1MD6"
HELIX 86..91
/evidence="ECO:0000244|PDB:1MD6"
STRAND 92..94
/evidence="ECO:0000244|PDB:1MD6"
HELIX 97..99
/evidence="ECO:0000244|PDB:1MD6"
STRAND 100..105
/evidence="ECO:0000244|PDB:1MD6"
STRAND 110..117
/evidence="ECO:0000244|PDB:1MD6"
STRAND 121..124
/evidence="ECO:0000244|PDB:1MD6"
STRAND 126..131
/evidence="ECO:0000244|PDB:1MD6"
STRAND 133..135
/evidence="ECO:0000244|PDB:1MD6"
STRAND 150..154
/evidence="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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