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Protein

Interleukin-1 receptor accessory protein

Gene

Il1rap

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

Functioni

Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B 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. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Secreted forms (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and increase the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33 signaling system.1 PublicationBy similarity5 Publications
Isoform 2: Associates with secreted ligand-bound IL1R2 and increases the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling.2 Publications
Isoform 3: Required for Src phosphorylation by IL1B. Required for IL1B-potentiated NMDA-induced calcium influx in neurons acting in cooperation with IL1R1 isoform 2 to mediate Akt kinase activation.2 Publications

GO - Molecular functioni

  • interleukin-1 receptor activity Source: MGI
  • interleukin-33 receptor activity Source: UniProtKB
  • protein tyrosine kinase binding Source: MGI
  • signal transducer activity Source: MGI

GO - Biological processi

  • cytokine-mediated signaling pathway Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • interleukin-2 biosynthetic process Source: MGI
  • interleukin-33-mediated signaling pathway Source: UniProtKB
  • interleukin-4 secretion Source: UniProtKB
  • positive regulation of dendrite development Source: MGI
  • positive regulation of interleukin-13 production Source: UniProtKB
  • positive regulation of interleukin-5 production Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of synapse assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-446652. Interleukin-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 receptor accessory protein
Short name:
IL-1 receptor accessory protein
Short name:
IL-1RAcP
Alternative name(s):
Interleukin-33 receptot beta chain1 Publication
Gene namesi
Name:Il1rap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:104975. Il1rap.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 367347ExtracellularSequence analysisAdd
BLAST
Transmembranei368 – 38821HelicalSequence analysisAdd
BLAST
Topological domaini389 – 570182CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi527 – 5348KGEKSKYP → AAAAAAAA: Abolishes interaction with MYD88 and IL-1-dependent activation of NF-kappa-B. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 570550Interleukin-1 receptor accessory proteinPRO_0000015452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 122PROSITE-ProRule annotation
Disulfide bondi47 ↔ 114PROSITE-ProRule annotation
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi137 ↔ 181PROSITE-ProRule annotation
Disulfide bondi160 ↔ 212PROSITE-ProRule annotation
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi266 ↔ 332PROSITE-ProRule annotation
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ61730.
MaxQBiQ61730.
PRIDEiQ61730.

PTM databases

iPTMnetiQ61730.
PhosphoSiteiQ61730.

Expressioni

Tissue specificityi

Detected in lung, brain, spleen, thymus and liver. Expressed in brain endothelial cells, astrocytes, microglia and neurons. Isoform 3 is predominantly expressed in brain; expressed in hippocampal neurons.4 Publications

Gene expression databases

BgeeiQ61730.
CleanExiMM_IL1RAP.
ExpressionAtlasiQ61730. baseline and differential.
GenevisibleiQ61730. MM.

Interactioni

Subunit structurei

The interleukin-36 receptor complex is a heterodimer of IL1RL2 and IL1RAP; the association is inhibited by IL36RN. The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with IL1R2 to form a non-signaling interleukin-1 receptor complex. Interacts with IL-33-bound IL1RL1 to form the minimal interleukin-33 signaling complex with a 1:1:1 stoechiometry. Interacts with KIT (independently of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TollipQ9QZ062EBI-525035,EBI-74272

GO - Molecular functioni

  • protein tyrosine kinase binding Source: MGI

Protein-protein interaction databases

BioGridi200628. 3 interactions.
DIPiDIP-296N.
IntActiQ61730. 3 interactions.

Structurei

Secondary structure

1
570
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295Combined sources
Beta strandi35 – 384Combined sources
Beta strandi43 – 464Combined sources
Helixi48 – 503Combined sources
Turni51 – 533Combined sources
Helixi58 – 625Combined sources
Turni63 – 653Combined sources
Beta strandi67 – 748Combined sources
Beta strandi85 – 873Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 955Combined sources
Beta strandi98 – 1036Combined sources
Helixi106 – 1083Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi188 – 1925Combined sources
Beta strandi194 – 2018Combined sources
Beta strandi208 – 21811Combined sources
Beta strandi221 – 23414Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi279 – 2868Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi315 – 3206Combined sources
Helixi323 – 3275Combined sources
Beta strandi331 – 34313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YFDX-ray3.25B21-351[»]
ProteinModelPortaliQ61730.
SMRiQ61730. Positions 24-345, 403-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 128108Ig-like C2-type 1Add
BLAST
Domaini139 – 23092Ig-like C2-type 2Add
BLAST
Domaini243 – 348106Ig-like C2-type 3Add
BLAST
Domaini403 – 549147TIRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the interleukin-1 receptor family.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119071.
HOGENOMiHOG000092977.
HOVERGENiHBG104298.
InParanoidiQ61730.
KOiK04723.
OMAiKRSHRWS.
PhylomeDBiQ61730.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL-1_rcpt_fam.
IPR004074. IL-1_rcpt_I/II-typ.
IPR000157. TIR_dom.
[Graphical view]
PANTHERiPTHR11890. PTHR11890. 1 hit.
PfamiPF13895. Ig_2. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PRINTSiPR01536. INTRLKN1R12F.
SMARTiSM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61730-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGLLWYLMSL SFYGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF
60 70 80 90 100
EHFLKYNYST AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW
110 120 130 140 150
FRPTLLNDTG NYTCMLRNTT YCSKVAFPLE VVQKDSCFNS AMRFPVHKMY
160 170 180 190 200
IEHGIHKITC PNVDGYFPSS VKPSVTWYKG CTEIVDFHNV LPEGMNLSFF
210 220 230 240 250
IPLVSNNGNY TCVVTYPENG RLFHLTRTVT VKVVGSPKDA LPPQIYSPND
260 270 280 290 300
RVVYEKEPGE ELVIPCKVYF SFIMDSHNEV WWTIDGKKPD DVTVDITINE
310 320 330 340 350
SVSYSSTEDE TRTQILSIKK VTPEDLRRNY VCHARNTKGE AEQAAKVKQK
360 370 380 390 400
VIPPRYTVEL ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL
410 420 430 440 450
DGKEYDIYVS YARNVEEEEF VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV
460 470 480 490 500
TDETLSFIQK SRRLLVVLSP NYVLQGTQAL LELKAGLENM ASRGNINVIL
510 520 530 540 550
VQYKAVKDMK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK QLQVAMPVKK
560 570
SPRWSSNDKQ GLSYSSLKNV
Length:570
Mass (Da):65,741
Last modified:November 1, 1996 - v1
Checksum:i4D4B07E0310AFDC5
GO
Isoform 2 (identifier: Q61730-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:360
Mass (Da):41,567
Checksum:iE525471759FF7719
GO
Isoform 3 (identifier: Q61730-3) [UniParc]FASTAAdd to basket

Also known as: IL-1RAcPb

The sequence of this isoform differs from the canonical sequence as follows:
     449-570: IVTDETLSFI...GLSYSSLKNV → NTVEAVFDFI...LSNNNDFYIL

Show »
Length:685
Mass (Da):78,640
Checksum:iE1EEC0B8F4AF720F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 3599VIPPRYTVE → GNGCTEPMTL in isoform 2. 3 PublicationsVSP_008054
Alternative sequencei360 – 570211Missing in isoform 2. 3 PublicationsVSP_008055Add
BLAST
Alternative sequencei449 – 570122IVTDE…SLKNV → NTVEAVFDFIQRSRRMIVVL SPDYVTEKSISMLEFKLGVM CQNSIATKLIVVEYRPLEQP HPGIMQLKESVSFVSWKGEK SKHSGSKFWKALRLALPLRS LSASSGWNESCSSQSDISLD HVQRRSRLKEPPELRSSERV SGAEPAPGTMSKHRGKPSAA CRCCVTYCEGESHLRSKSRA EMHTHPQWETHLCKPPLQES ESQWIQNGTRPEPAPQISAL ALRHFTDLSNNNDFYIL in isoform 3. VSP_058171Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85999 mRNA. Translation: CAA59991.1.
AK039582 mRNA. Translation: BAC30392.1.
AK045686 mRNA. Translation: BAC32457.1.
AK136782 mRNA. Translation: BAE23128.1.
AC154234 Genomic DNA. No translation available.
AC154601 Genomic DNA. No translation available.
CT009561 Genomic DNA. No translation available.
BC021159 mRNA. Translation: AAH21159.1.
CCDSiCCDS28089.1. [Q61730-1]
CCDS49815.1. [Q61730-3]
CCDS57023.1. [Q61730-2]
PIRiA57535.
RefSeqiNP_001152790.1. NM_001159318.1. [Q61730-3]
NP_032390.1. NM_008364.2. [Q61730-1]
NP_598864.1. NM_134103.2. [Q61730-2]
UniGeneiMm.253424.

Genome annotation databases

EnsembliENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514. [Q61730-1]
ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514. [Q61730-3]
ENSMUST00000174202; ENSMUSP00000134202; ENSMUSG00000022514. [Q61730-2]
GeneIDi16180.
KEGGimmu:16180.
UCSCiuc007yve.2. mouse. [Q61730-1]
uc007yvg.2. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85999 mRNA. Translation: CAA59991.1.
AK039582 mRNA. Translation: BAC30392.1.
AK045686 mRNA. Translation: BAC32457.1.
AK136782 mRNA. Translation: BAE23128.1.
AC154234 Genomic DNA. No translation available.
AC154601 Genomic DNA. No translation available.
CT009561 Genomic DNA. No translation available.
BC021159 mRNA. Translation: AAH21159.1.
CCDSiCCDS28089.1. [Q61730-1]
CCDS49815.1. [Q61730-3]
CCDS57023.1. [Q61730-2]
PIRiA57535.
RefSeqiNP_001152790.1. NM_001159318.1. [Q61730-3]
NP_032390.1. NM_008364.2. [Q61730-1]
NP_598864.1. NM_134103.2. [Q61730-2]
UniGeneiMm.253424.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YFDX-ray3.25B21-351[»]
ProteinModelPortaliQ61730.
SMRiQ61730. Positions 24-345, 403-547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200628. 3 interactions.
DIPiDIP-296N.
IntActiQ61730. 3 interactions.

PTM databases

iPTMnetiQ61730.
PhosphoSiteiQ61730.

Proteomic databases

EPDiQ61730.
MaxQBiQ61730.
PRIDEiQ61730.

Protocols and materials databases

DNASUi16180.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514. [Q61730-1]
ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514. [Q61730-3]
ENSMUST00000174202; ENSMUSP00000134202; ENSMUSG00000022514. [Q61730-2]
GeneIDi16180.
KEGGimmu:16180.
UCSCiuc007yve.2. mouse. [Q61730-1]
uc007yvg.2. mouse.

Organism-specific databases

CTDi3556.
MGIiMGI:104975. Il1rap.

Phylogenomic databases

GeneTreeiENSGT00760000119071.
HOGENOMiHOG000092977.
HOVERGENiHBG104298.
InParanoidiQ61730.
KOiK04723.
OMAiKRSHRWS.
PhylomeDBiQ61730.

Enzyme and pathway databases

ReactomeiR-MMU-446652. Interleukin-1 signaling.

Miscellaneous databases

NextBioi289053.
PROiQ61730.
SOURCEiSearch...

Gene expression databases

BgeeiQ61730.
CleanExiMM_IL1RAP.
ExpressionAtlasiQ61730. baseline and differential.
GenevisibleiQ61730. MM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR015621. IL-1_rcpt_fam.
IPR004074. IL-1_rcpt_I/II-typ.
IPR000157. TIR_dom.
[Graphical view]
PANTHERiPTHR11890. PTHR11890. 1 hit.
PfamiPF13895. Ig_2. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PRINTSiPR01536. INTRLKN1R12F.
SMARTiSM00409. IG. 3 hits.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain, Diencephalon and Spinal cord.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: a novel mechanism of regulation of IL-1 responsiveness."
    Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D., Martin M.U.
    J. Immunol. 161:6871-6877(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IL1R2.
  6. "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.
  7. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 527-LYS--PRO-534, INTERACTION WITH MYD88, FUNCTION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRAK2.
  9. "Soluble interleukin-1 receptor accessory protein ameliorates collagen-induced arthritis by a different mode of action from that of interleukin-1 receptor antagonist."
    Smeets R.L., Joosten L.A., Arntz O.J., Bennink M.B., Takahashi N., Carlsen H., Martin M.U., van den Berg W.B., van de Loo F.A.
    Arthritis Rheum. 52:2202-2211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor complex."
    Chackerian A.A., Oldham E.R., Murphy E.E., Schmitz J., Pflanz S., Kastelein R.A.
    J. Immunol. 179:2551-2555(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  11. "IL-1 receptor accessory protein is essential for IL-33-induced activation of T lymphocytes and mast cells."
    Ali S., Huber M., Kollewe C., Bischoff S.C., Falk W., Martin M.U.
    Proc. Natl. Acad. Sci. U.S.A. 104:18660-18665(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IL1RL1.
  12. "The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33."
    Palmer G., Lipsky B.P., Smithgall M.D., Meininger D., Siu S., Talabot-Ayer D., Gabay C., Smith D.E.
    Cytokine 42:358-364(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IL1RL1.
  13. "A central nervous system-restricted isoform of the interleukin-1 receptor accessory protein modulates neuronal responses to interleukin-1."
    Smith D.E., Lipsky B.P., Russell C., Ketchem R.R., Kirchner J., Hensley K., Huang Y., Friedman W.J., Boissonneault V., Plante M.M., Rivest S., Sims J.E.
    Immunity 30:817-831(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY (ISOFORM 3).
  14. Cited for: INTERACTION WITH KIT, SUBUNIT.
  15. Cited for: TISSUE SPECIFICITY.
  16. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IL1RL2, SUBUNIT.
  17. "Neuron-specific effects of interleukin-1beta are mediated by a novel isoform of the IL-1 receptor accessory protein."
    Huang Y., Smith D.E., Ibanez-Sandoval O., Sims J.E., Friedman W.J.
    J. Neurosci. 31:18048-18059(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3), TISSUE SPECIFICITY (ISOFORM 3).
  18. "Interleukin-1R3 mediates interleukin-1-induced potassium current increase through fast activation of Akt kinase."
    Qian J., Zhu L., Li Q., Belevych N., Chen Q., Zhao F., Herness S., Quan N.
    Proc. Natl. Acad. Sci. U.S.A. 109:12189-12194(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 3).

Entry informationi

Entry nameiIL1AP_MOUSE
AccessioniPrimary (citable) accession number: Q61730
Secondary accession number(s): Q3UVZ1, Q8VCB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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 one 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.