IL1AP_MOUSE
ID IL1AP_MOUSE Reviewed; 570 AA.
AC Q61730; Q3UVZ1; Q8VCB9;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Interleukin-1 receptor accessory protein;
DE Short=IL-1 receptor accessory protein;
DE Short=IL-1RAcP;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Interleukin-33 receptot beta chain {ECO:0000303|PubMed:18003919};
DE Flags: Precursor;
GN Name=Il1rap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH IL1R1,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=7775431; DOI=10.1074/jbc.270.23.13757;
RA Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.;
RT "Molecular cloning and characterization of a second subunit of the
RT interleukin 1 receptor complex.";
RL J. Biol. Chem. 270:13757-13765(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, Diencephalon, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH IL1R2.
RX PubMed=9862719;
RA Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
RA Martin M.U.;
RT "The type II IL-1 receptor interacts with the IL-1 receptor accessory
RT protein: a novel mechanism of regulation of IL-1 responsiveness.";
RL J. Immunol. 161:6871-6877(1998).
RN [6]
RP INTERACTION WITH TOLLIP.
RX PubMed=10854325; DOI=10.1038/35014038;
RA Burns K., Clatworthy J., Martin L., Martinon F., Plumpton C., Maschera B.,
RA Lewis A., Ray K., Tschopp J., Volpe F.;
RT "Tollip, a new component of the IL-1R1 pathway, links IRAK to the IL-1
RT receptor.";
RL Nat. Cell Biol. 2:346-351(2000).
RN [7]
RP MUTAGENESIS OF 527-LYS--PRO-534, INTERACTION WITH MYD88, AND FUNCTION.
RX PubMed=11880380; DOI=10.1074/jbc.m201000200;
RA Radons J., Gabler S., Wesche H., Korherr C., Hofmeister R., Falk W.;
RT "Identification of essential regions in the cytoplasmic tail of
RT interleukin-1 receptor accessory protein critical for interleukin-1
RT signaling.";
RL J. Biol. Chem. 277:16456-16463(2002).
RN [8]
RP INTERACTION WITH IRAK2.
RX PubMed=12659850; DOI=10.1016/s0006-291x(03)00385-1;
RA Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S.,
RA Auron P.E.;
RT "Characterization of a cascade of protein interactions initiated at the IL-
RT 1 receptor.";
RL Biochem. Biophys. Res. Commun. 303:525-531(2003).
RN [9]
RP FUNCTION.
RX PubMed=15986350; DOI=10.1002/art.21108;
RA Smeets R.L., Joosten L.A., Arntz O.J., Bennink M.B., Takahashi N.,
RA Carlsen H., Martin M.U., van den Berg W.B., van de Loo F.A.;
RT "Soluble interleukin-1 receptor accessory protein ameliorates collagen-
RT induced arthritis by a different mode of action from that of interleukin-1
RT receptor antagonist.";
RL Arthritis Rheum. 52:2202-2211(2005).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17675517; DOI=10.4049/jimmunol.179.4.2551;
RA Chackerian A.A., Oldham E.R., Murphy E.E., Schmitz J., Pflanz S.,
RA Kastelein R.A.;
RT "IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor
RT complex.";
RL J. Immunol. 179:2551-2555(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH IL1RL1.
RX PubMed=18003919; DOI=10.1073/pnas.0705939104;
RA Ali S., Huber M., Kollewe C., Bischoff S.C., Falk W., Martin M.U.;
RT "IL-1 receptor accessory protein is essential for IL-33-induced activation
RT of T lymphocytes and mast cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18660-18665(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH IL1RL1.
RX PubMed=18450470; DOI=10.1016/j.cyto.2008.03.008;
RA Palmer G., Lipsky B.P., Smithgall M.D., Meininger D., Siu S.,
RA Talabot-Ayer D., Gabay C., Smith D.E.;
RT "The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling
RT and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33.";
RL Cytokine 42:358-364(2008).
RN [13]
RP ALTERNATIVE SPLICING (ISOFORM 3), AND TISSUE SPECIFICITY (ISOFORM 3).
RX PubMed=19481478; DOI=10.1016/j.immuni.2009.03.020;
RA Smith D.E., Lipsky B.P., Russell C., Ketchem R.R., Kirchner J., Hensley K.,
RA Huang Y., Friedman W.J., Boissonneault V., Plante M.M., Rivest S.,
RA Sims J.E.;
RT "A central nervous system-restricted isoform of the interleukin-1 receptor
RT accessory protein modulates neuronal responses to interleukin-1.";
RL Immunity 30:817-831(2009).
RN [14]
RP INTERACTION WITH KIT, AND SUBUNIT.
RX PubMed=20200353; DOI=10.1182/blood-2009-10-247411;
RA Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A.,
RA Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D.,
RA Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.;
RT "The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in
RT mast cells.";
RL Blood 115:3899-3906(2010).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=21349253; DOI=10.1016/j.brainres.2011.02.045;
RA Yasuoka S., Kawanokuchi J., Parajuli B., Jin S., Doi Y., Noda M.,
RA Sonobe Y., Takeuchi H., Mizuno T., Suzumura A.;
RT "Production and functions of IL-33 in the central nervous system.";
RL Brain Res. 1385:8-17(2011).
RN [16]
RP INTERACTION WITH IL1RL2, AND SUBUNIT.
RX PubMed=21965679; DOI=10.1074/jbc.m111.267922;
RA Towne J.E., Renshaw B.R., Douangpanya J., Lipsky B.P., Shen M., Gabel C.A.,
RA Sims J.E.;
RT "Interleukin-36 (IL-36) ligands require processing for full agonist (IL-
RT 36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity.";
RL J. Biol. Chem. 286:42594-42602(2011).
RN [17]
RP FUNCTION (ISOFORM 3), AND TISSUE SPECIFICITY (ISOFORM 3).
RX PubMed=22159118; DOI=10.1523/jneurosci.4067-11.2011;
RA Huang Y., Smith D.E., Ibanez-Sandoval O., Sims J.E., Friedman W.J.;
RT "Neuron-specific effects of interleukin-1beta are mediated by a novel
RT isoform of the IL-1 receptor accessory protein.";
RL J. Neurosci. 31:18048-18059(2011).
RN [18]
RP FUNCTION (ISOFORM 3).
RX PubMed=22778412; DOI=10.1073/pnas.1205207109;
RA Qian J., Zhu L., Li Q., Belevych N., Chen Q., Zhao F., Herness S., Quan N.;
RT "Interleukin-1R3 mediates interleukin-1-induced potassium current increase
RT through fast activation of Akt kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12189-12194(2012).
RN [19] {ECO:0007744|PDB:4YFD}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 21-351 IN COMPLEX WITH PTPRD,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-57; ASN-107; ASN-111; ASN-118 AND
RP ASN-209, INTERACTION WITH PTPRD, FUNCTION, MUTAGENESIS OF TRP-27; ASP-30;
RP 69-ILE--TYR-71; 82-PRO--PHE-85 AND LYS-94, AND REGION.
RX PubMed=25908590; DOI=10.1038/ncomms7926;
RA Yamagata A., Yoshida T., Sato Y., Goto-Ito S., Uemura T., Maeda A.,
RA Shiroshima T., Iwasawa-Okamoto S., Mori H., Mishina M., Fukai S.;
RT "Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-
RT IL1RAPL1/IL-1RAcP for synaptic differentiation.";
RL Nat. Commun. 6:6926-6926(2015).
CC -!- FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system.
CC Coreceptor with IL1R1 in the IL-1 signaling system. Associates with
CC IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor
CC complex which mediates interleukin-1-dependent activation of NF-kappa-B
CC and other pathways. Signaling involves the recruitment of adapter
CC molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective
CC TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the
CC signaling complex. Does not bind to interleukin-1 alone; binding of
CC IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling
CC complex. The cellular response is modulated through a non-signaling
CC association with the membrane IL1R2 decoy receptor. Secreted forms
CC (isoforms 2 and 3) associate with secreted ligand-bound IL1R2 and
CC increase the affinity of secreted IL1R2 for IL1B; this complex
CC formation may be the dominant mechanism for neutralization of IL1B by
CC secreted/soluble receptors. Coreceptor for IL1RL1 in the IL-33
CC signaling system. Can bidirectionally induce pre- and postsynaptic
CC differentiation of neurons by trans-synaptically binding to PTPRD
CC (PubMed:25908590). May play a role in IL1B-mediated costimulation of
CC IFNG production from T-helper 1 (Th1) cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPH3, ECO:0000269|PubMed:11880380,
CC ECO:0000269|PubMed:15986350, ECO:0000269|PubMed:17675517,
CC ECO:0000269|PubMed:18003919, ECO:0000269|PubMed:18450470,
CC ECO:0000269|PubMed:25908590, ECO:0000303|PubMed:21965679}.
CC -!- FUNCTION: [Isoform 2]: Associates with secreted ligand-bound IL1R2 and
CC increases the affinity of secreted IL1R2 for IL1B; this complex
CC formation may be the dominant mechanism for neutralization of IL1B by
CC secreted/soluble receptors. Enhances the ability of secreted IL1R1 to
CC inhibit IL-33 signaling. {ECO:0000269|PubMed:15986350,
CC ECO:0000269|PubMed:18450470}.
CC -!- FUNCTION: [Isoform 3]: Required for Src phosphorylation by IL1B.
CC Required for IL1B-potentiated NMDA-induced calcium influx in neurons
CC acting in cooperation with IL1R1 isoform 2 to mediate Akt kinase
CC activation. {ECO:0000269|PubMed:22159118, ECO:0000269|PubMed:22778412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: The interleukin-36 receptor complex is a heterodimer of IL1RL2
CC and IL1RAP; the association is inhibited by IL36RN. The interleukin-1
CC receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with
CC IL1R2 to form a non-signaling interleukin-1 receptor complex. Interacts
CC with IL-33-bound IL1RL1 to form the minimal interleukin-33 signaling
CC complex with a 1:1:1 stoichiometry. Interacts with KIT (independently
CC of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced
CC interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and
CC MYD88. Interacts (via the first immunoglobilin domain) with PTPRD (via
CC the third immunoglobilin domain); induces pre- and postsynaptic
CC differentiation of neurons (PubMed:25908590).
CC {ECO:0000269|PubMed:17675517, ECO:0000269|PubMed:18003919,
CC ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:21965679,
CC ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:9862719}.
CC -!- INTERACTION:
CC Q61730; P14719: Il1rl1; NbExp=3; IntAct=EBI-525035, EBI-525078;
CC Q61730; Q9QZ06: Tollip; NbExp=2; IntAct=EBI-525035, EBI-74272;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=MuIL-1R AcP;
CC IsoId=Q61730-1; Sequence=Displayed;
CC Name=2; Synonyms=SmuIL-1R AcP;
CC IsoId=Q61730-2; Sequence=VSP_008054, VSP_008055;
CC Name=3; Synonyms=IL-1RAcPb;
CC IsoId=Q61730-3; Sequence=VSP_058171;
CC -!- TISSUE SPECIFICITY: Detected in lung, brain, spleen, thymus and liver.
CC Expressed in brain endothelial cells, astrocytes, microglia and
CC neurons. Isoform 3 is predominantly expressed in brain; expressed in
CC hippocampal neurons. {ECO:0000269|PubMed:19481478,
CC ECO:0000269|PubMed:21349253, ECO:0000269|PubMed:22159118,
CC ECO:0000269|PubMed:7775431}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X85999; CAA59991.1; -; mRNA.
DR EMBL; AK039582; BAC30392.1; -; mRNA.
DR EMBL; AK045686; BAC32457.1; -; mRNA.
DR EMBL; AK136782; BAE23128.1; -; mRNA.
DR EMBL; AC154234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021159; AAH21159.1; -; mRNA.
DR CCDS; CCDS28089.1; -. [Q61730-1]
DR CCDS; CCDS49815.1; -. [Q61730-3]
DR CCDS; CCDS57023.1; -. [Q61730-2]
DR PIR; A57535; A57535.
DR RefSeq; NP_001152790.1; NM_001159318.1. [Q61730-3]
DR RefSeq; NP_032390.1; NM_008364.2. [Q61730-1]
DR RefSeq; NP_598864.1; NM_134103.2. [Q61730-2]
DR PDB; 4YFD; X-ray; 3.25 A; B=21-351.
DR PDB; 5VI4; X-ray; 2.79 A; C/F=21-350.
DR PDBsum; 4YFD; -.
DR PDBsum; 5VI4; -.
DR AlphaFoldDB; Q61730; -.
DR SMR; Q61730; -.
DR BioGRID; 200628; 5.
DR CORUM; Q61730; -.
DR DIP; DIP-296N; -.
DR IntAct; Q61730; 3.
DR GlyGen; Q61730; 7 sites.
DR iPTMnet; Q61730; -.
DR PhosphoSitePlus; Q61730; -.
DR CPTAC; non-CPTAC-3320; -.
DR EPD; Q61730; -.
DR jPOST; Q61730; -.
DR MaxQB; Q61730; -.
DR PeptideAtlas; Q61730; -.
DR PRIDE; Q61730; -.
DR ProteomicsDB; 269469; -. [Q61730-1]
DR ProteomicsDB; 269470; -. [Q61730-2]
DR ProteomicsDB; 269471; -. [Q61730-3]
DR ABCD; Q61730; 22 sequenced antibodies.
DR Antibodypedia; 19361; 386 antibodies from 38 providers.
DR DNASU; 16180; -.
DR Ensembl; ENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514. [Q61730-1]
DR Ensembl; ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514. [Q61730-3]
DR Ensembl; ENSMUST00000174202; ENSMUSP00000134202; ENSMUSG00000022514. [Q61730-2]
DR GeneID; 16180; -.
DR KEGG; mmu:16180; -.
DR UCSC; uc007yve.2; mouse. [Q61730-1]
DR UCSC; uc007yvg.2; mouse.
DR CTD; 3556; -.
DR MGI; MGI:104975; Il1rap.
DR VEuPathDB; HostDB:ENSMUSG00000022514; -.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_3_2_1; -.
DR InParanoid; Q61730; -.
DR OMA; KRSHRWS; -.
DR PhylomeDB; Q61730; -.
DR TreeFam; TF325519; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9014826; Interleukin-36 pathway.
DR Reactome; R-MMU-9014843; Interleukin-33 signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR BioGRID-ORCS; 16180; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Il1rap; mouse.
DR PRO; PR:Q61730; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61730; protein.
DR Bgee; ENSMUSG00000022514; Expressed in left lobe of liver and 213 other tissues.
DR ExpressionAtlas; Q61730; baseline and differential.
DR Genevisible; Q61730; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IDA:MGI.
DR GO; GO:0005149; F:interleukin-1 receptor binding; ISO:MGI.
DR GO; GO:0002114; F:interleukin-33 receptor activity; IMP:UniProtKB.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0038172; P:interleukin-33-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; IDA:SynGO.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunity; Immunoglobulin domain;
KW Inflammatory response; Innate immunity; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..570
FT /note="Interleukin-1 receptor accessory protein"
FT /id="PRO_0000015452"
FT TOPO_DOM 21..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 139..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 243..348
FT /note="Ig-like C2-type 3"
FT DOMAIN 403..546
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 69..85
FT /note="Essential for interaction with PTPRD"
FT /evidence="ECO:0000269|PubMed:25908590"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YFD"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YFD"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YFD"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YFD"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YFD"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YFD"
FT DISULFID 47..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YFD"
FT DISULFID 137..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YFD"
FT DISULFID 160..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YFD"
FT DISULFID 266..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YFD"
FT VAR_SEQ 351..359
FT /note="VIPPRYTVE -> GNGCTEPMTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7775431"
FT /id="VSP_008054"
FT VAR_SEQ 360..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7775431"
FT /id="VSP_008055"
FT VAR_SEQ 449..570
FT /note="IVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVIL
FT VQYKAVKDMKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRWSSNDK
FT QGLSYSSLKNV -> NTVEAVFDFIQRSRRMIVVLSPDYVTEKSISMLEFKLGVMCQNS
FT IATKLIVVEYRPLEQPHPGIMQLKESVSFVSWKGEKSKHSGSKFWKALRLALPLRSLSA
FT SSGWNESCSSQSDISLDHVQRRSRLKEPPELRSSERVSGAEPAPGTMSKHRGKPSAACR
FT CCVTYCEGESHLRSKSRAEMHTHPQWETHLCKPPLQESESQWIQNGTRPEPAPQISALA
FT LRHFTDLSNNNDFYIL (in isoform 3)"
FT /id="VSP_058171"
FT MUTAGEN 27
FT /note="W->A: Reduces affinity for PTPRD."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 30
FT /note="D->A: Does not affect affinity for PTPRD."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 69..71
FT /note="IWY->AWA: Abolishes interaction with PTPRD; when
FT associates with 82-A--A-85. Significantly reduces
FT synaptogenesis; when associates with 82-A--A-85."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 82..85
FT /note="PINF->AINA: Abolishes interaction with PTPRD; when
FT associates with 69-A--A-71 Significantly reduces
FT synaptogenesis; when associates with 82-A--A-85."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 94
FT /note="K->A: Reduces affinity for PTPRD."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 527..534
FT /note="KGEKSKYP->AAAAAAAA: Abolishes interaction with MYD88
FT and IL-1-dependent activation of NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:11880380"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4YFD"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4YFD"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:5VI4"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4YFD"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:4YFD"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:5VI4"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:5VI4"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:5VI4"
SQ SEQUENCE 570 AA; 65741 MW; 4D4B07E0310AFDC5 CRC64;
MGLLWYLMSL SFYGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKYNYST
AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT
YCSKVAFPLE VVQKDSCFNS AMRFPVHKMY IEHGIHKITC PNVDGYFPSS VKPSVTWYKG
CTEIVDFHNV LPEGMNLSFF IPLVSNNGNY TCVVTYPENG RLFHLTRTVT VKVVGSPKDA
LPPQIYSPND RVVYEKEPGE ELVIPCKVYF SFIMDSHNEV WWTIDGKKPD DVTVDITINE
SVSYSSTEDE TRTQILSIKK VTPEDLRRNY VCHARNTKGE AEQAAKVKQK VIPPRYTVEL
ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNVEEEEF
VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL
LELKAGLENM ASRGNINVIL VQYKAVKDMK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK
QLQVAMPVKK SPRWSSNDKQ GLSYSSLKNV
