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   11-NOV-2015, entry version 159.
DE   RecName: Full=Interleukin-1 receptor type 1;
DE            Short=IL-1R-1;
DE            Short=IL-1RT-1;
DE            Short=IL-1RT1;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   McMahan C.J., Grubin C.E., Wignall J.M., Jackson J.L., Call S.M.,
RA   Friend D., Alpert A.R., 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.,
RA   Maschera B., 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   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 corecptor IL1RAP to form the
CC       high affinity interleukin-1 receptor complex which mediates
CC       interleukin-1-dependent activation of NF-kappa-B, MAPK and other
CC       pathways. Signaling involves the recruitment of adapter molecules
CC       such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR
CC       domains of the receptor/coreceptor subunits. Binds ligands with
CC       comparable affinity and binding of antagonist IL1RN prevents
CC       association with IL1RAP to form a signaling complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The interleukin-1 receptor complex is a heterodimer of
CC       IL1R1 and IL1RAP. Interacts with PIK3R1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cell membrane {ECO:0000305}. Secreted {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 TIR domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00204}.
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DR   EMBL; M20658; AAA39279.1; -; mRNA.
DR   CCDS; CCDS35547.1; -.
DR   PIR; A32604; A32604.
DR   RefSeq; NP_032388.1; NM_008362.2.
DR   RefSeq; XP_006495776.1; XM_006495713.2.
DR   UniGene; Mm.896; -.
DR   PDB; 1OU3; Model; -; A=25-334.
DR   PDBsum; 1OU3; -.
DR   ProteinModelPortal; P13504; -.
DR   SMR; P13504; 25-334, 386-542.
DR   BioGrid; 200625; 6.
DR   DIP; DIP-40669N; -.
DR   IntAct; P13504; 5.
DR   STRING; 10090.ENSMUSP00000027241; -.
DR   ChEMBL; CHEMBL2189148; -.
DR   PhosphoSite; P13504; -.
DR   PaxDb; P13504; -.
DR   PRIDE; P13504; -.
DR   Ensembl; ENSMUST00000027241; ENSMUSP00000027241; ENSMUSG00000026072.
DR   GeneID; 16177; -.
DR   UCSC; uc007atv.1; mouse.
DR   CTD; 3554; -.
DR   MGI; MGI:96545; Il1r1.
DR   eggNOG; ENOG410IQBC; Eukaryota.
DR   eggNOG; ENOG410Z3W1; LUCA.
DR   HOGENOM; HOG000253916; -.
DR   HOVERGEN; HBG052103; -.
DR   InParanoid; P13504; -.
DR   OMA; IQDYEKM; -.
DR   OrthoDB; EOG7H1JK3; -.
DR   PhylomeDB; P13504; -.
DR   TreeFam; TF325519; -.
DR   Reactome; R-MMU-446652; Interleukin-1 signaling.
DR   NextBio; 289041; -.
DR   PRO; PR:P13504; -.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; P13504; -.
DR   CleanEx; MM_IL1R1; -.
DR   ExpressionAtlas; P13504; baseline and differential.
DR   Genevisible; P13504; MM.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0004908; F:interleukin-1 receptor activity; IDA:MGI.
DR   GO; GO:0004909; F:interleukin-1, Type I, activating receptor activity; IEA:InterPro.
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:0004871; F:signal transducer activity; IDA:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0010286; P:heat acclimation; IEA:Ensembl.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0070849; P:response to epidermal growth factor; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR   GO; GO:0071731; P:response to nitric oxide; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR   GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.40.50.10140; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
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; IPR000157; TIR_dom.
DR   PANTHER; PTHR11890; PTHR11890; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR01538; INTRLEUKN1R1.
DR   PRINTS; PR01536; INTRLKN1R12F.
DR   SMART; SM00409; IG; 2.
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   3D-structure; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:2969618}.
FT   CHAIN        20    576       Interleukin-1 receptor type 1, membrane
FT                                form.
FT                                /FTId=PRO_0000015436.
FT   CHAIN        20      ?       Interleukin-1 receptor type 1, soluble
FT                                form.
FT                                /FTId=PRO_0000415345.
FT   TOPO_DOM     20    338       Extracellular. {ECO:0000255}.
FT   TRANSMEM    339    359       Helical. {ECO:0000255}.
FT   TOPO_DOM    360    576       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    115       Ig-like C2-type 1.
FT   DOMAIN      121    213       Ig-like C2-type 2.
FT   DOMAIN      229    329       Ig-like C2-type 3.
FT   DOMAIN      386    544       TIR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00204}.
FT   MOD_RES     499    499       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P14778}.
FT   MOD_RES     556    556       Phosphothreonine; by PKC.
FT                                {ECO:0000269|PubMed:1828344}.
FT   CARBOHYD     63     63       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    252    252       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    266    266       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    300    300       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     25    107       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID     46     99       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    145    199       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    251    315       {ECO:0000255|PROSITE-ProRule:PRU00114}.
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
//