IL1R1_MOUSE
ID IL1R1_MOUSE Reviewed; 576 AA.
AC P13504;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Interleukin-1 receptor type 1;
DE Short=IL-1R-1;
DE Short=IL-1RT-1;
DE Short=IL-1RT1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=CD121 antigen-like family member A;
DE AltName: Full=Interleukin-1 receptor alpha;
DE Short=IL-1R-alpha;
DE AltName: Full=Interleukin-1 receptor type I;
DE AltName: Full=p80;
DE AltName: CD_antigen=CD121a;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 1, membrane form;
DE Short=mIL-1R1;
DE Short=mIL-1RI;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 1, soluble form;
DE Short=sIL-1R1;
DE Short=sIL-1RI;
DE Flags: Precursor;
GN Name=Il1r1; Synonyms=Il-1r1, Il1ra;
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], AND PROTEIN SEQUENCE OF 20-45.
RX PubMed=2969618; DOI=10.1126/science.2969618;
RA Sims J.E., March C.J., Cosman D., Widmer M.B., McDonald H.R., McMahan C.J.,
RA Grubin C.E., Wignall J.M., Jackson J.L., Call S.M., Friend D., Alpert A.R.,
RA Gillis S., Urdal D.L., Dower S.K.;
RT "cDNA expression cloning of the IL-1 receptor, a member of the
RT immunoglobulin superfamily.";
RL Science 241:585-589(1988).
RN [2]
RP PHOSPHORYLATION AT THR-556.
RX PubMed=1828344; DOI=10.1016/0006-291x(91)91948-c;
RA Bird T.A., Woodward A., Jackson J.L., Dower S.K., Sims J.E.;
RT "Phorbol ester induces phosphorylation of the 80 kilodalton murine
RT interleukin 1 receptor at a single threonine residue.";
RL Biochem. Biophys. Res. Commun. 177:61-67(1991).
RN [3]
RP INTERACTION WITH IL1RAP.
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 [4]
RP INTERACTION WITH TOLLIP; MYD88 AND IRAK1.
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 [5]
RP FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
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 [6]
RP 3D-STRUCTURE MODELING OF 25-334.
RX PubMed=15062642; DOI=10.1016/j.dci.2003.09.014;
RA Scapigliati G., Costantini S., Colonna G., Facchiano A., Buonocore F.,
RA Bossu P., Cunningham C., Holland J.W., Secombes C.J.;
RT "Modelling of fish interleukin-1 and its receptor.";
RL Dev. Comp. Immunol. 28:429-441(2004).
CC -!- FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to
CC interleukin-1 associates with the coreceptor IL1RAP to form the high
CC affinity interleukin-1 receptor complex which mediates interleukin-1-
CC dependent activation of NF-kappa-B, MAPK and other pathways. Signaling
CC involves the recruitment of adapter molecules such as TOLLIP, MYD88,
CC and IRAK1 or IRAK2 via the respective TIR domains of the
CC receptor/coreceptor subunits. Binds ligands with comparable affinity
CC and binding of antagonist IL1RN prevents association with IL1RAP to
CC form a signaling complex. Involved in IL1B-mediated costimulation of
CC IFNG production from T-helper 1 (Th1) cells (By similarity).
CC {ECO:0000250|UniProtKB:P14778}.
CC -!- FUNCTION: [Isoform 2]: Unable to mediate canonical IL-1 signaling.
CC Cooperates with IL1RAP isoform 3 to mediate IL1B-induced neuronal
CC activity including IL1B-potentiated NMDA-induced calcium influx
CC mediated by Akt kinase activation. {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-1 receptor complex is a heterodimer of IL1R1
CC and IL1RAP. Interacts with PIK3R1. Interacts with IL1A (By similarity).
CC {ECO:0000250|UniProtKB:P14778}.
CC -!- INTERACTION:
CC P13504; P22366: Myd88; NbExp=2; IntAct=EBI-1782675, EBI-525108;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000305}. Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P13504-1; Sequence=Displayed;
CC Name=2; Synonyms=IL-1R3;
CC IsoId=P13504-2; Sequence=VSP_058170;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in various brain tissues.
CC {ECO:0000269|PubMed:22778412}.
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 -!- PTM: A soluble form (sIL1R1) is probably produced by proteolytic
CC cleavage at the cell surface (shedding). {ECO:0000250}.
CC -!- PTM: Rapidly phosphorylated on Tyr-499 in response to IL-1, which
CC creates a SH2 binding site for the PI 3-kinase regulatory subunit
CC PIK3R1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; M20658; AAA39279.1; -; mRNA.
DR CCDS; CCDS35547.1; -. [P13504-1]
DR PIR; A32604; A32604.
DR RefSeq; NP_032388.1; NM_008362.2. [P13504-1]
DR RefSeq; XP_006495776.1; XM_006495713.2. [P13504-1]
DR AlphaFoldDB; P13504; -.
DR SMR; P13504; -.
DR BioGRID; 200625; 6.
DR DIP; DIP-40669N; -.
DR IntAct; P13504; 5.
DR STRING; 10090.ENSMUSP00000027241; -.
DR ChEMBL; CHEMBL2189148; -.
DR GlyGen; P13504; 7 sites.
DR iPTMnet; P13504; -.
DR PhosphoSitePlus; P13504; -.
DR PaxDb; P13504; -.
DR PRIDE; P13504; -.
DR ProteomicsDB; 267122; -. [P13504-1]
DR ProteomicsDB; 267123; -. [P13504-2]
DR Antibodypedia; 3576; 980 antibodies from 41 providers.
DR DNASU; 16177; -.
DR Ensembl; ENSMUST00000027241; ENSMUSP00000027241; ENSMUSG00000026072. [P13504-1]
DR GeneID; 16177; -.
DR KEGG; mmu:16177; -.
DR UCSC; uc007atv.1; mouse. [P13504-1]
DR CTD; 3554; -.
DR MGI; MGI:96545; Il1r1.
DR VEuPathDB; HostDB:ENSMUSG00000026072; -.
DR eggNOG; ENOG502QWEU; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR InParanoid; P13504; -.
DR OMA; EISGFSW; -.
DR PhylomeDB; P13504; -.
DR TreeFam; TF325519; -.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR BioGRID-ORCS; 16177; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Il1r1; mouse.
DR PRO; PR:P13504; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P13504; protein.
DR Bgee; ENSMUSG00000026072; Expressed in islet of Langerhans and 170 other tissues.
DR ExpressionAtlas; P13504; baseline and differential.
DR Genevisible; P13504; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019966; F:interleukin-1 binding; IPI:MGI.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IDA:UniProtKB.
DR GO; GO:0004909; F:interleukin-1, type I, activating receptor activity; IEA:InterPro.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
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:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0010286; P:heat acclimation; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:2000661; P:positive regulation of interleukin-1-mediated signaling pathway; IMP:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IMP:MGI.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0009314; P:response to radiation; ISO:MGI.
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; IPR004076; IL-1_rcpt_I-typ.
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; PR01538; INTRLEUKN1R1.
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; 3.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Inflammatory response; Membrane; NAD; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2969618"
FT CHAIN 20..576
FT /note="Interleukin-1 receptor type 1, membrane form"
FT /id="PRO_0000015436"
FT CHAIN 20..?
FT /note="Interleukin-1 receptor type 1, soluble form"
FT /id="PRO_0000415345"
FT TOPO_DOM 20..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..213
FT /note="Ig-like C2-type 2"
FT DOMAIN 229..329
FT /note="Ig-like C2-type 3"
FT DOMAIN 386..541
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14778"
FT MOD_RES 556
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:1828344"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 46..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 251..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..200
FT /note="Missing (in isoform 2)"
FT /id="VSP_058170"
SQ SEQUENCE 576 AA; 66698 MW; 7AA8304C86412A16 CRC64;
MENMKVLLGL ICLMVPLLSL EIDVCTEYPN QIVLFLSVNE IDIRKCPLTP NKMHGDTIIW
YKNDSKTPIS ADRDSRIHQQ NEHLWFVPAK VEDSGYYYCI VRNSTYCLKT KVTVTVLEND
PGLCYSTQAT FPQRLHIAGD GSLVCPYVSY FKDENNELPE VQWYKNCKPL LLDNVSFFGV
KDKLLVRNVA EEHRGDYICR MSYTFRGKQY PVTRVIQFIT IDENKRDRPV ILSPRNETIE
ADPGSMIQLI CNVTGQFSDL VYWKWNGSEI EWNDPFLAED YQFVEHPSTK RKYTLITTLN
ISEVKSQFYR YPFICVVKNT NIFESAHVQL IYPVPDFKNY LIGGFIILTA TIVCCVCIYK
VFKVDIVLWY RDSCSGFLPS KASDGKTYDA YILYPKTLGE GSFSDLDTFV FKLLPEVLEG
QFGYKLFIYG RDDYVGEDTI EVTNENVKKS RRLIIILVRD MGGFSWLGQS SEEQIAIYNA
LIQEGIKIVL LELEKIQDYE KMPDSIQFIK QKHGVICWSG DFQERPQSAK TRFWKNLRYQ
MPAQRRSPLS KHRLLTLDPV RDTKEKLPAA THLPLG
