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Q9QYY1 (I36RA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-36 receptor antagonist protein
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 names
Name:IL36RN
Synonyms:Fil1d, Il1f5, Il1h3, Il1hy1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is a highly and a specific antagonist of the IL-1 receptor-related protein 2/IL1RL2-mediated response to interleukin IL36G. Could constitute part of an independent signaling system analogous to interleukin-1 alpha (IL-1A), beta (IL-1B) receptor agonist and interleukin-1 receptor type I (IL-1R1), that is present in epithelial barriers and takes part in local inflammatory response By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Highly abundant in embryonic tissue and tissues containing epithelial cells.

Sequence similarities

Belongs to the IL-1 family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Interleukin-36 receptor antagonist protein
PRO_0000153643

Amino acid modifications

Disulfide bond9 ↔ 155 Ref.5

Experimental info

Sequence conflict21Missing in AAF69251. Ref.3

Secondary structure

..................................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QYY1 [UniParc].

Last modified November 8, 2002. Version 2.
Checksum: A4D1EE2F93CF77A7

FASTA15617,136
        10         20         30         40         50         60 
MMVLSGALCF RMKDSALKVL YLHNNQLLAG GLHAEKVIKG EEISVVPNRA LDASLSPVIL 

        70         80         90        100        110        120 
GVQGGSQCLS CGTEKGPILK LEPVNIMELY LGAKESKSFT FYRRDMGLTS SFESAAYPGW 

       130        140        150 
FLCTSPEADQ PVRLTQIPED PAWDAPITDF YFQQCD 

« Hide

References

« Hide 'large scale' references
[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(2000) [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(2000) [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(2001) [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. expand/collapse author list , 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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach and Tongue.
[5]"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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3-156, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS50519.1.
RefSeqNP_001139559.1. NM_001146087.1.
NP_001139560.1. NM_001146088.1.
NP_062324.2. NM_019451.2.
UniGeneMm.29261.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MD6X-ray1.60A3-156[»]
ProteinModelPortalQ9QYY1.
SMRQ9QYY1. Positions 3-156.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

MaxQBQ9QYY1.
PRIDEQ9QYY1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028360; ENSMUSP00000028360; ENSMUSG00000026983.
ENSMUST00000114490; ENSMUSP00000110134; ENSMUSG00000026983.
ENSMUST00000168941; ENSMUSP00000126028; ENSMUSG00000026983.
GeneID54450.
KEGGmmu:54450.
UCSCuc008ios.2. mouse.

Organism-specific databases

CTD54450.
MGIMGI:1859325. Il1f5.

Phylogenomic databases

eggNOGNOG46537.
GeneTreeENSGT00530000062899.
HOVERGENHBG052099.
InParanoidQ9QYY1.
KOK05483.
OMAFYRRDMG.
OrthoDBEOG7QG45K.
PhylomeDBQ9QYY1.
TreeFamTF300203.

Gene expression databases

BgeeQ9QYY1.
CleanExMM_IL1F5.
GenevestigatorQ9QYY1.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR020877. IL-1_CS.
IPR000975. IL-1_fam.
IPR003297. IL-1RA/IL-36.
IPR027171. IL-36RA.
[Graphical view]
PANTHERPTHR10078:SF7. PTHR10078:SF7. 1 hit.
PfamPF00340. IL1. 1 hit.
[Graphical view]
PRINTSPR00264. INTERLEUKIN1.
PR01360. INTRLEUKIN1X.
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QYY1.
NextBio311328.
PROQ9QYY1.
SOURCESearch...

Entry information

Entry nameI36RA_MOUSE
AccessionPrimary (citable) accession number: Q9QYY1
Secondary accession number(s): Q9JIG2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot