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Reviewed, UniProtKB/Swiss-Prot Q61730 (IL1AP_MOUSE)

Last modified December 15, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Interleukin-1 receptor accessory protein
      Short name=IL-1 receptor accessory protein
      Short name=IL-1RAcP
Gene names
Name: Il1rap
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Mediates interleukin-1-dependent activation of NF-kappa-B. Isoform 1 is part of the membrane-bound form of the IL-1 receptor. Signaling involves formation of a ternary complex containing IL1R1, TOLLIP, MYD88, and IRAK1 or IRAK2. Isoform 2 modulates the response to interleukins by associating with soluble IL1R1 and enhancing interleukin-binding to the decoy receptor. Ref.5

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.1.

Isoform 2: Secreted Ref.1.

Tissue specificity

Detected in lung, brain, spleen, thymus and liver. Ref.1

Sequence similarities

Belongs to the interleukin-1 receptor family.

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

Contains 1 TIR domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TollipQ9QZ061EBI-525035,EBI-74272

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61730-1)

Also known as: MuIL-1R AcP;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q61730-2)

Also known as: SmuIL-1R AcP;

The sequence of this isoform differs from the canonical sequence as follows:
     351-359: VIPPRYTVE → GNGCTEPMTL
     360-570: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 570550Interleukin-1 receptor accessory protein
PRO_0000015452

Regions

Topological domain21 – 367347Extracellular Potential
Transmembrane368 – 38821 Potential
Topological domain389 – 570182Cytoplasmic Potential
Domain21 – 128108Ig-like C2-type 1
Domain139 – 23092Ig-like C2-type 2
Domain243 – 348106Ig-like C2-type 3
Domain403 – 549147TIR

Amino acid modifications

Modified residue3951Phosphothreonine Ref.7
Modified residue3981Phosphothreonine Ref.7
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 114 Potential
Disulfide bond137 ↔ 181 Potential
Disulfide bond160 ↔ 212 Potential
Disulfide bond266 ↔ 332 Potential

Natural variations

Alternative sequence351 – 3599VIPPRYTVE → GNGCTEPMTL in isoform 2.
VSP_008054
Alternative sequence360 – 570211Missing in isoform 2.
VSP_008055

Experimental info

Mutagenesis527 – 5348KGEKSKYP → AAAAAAAA: Abolishes interaction with MYD88 and IL-1-dependent activation of NF-kappa-B. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MuIL-1R AcP) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4D4B07E0310AFDC5

FASTA57065,741
        10         20         30         40         50         60 
MGLLWYLMSL SFYGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKYNYST 

        70         80         90        100        110        120 
AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT 

       130        140        150        160        170        180 
YCSKVAFPLE VVQKDSCFNS AMRFPVHKMY IEHGIHKITC PNVDGYFPSS VKPSVTWYKG 

       190        200        210        220        230        240 
CTEIVDFHNV LPEGMNLSFF IPLVSNNGNY TCVVTYPENG RLFHLTRTVT VKVVGSPKDA 

       250        260        270        280        290        300 
LPPQIYSPND RVVYEKEPGE ELVIPCKVYF SFIMDSHNEV WWTIDGKKPD DVTVDITINE 

       310        320        330        340        350        360 
SVSYSSTEDE TRTQILSIKK VTPEDLRRNY VCHARNTKGE AEQAAKVKQK VIPPRYTVEL 

       370        380        390        400        410        420 
ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNVEEEEF 

       430        440        450        460        470        480 
VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL 

       490        500        510        520        530        540 
LELKAGLENM ASRGNINVIL VQYKAVKDMK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK 

       550        560        570 
QLQVAMPVKK SPRWSSNDKQ GLSYSSLKNV 

« Hide

Isoform 2 (SmuIL-1R AcP).

Checksum: E525471759FF7719
Show »

FASTA36041,567

References

« Hide 'large scale' references
[1]"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: 7775431] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH IL1R1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Fibroblast.
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Brain and Spinal cord.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[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: 10854325] [Abstract]
Cited for: INTERACTION WITH TOLLIP.
[5]"Identification of essential regions in the cytoplasmic tail of interleukin-1 receptor accessory protein critical for interleukin-1 signaling."
Radons J., Gabler S., Wesche H., Korherr C., Hofmeister R., Falk W.
J. Biol. Chem. 277:16456-16463(2002) [PubMed: 11880380] [Abstract]
Cited for: MUTAGENESIS OF 527-LYS--PRO-534, INTERACTION WITH MYD88, FUNCTION.
[6]"Characterization of a cascade of protein interactions initiated at the IL-1 receptor."
Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S., Auron P.E.
Biochem. Biophys. Res. Commun. 303:525-531(2003) [PubMed: 12659850] [Abstract]
Cited for: INTERACTION WITH IRAK2.
[7]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395 AND THR-398, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X85999 mRNA. Translation: CAA59991.1.
AK039582 mRNA. Translation: BAC30392.1.
AK045686 mRNA. Translation: BAC32457.1.
BC021159 mRNA. Translation: AAH21159.1.
IPIIPI00113879.
IPI00124823.
PIRA57535.
RefSeqNP_032390.1.
NP_598864.1.
UniGeneMm.253424

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-296N.
IntActQ61730. 3 interactions.
STRINGQ61730.

PTM databases

PhosphoSiteQ61730.

Proteomic databases

PRIDEQ61730.

Genome annotation databases

EnsemblENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514; Mus musculus. [Genome view]
ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514; Mus musculus. [Genome view]
GeneID16180.
UCSCuc007yvd.1. mouse.
uc007yve.1. mouse.

Organism-specific databases

CTD16180.
MGIMGI:104975. Il1rap.

Phylogenomic databases

HOVERGENQ61730.
OMAVDGFFPS.

Gene expression databases

ArrayExpressQ61730.
BgeeQ61730.
CleanExMM_IL1RAP.
GenevestigatorQ61730.
GermOnlineENSMUSG00000022514. Mus musculus.

Family and domain databases

InterProIPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL1-receptor.
IPR004075. IL1_rcpt_1.
IPR004074. IL1_rcpt_I/II.
IPR000157. Toll-Interleukin_rcpt.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHERPTHR11890. IL1-receptor. 1 hit.
PfamPF00047. ig. 3 hits.
PF01582. TIR. 1 hit.
[Graphical view]
PRINTSPR01536. INTRLKN1R12F.
PR01537. INTRLKN1R1F.
SMARTSM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio289053.
SOURCESearch...

Entry information

Entry nameIL1AP_MOUSE
AccessionPrimary (citable) accession number: Q61730
Secondary accession number(s): Q8VCB9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1996
Last modified: December 15, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents