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Protein

Interleukin-36 receptor antagonist protein

Gene

IL36RN

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. cytokine activity Source: GO_Central
  2. interleukin-1 receptor binding Source: GO_Central

GO - Biological processi

  1. antifungal humoral response Source: MGI
  2. cytokine-mediated signaling pathway Source: GO_Central
  3. innate immune response Source: UniProtKB-KW
  4. negative regulation of cytokine-mediated signaling pathway Source: MGI
  5. negative regulation of interferon-gamma secretion Source: MGI
  6. negative regulation of interleukin-17 production Source: MGI
  7. negative regulation of interleukin-6 production Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-36 receptor antagonist protein
Short name:
IL-36Ra1 Publication
Alternative name(s):
Interleukin-1 HY1
Short name:
IL-1HY1
Interleukin-1 delta
Short name:
IL-1 delta
Interleukin-1 family member 5
Short name:
IL-1F5
Interleukin-1 homolog 3
Short name:
IL-1H3
Interleukin-1-like protein 1
Short name:
IL-1L1
Gene namesi
Name:IL36RN
Synonyms:Fil1d, Il1f5, Il1h3, Il1hy1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1859325. Il1f5.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

In combination with transgenic IL36A exacerbates skin abnormalities (acanthosis, hyperkeratosis, presence of a mixed inflammatory cell infiltrate and increased cytokine and chemokine expression).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 156155Interleukin-36 receptor antagonist proteinPRO_0000153643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi9 ↔ 1551 Publication

Post-translational modificationi

Removal of N-terminal methionine is necessary for full antagonistic activity.1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9QYY1.
PRIDEiQ9QYY1.

Expressioni

Tissue specificityi

Highly abundant in embryonic tissue and tissues containing epithelial cells.

Gene expression databases

BgeeiQ9QYY1.
CleanExiMM_IL1F5.
ExpressionAtlasiQ9QYY1. baseline and differential.
GenevestigatoriQ9QYY1.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Beta strandi19 – 235Combined sources
Beta strandi26 – 294Combined sources
Helixi32 – 354Combined sources
Beta strandi43 – 475Combined sources
Helixi53 – 553Combined sources
Beta strandi57 – 626Combined sources
Turni63 – 664Combined sources
Beta strandi67 – 704Combined sources
Beta strandi73 – 764Combined sources
Beta strandi80 – 834Combined sources
Helixi86 – 916Combined sources
Beta strandi92 – 943Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi150 – 1545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MD6X-ray1.60A3-156[»]
ProteinModelPortaliQ9QYY1.
SMRiQ9QYY1. Positions 3-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QYY1.

Family & Domainsi

Sequence similaritiesi

Belongs to the IL-1 family.Curated

Phylogenomic databases

eggNOGiNOG46537.
GeneTreeiENSGT00530000062899.
HOVERGENiHBG052099.
InParanoidiQ9QYY1.
KOiK05483.
OMAiMKDSALK.
OrthoDBiEOG7QG45K.
PhylomeDBiQ9QYY1.
TreeFamiTF300203.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR020877. IL-1_CS.
IPR000975. IL-1_fam.
IPR003297. IL-1RA/IL-36.
IPR027171. IL-36RA.
[Graphical view]
PANTHERiPTHR10078:SF7. PTHR10078:SF7. 1 hit.
PfamiPF00340. IL1. 1 hit.
[Graphical view]
PRINTSiPR00264. INTERLEUKIN1.
PR01360. INTRLEUKIN1X.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9QYY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMVLSGALCF RMKDSALKVL YLHNNQLLAG GLHAEKVIKG EEISVVPNRA
60 70 80 90 100
LDASLSPVIL GVQGGSQCLS CGTEKGPILK LEPVNIMELY LGAKESKSFT
110 120 130 140 150
FYRRDMGLTS SFESAAYPGW FLCTSPEADQ PVRLTQIPED PAWDAPITDF

YFQQCD
Length:156
Mass (Da):17,136
Last modified:November 7, 2002 - v2
Checksum:iA4D1EE2F93CF77A7
GO

Sequence cautioni

The sequence CAB59831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing in AAF69251 (PubMed:11466363).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250429 mRNA. Translation: CAB59831.1. Different initiation.
AF200495 mRNA. Translation: AAF69251.1.
AF230378 mRNA. Translation: AAF91275.1.
AK008977 mRNA. Translation: BAB26002.1.
AK009741 mRNA. Translation: BAB26471.1.
CCDSiCCDS50519.1.
RefSeqiNP_001139559.1. NM_001146087.1.
NP_001139560.1. NM_001146088.1.
NP_062324.2. NM_019451.2.
UniGeneiMm.29261.

Genome annotation databases

EnsembliENSMUST00000028360; ENSMUSP00000028360; ENSMUSG00000026983.
ENSMUST00000114490; ENSMUSP00000110134; ENSMUSG00000026983.
ENSMUST00000168941; ENSMUSP00000126028; ENSMUSG00000026983.
GeneIDi54450.
KEGGimmu:54450.
UCSCiuc008ios.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250429 mRNA. Translation: CAB59831.1. Different initiation.
AF200495 mRNA. Translation: AAF69251.1.
AF230378 mRNA. Translation: AAF91275.1.
AK008977 mRNA. Translation: BAB26002.1.
AK009741 mRNA. Translation: BAB26471.1.
CCDSiCCDS50519.1.
RefSeqiNP_001139559.1. NM_001146087.1.
NP_001139560.1. NM_001146088.1.
NP_062324.2. NM_019451.2.
UniGeneiMm.29261.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MD6X-ray1.60A3-156[»]
ProteinModelPortaliQ9QYY1.
SMRiQ9QYY1. Positions 3-156.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

MaxQBiQ9QYY1.
PRIDEiQ9QYY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028360; ENSMUSP00000028360; ENSMUSG00000026983.
ENSMUST00000114490; ENSMUSP00000110134; ENSMUSG00000026983.
ENSMUST00000168941; ENSMUSP00000126028; ENSMUSG00000026983.
GeneIDi54450.
KEGGimmu:54450.
UCSCiuc008ios.2. mouse.

Organism-specific databases

CTDi54450.
MGIiMGI:1859325. Il1f5.

Phylogenomic databases

eggNOGiNOG46537.
GeneTreeiENSGT00530000062899.
HOVERGENiHBG052099.
InParanoidiQ9QYY1.
KOiK05483.
OMAiMKDSALK.
OrthoDBiEOG7QG45K.
PhylomeDBiQ9QYY1.
TreeFamiTF300203.

Miscellaneous databases

EvolutionaryTraceiQ9QYY1.
NextBioi311328.
PROiQ9QYY1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYY1.
CleanExiMM_IL1F5.
ExpressionAtlasiQ9QYY1. baseline and differential.
GenevestigatoriQ9QYY1.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR020877. IL-1_CS.
IPR000975. IL-1_fam.
IPR003297. IL-1RA/IL-36.
IPR027171. IL-36RA.
[Graphical view]
PANTHERiPTHR10078:SF7. PTHR10078:SF7. 1 hit.
PfamiPF00340. IL1. 1 hit.
[Graphical view]
PRINTSiPR00264. INTERLEUKIN1.
PR01360. INTRLEUKIN1X.
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Barton J.L., Herbst R., Bosisio D., Higgins L., Nicklin M.J.H.
    Eur. J. Immunol. 30:3299-3308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification and initial characterization of four novel members of the interleukin-1 family."
    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.
    J. Biol. Chem. 275:10308-10314(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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."
    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.
    J. Immunol. 167:1440-1446(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Stomach and Tongue.
  5. "Opposing activities of two novel members of the IL-1 ligand family regulate skin inflammation."
    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.
    J. Exp. Med. 204:2603-2614(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "IL-1F5 mediates anti-inflammatory activity in the brain through induction of IL-4 following interaction with SIGIRR/TIR8."
    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.
    J. Neurochem. 105:1960-1969(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: FUNCTION.
  8. "Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity."
    Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M., Gabel C.A., Sims J.E.
    J. Biol. Chem. 286:42594-42602(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CLEAVAGE OF INITIATOR METHIONINE.
  9. "High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity."
    Dunn E.F., Gay N.J., Bristow A.F., Gearing D.P., O'Neill L.A.J., Pei X.Y.
    Biochemistry 42:10938-10944(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3-156, DISULFIDE BOND.

Entry informationi

Entry nameiI36RA_MOUSE
AccessioniPrimary (citable) accession number: Q9QYY1
Secondary accession number(s): Q9JIG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2002
Last sequence update: November 7, 2002
Last modified: February 3, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Bioactive (processed) recombinant IL36RN inhibits effects of IL-36 when used in 100- 1000-fold molar excess.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.