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P13504 (IL1R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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
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-1 receptor type 1
Short name=IL-1R-1
Short name=IL-1RT-1
Short name=IL-1RT1
Alternative name(s):
CD121 antigen-like family member A
Interleukin-1 receptor alpha
Short name=IL-1R-alpha
Interleukin-1 receptor type I
p80
CD_antigen=CD121a

Cleaved into the following 2 chains:

  1. Interleukin-1 receptor type 1, membrane form
    Short name=mIL-1R1
    Short name=mIL-1RI
  2. Interleukin-1 receptor type 1, soluble form
    Short name=sIL-1R1
    Short name=sIL-1RI
Gene names
Name:Il1r1
Synonyms:Il-1r1, Il1ra
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex By similarity.

Subunit structure

The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Interacts with PIK3R1 By similarity. Ref.3 Ref.4

Subcellular location

Membrane; Single-pass type I membrane protein. Cell membrane Probable. Secreted By similarity.

Post-translational modification

A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding) By similarity.

Rapidly phosphorylated on Tyr-499 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1 By similarity. Ref.2

Sequence similarities

Belongs to the interleukin-1 receptor family.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 TIR domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1
Chain20 – 576557Interleukin-1 receptor type 1, membrane form
PRO_0000015436
Chain20 – ?Interleukin-1 receptor type 1, soluble formPRO_0000415345

Regions

Topological domain20 – 338319Extracellular Potential
Transmembrane339 – 35921Helical; Potential
Topological domain360 – 576217Cytoplasmic Potential
Domain25 – 11591Ig-like C2-type 1
Domain121 – 21393Ig-like C2-type 2
Domain229 – 329101Ig-like C2-type 3
Domain386 – 544159TIR

Amino acid modifications

Modified residue4991Phosphotyrosine By similarity
Modified residue5561Phosphothreonine; by PKC Ref.2
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 107 By similarity
Disulfide bond46 ↔ 99 By similarity
Disulfide bond145 ↔ 199 By similarity
Disulfide bond251 ↔ 315 By similarity

Secondary structure

1 ........................................................... 576
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13504 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 7AA8304C86412A16

FASTA57666,698
        10         20         30         40         50         60 
MENMKVLLGL ICLMVPLLSL EIDVCTEYPN QIVLFLSVNE IDIRKCPLTP NKMHGDTIIW 

        70         80         90        100        110        120 
YKNDSKTPIS ADRDSRIHQQ NEHLWFVPAK VEDSGYYYCI VRNSTYCLKT KVTVTVLEND 

       130        140        150        160        170        180 
PGLCYSTQAT FPQRLHIAGD GSLVCPYVSY FKDENNELPE VQWYKNCKPL LLDNVSFFGV 

       190        200        210        220        230        240 
KDKLLVRNVA EEHRGDYICR MSYTFRGKQY PVTRVIQFIT IDENKRDRPV ILSPRNETIE 

       250        260        270        280        290        300 
ADPGSMIQLI CNVTGQFSDL VYWKWNGSEI EWNDPFLAED YQFVEHPSTK RKYTLITTLN 

       310        320        330        340        350        360 
ISEVKSQFYR YPFICVVKNT NIFESAHVQL IYPVPDFKNY LIGGFIILTA TIVCCVCIYK 

       370        380        390        400        410        420 
VFKVDIVLWY RDSCSGFLPS KASDGKTYDA YILYPKTLGE GSFSDLDTFV FKLLPEVLEG 

       430        440        450        460        470        480 
QFGYKLFIYG RDDYVGEDTI EVTNENVKKS RRLIIILVRD MGGFSWLGQS SEEQIAIYNA 

       490        500        510        520        530        540 
LIQEGIKIVL LELEKIQDYE KMPDSIQFIK QKHGVICWSG DFQERPQSAK TRFWKNLRYQ 

       550        560        570 
MPAQRRSPLS KHRLLTLDPV RDTKEKLPAA THLPLG

« Hide

References

[1]"cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily."
Sims J.E., March C.J., Cosman D., Widmer M.B., McDonald H.R., McMahan C.J., Grubin C.E., Wignall J.M., Jackson J.L., Call S.M., Friend D., Alpert A.R., Gillis S., Urdal D.L., Dower S.K.
Science 241:585-589(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-45.
[2]"Phorbol ester induces phosphorylation of the 80 kilodalton murine interleukin 1 receptor at a single threonine residue."
Bird T.A., Woodward A., Jackson J.L., Dower S.K., Sims J.E.
Biochem. Biophys. Res. Commun. 177:61-67(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-556.
[3]"Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex."
Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.
J. Biol. Chem. 270:13757-13765(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IL1RAP.
[4]"Tollip, a new component of the IL-1R1 pathway, links IRAK to the IL-1 receptor."
Burns K., Clatworthy J., Martin L., Martinon F., Plumpton C., Maschera B., Lewis A., Ray K., Tschopp J., Volpe F.
Nat. Cell Biol. 2:346-351(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOLLIP; MYD88 AND IRAK1.
[5]"Modelling of fish interleukin-1 and its receptor."
Scapigliati G., Costantini S., Colonna G., Facchiano A., Buonocore F., Bossu P., Cunningham C., Holland J.W., Secombes C.J.
Dev. Comp. Immunol. 28:429-441(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 25-334.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M20658 mRNA. Translation: AAA39279.1.
CCDSCCDS35547.1.
PIRA32604.
RefSeqNP_032388.1. NM_008362.2.
XP_006495776.1. XM_006495713.1.
UniGeneMm.896.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OU3model-A25-334[»]
ProteinModelPortalP13504.
SMRP13504. Positions 25-334, 386-542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200625. 6 interactions.
IntActP13504. 5 interactions.

Chemistry

ChEMBLCHEMBL2189148.

PTM databases

PhosphoSiteP13504.

Proteomic databases

PRIDEP13504.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027241; ENSMUSP00000027241; ENSMUSG00000026072.
GeneID16177.
KEGGmmu:16177.
UCSCuc007atv.1. mouse.

Organism-specific databases

CTD3554.
MGIMGI:96545. Il1r1.

Phylogenomic databases

eggNOGNOG40914.
HOGENOMHOG000253916.
HOVERGENHBG052103.
InParanoidP13504.
KOK04386.
OMAIQDYEKM.
OrthoDBEOG7H1JK3.
PhylomeDBP13504.
TreeFamTF325519.

Gene expression databases

ArrayExpressP13504.
BgeeP13504.
CleanExMM_IL1R1.
GenevestigatorP13504.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR015621. IL-1_rcpt_fam.
IPR004076. IL-1_rcpt_I-typ.
IPR004074. IL-1_rcpt_I/II-typ.
IPR000157. TIR_dom.
[Graphical view]
PANTHERPTHR11890. PTHR11890. 1 hit.
PfamPF07679. I-set. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PRINTSPR01538. INTRLEUKN1R1.
PR01536. INTRLKN1R12F.
SMARTSM00409. IG. 2 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289041.
PROP13504.
SOURCESearch...

Entry information

Entry nameIL1R1_MOUSE
AccessionPrimary (citable) accession number: P13504
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 146 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents