ID IL1R1_HUMAN Reviewed; 569 AA. AC P14778; Q587I7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 09-APR-2025, entry version 248. 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=IL1R, IL1RA, IL1RT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=2532321; DOI=10.1093/nar/17.23.10114; RA Chua A.O., Gubler U.; RT "Sequence of the cDNA for the human fibroblast type interleukin-1 RT receptor."; RL Nucleic Acids Res. 17:10114-10114(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=T-cell; RX PubMed=2530587; DOI=10.1073/pnas.86.22.8946; RA Sims J.E., Acres R.B., Grubin C.E., McMahan C.J., Wignall J.M., March C.J., RA Dower S.K.; RT "Cloning the interleukin 1 receptor from human T cells."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8946-8950(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-124. RG SeattleSNPs variation discovery resource; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [7] RP FUNCTION, AND INTERACTION WITH IL1A. RX PubMed=2950091; DOI=10.1016/s0021-9258(18)61450-4; RA Mosley B., Urdal D.L., Prickett K.S., Larsen A., Cosman D., Conlon P.J., RA Gillis S., Dower S.K.; RT "The interleukin-1 receptor binds the human interleukin-1 alpha precursor RT but not the interleukin-1 beta precursor."; RL J. Biol. Chem. 262:2941-2944(1987). RN [8] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING. RX PubMed=8142597; DOI=10.1016/1043-4666(93)90032-z; RA Svenson M., Hansen M.B., Heegaard P., Abell K., Bendtzen K.; RT "Specific binding of interleukin 1 (IL-1) beta and IL-1 receptor antagonist RT (IL-1ra) to human serum. High-affinity binding of IL-1ra to soluble IL-1 RT receptor type I."; RL Cytokine 5:427-435(1993). RN [9] RP LIGAND-BINDING. RX PubMed=7989776; RA Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J., RA Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.; RT "Elevated levels of shed type II IL-1 receptor in sepsis. Potential role RT for type II receptor in regulation of IL-1 responses."; RL J. Immunol. 153:5802-5809(1994). RN [10] RP INTERACTION WITH IL1RAP AND IRAK1. RC TISSUE=Placenta; RX PubMed=9371760; DOI=10.1073/pnas.94.24.12829; RA Huang J., Gao X., Li S., Cao Z.; RT "Recruitment of IRAK to the interleukin 1 receptor complex requires RT interleukin 1 receptor accessory protein."; RL Proc. Natl. Acad. Sci. U.S.A. 94:12829-12832(1997). RN [11] RP PHOSPHORYLATION AT TYR-496, AND INTERACTION WITH PIK3R1. RX PubMed=9821957; DOI=10.1016/s0014-5793(98)01270-8; RA Marmiroli S., Bavelloni A., Faenza I., Sirri A., Ognibene A., Cenni V., RA Tsukada J., Koyama Y., Ruzzene M., Ferri A., Auron P.E., Toker A., RA Maraldi N.M.; RT "Phosphatidylinositol 3-kinase is recruited to a specific site in the RT activated IL-1 receptor I."; RL FEBS Lett. 438:49-54(1998). RN [12] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=10653850; DOI=10.1093/intimm/12.2.151; RA Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K., Hada T., RA Okamura H., Nakanishi K.; RT "IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from RT human T cells."; RL Int. Immunol. 12:151-160(2000). RN [13] RP FUNCTION, AND MUTAGENESIS OF ASP-369 AND ARG-428. RX PubMed=10671496; DOI=10.1074/jbc.275.7.4670; RA Slack J.L., Schooley K., Bonnert T.P., Mitcham J.L., Qwarnstrom E.E., RA Sims J.E., Dower S.K.; RT "Identification of two major sites in the type I interleukin-1 receptor RT cytoplasmic region responsible for coupling to pro-inflammatory signaling RT pathways."; RL J. Biol. Chem. 275:4670-4678(2000). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-332 IN COMPLEX WITH IL1B. RX PubMed=9062193; DOI=10.1038/386190a0; RA Vigers G.P.A., Anderson L.J., Caffes P., Brandhuber B.J.; RT "Crystal structure of the type-I interleukin-1 receptor complexed with RT interleukin-1beta."; RL Nature 386:190-194(1997). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-331 IN COMPLEX WITH IL1RA. RX PubMed=9062194; DOI=10.1038/386194a0; RA Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., RA Akeson A., Bowlin T., Yanofsky S., Barrett R.W.; RT "A new cytokine-receptor binding mode revealed by the crystal structure of RT the IL-1 receptor with an antagonist."; RL Nature 386:194-200(1997). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 4-315 IN COMPLEX WITH THE RP ANTAGONIST PEPTIDE AF10847. RX PubMed=10903327; DOI=10.1074/jbc.m006071200; RA Vigers G.P.A., Dripps D.J., Edwards C.K. III, Brandhuber B.J.; RT "X-ray crystal structure of a small antagonist peptide bound to RT interleukin-1 receptor type 1."; RL J. Biol. Chem. 275:36927-36933(2000). RN [17] RP VARIANT CRMO3 GLU-131, CHARACTERIZATION OF VARIANT CRMO3 GLU-131, RP INVOLVEMENT IN CRMO3, FUNCTION, AND MUTAGENESIS OF LYS-131. RX PubMed=37315560; DOI=10.1016/j.immuni.2023.05.014; RA Wang Y., Wang J., Zheng W., Zhang J., Wang J., Jin T., Tao P., Wang Y., RA Liu C., Huang J., Lee P.Y., Yu X., Zhou Q.; RT "Identification of an IL-1 receptor mutation driving autoinflammation RT directs IL-1-targeted drug design."; RL Immunity 56:1485-1501(2023). CC -!- FUNCTION: Receptor for IL1A, IL1B and IL1RN (PubMed:2950091, CC PubMed:37315560). After binding to interleukin-1 associates with the CC coreceptor IL1RAP to form the high affinity interleukin-1 receptor CC complex which mediates interleukin-1-dependent activation of NF-kappa- CC B, MAPK and other pathways. Signaling involves the recruitment of CC adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the CC respective TIR domains of the receptor/coreceptor subunits. Binds CC ligands with comparable affinity and binding of antagonist IL1RN CC prevents association with IL1RAP to form a signaling complex. Involved CC in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) CC cells (PubMed:10653850). {ECO:0000269|PubMed:10653850, CC ECO:0000269|PubMed:10671496, ECO:0000269|PubMed:2950091, CC ECO:0000269|PubMed:37315560}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + H2O = ADP-D-ribose + nicotinamide + H(+); 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 CC (PubMed:2950091). {ECO:0000269|PubMed:10903327, CC ECO:0000269|PubMed:2950091, ECO:0000269|PubMed:9062193, CC ECO:0000269|PubMed:9062194, ECO:0000269|PubMed:9371760, CC ECO:0000269|PubMed:9821957}. CC -!- INTERACTION: CC P14778; P18510: IL1RN; NbExp=2; IntAct=EBI-525905, EBI-1026330; CC P14778; P09619: PDGFRB; NbExp=2; IntAct=EBI-525905, EBI-641237; CC P14778; Q9Y4K3: TRAF6; NbExp=2; IntAct=EBI-525905, EBI-359276; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597}; Single- CC pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell CC membrane {ECO:0000305|PubMed:8142597}. Secreted CC {ECO:0000269|PubMed:8142597}. CC -!- TISSUE SPECIFICITY: Expressed in T-helper cell subsets. Preferentially CC expressed in T-helper 1 (Th1) cells. {ECO:0000269|PubMed:10653850}. 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:0000269|PubMed:8142597}. CC -!- PTM: Rapidly phosphorylated on Tyr-496 in response to IL-1, which CC creates a SH2 binding site for the PI 3-kinase regulatory subunit CC PIK3R1. {ECO:0000269|PubMed:9821957}. CC -!- DISEASE: Chronic recurrent multifocal osteomyelitis 3 (CRMO3) CC [MIM:259680]: An autosomal dominant autoinflammatory bone disease CC characterized by early-childhood onset of bone pain and arthritis CC caused by sterile osteomyelitis. {ECO:0000269|PubMed:37315560}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. 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; X16896; CAA34773.1; -; mRNA. DR EMBL; M27492; AAA59137.1; -; mRNA. DR EMBL; AF531102; AAM88423.1; -; Genomic_DNA. DR EMBL; AC007271; AAX81988.1; -; Genomic_DNA. DR EMBL; CH471127; EAX01799.1; -; Genomic_DNA. DR EMBL; BC067506; AAH67506.1; -; mRNA. DR EMBL; BC075062; AAH75062.1; -; mRNA. DR EMBL; BC075063; AAH75063.1; -; mRNA. DR CCDS; CCDS2055.1; -. DR PIR; A36187; A36187. DR RefSeq; NP_000868.1; NM_000877.4. DR RefSeq; NP_001275635.1; NM_001288706.1. DR RefSeq; NP_001307907.1; NM_001320978.2. DR RefSeq; NP_001307909.1; NM_001320980.2. DR RefSeq; NP_001307910.1; NM_001320981.2. DR RefSeq; NP_001307911.1; NM_001320982.2. DR RefSeq; NP_001307912.1; NM_001320983.1. DR RefSeq; NP_001307913.1; NM_001320984.1. DR RefSeq; NP_001307914.1; NM_001320985.1. DR RefSeq; XP_005263987.1; XM_005263930.4. DR RefSeq; XP_005263991.1; XM_005263934.5. DR RefSeq; XP_011509417.1; XM_011511115.3. DR RefSeq; XP_011509418.1; XM_011511116.2. DR RefSeq; XP_011509419.1; XM_011511117.1. DR RefSeq; XP_011509420.1; XM_011511118.3. DR RefSeq; XP_016859478.1; XM_017003989.1. DR RefSeq; XP_047300132.1; XM_047444176.1. DR RefSeq; XP_047300133.1; XM_047444177.1. DR RefSeq; XP_047300134.1; XM_047444178.1. DR RefSeq; XP_047300135.1; XM_047444179.1. DR RefSeq; XP_054197786.1; XM_054341811.1. DR RefSeq; XP_054197787.1; XM_054341812.1. DR RefSeq; XP_054197788.1; XM_054341813.1. DR RefSeq; XP_054197789.1; XM_054341814.1. DR RefSeq; XP_054197790.1; XM_054341815.1. DR RefSeq; XP_054197791.1; XM_054341816.1. DR PDB; 1G0Y; X-ray; 3.00 A; R=21-332. DR PDB; 1IRA; X-ray; 2.70 A; Y=18-336. DR PDB; 1ITB; X-ray; 2.50 A; B=18-332. DR PDB; 4DEP; X-ray; 3.10 A; B/E=18-336. DR PDB; 4GAF; X-ray; 2.15 A; B=18-336. DR PDBsum; 1G0Y; -. DR PDBsum; 1IRA; -. DR PDBsum; 1ITB; -. DR PDBsum; 4DEP; -. DR PDBsum; 4GAF; -. DR AlphaFoldDB; P14778; -. DR SASBDB; P14778; -. DR SMR; P14778; -. DR BioGRID; 109770; 31. DR ComplexPortal; CPX-527; Interleukin-1 beta ligand-membrane bound receptor type 1 complex. DR ComplexPortal; CPX-8830; Interleukin-1 alpha-soluble receptor type 1 complex. DR ComplexPortal; CPX-9126; Interleukin-1 antagonist complex. DR ComplexPortal; CPX-9128; Interleukin-1 beta ligand-soluble receptor type 1 complex. DR ComplexPortal; CPX-9166; Precursor interleukin-1 alpha-soluble receptor type 1 complex. DR ComplexPortal; CPX-9169; Precursor interleukin-1 alpha-membrane-bound receptor type 1 complex. DR ComplexPortal; CPX-9173; Interleukin-1 alpha-membrane-bound receptor type 1 complex. DR DIP; DIP-93N; -. DR IntAct; P14778; 16. DR STRING; 9606.ENSP00000386380; -. DR BindingDB; P14778; -. DR ChEMBL; CHEMBL1959; -. DR DrugBank; DB00026; Anakinra. DR DrugBank; DB10770; Foreskin fibroblast (neonatal). DR DrugBank; DB05303; OMS-103HP. DR DrugBank; DB05207; SD118. DR DrugCentral; P14778; -. DR GuidetoPHARMACOLOGY; 1734; -. DR TCDB; 8.A.23.1.11; the basigin (basigin) family. DR GlyCosmos; P14778; 6 sites, No reported glycans. DR GlyGen; P14778; 6 sites, 1 N-linked glycan (1 site). DR iPTMnet; P14778; -. DR PhosphoSitePlus; P14778; -. DR BioMuta; IL1R1; -. DR DMDM; 124308; -. DR jPOST; P14778; -. DR MassIVE; P14778; -. DR PaxDb; 9606-ENSP00000386380; -. DR PeptideAtlas; P14778; -. DR ProteomicsDB; 53081; -. DR ABCD; P14778; 148 sequenced antibodies. DR Antibodypedia; 3576; 1154 antibodies from 43 providers. DR DNASU; 3554; -. DR Ensembl; ENST00000410023.6; ENSP00000386380.1; ENSG00000115594.12. DR GeneID; 3554; -. DR KEGG; hsa:3554; -. DR MANE-Select; ENST00000410023.6; ENSP00000386380.1; NM_000877.4; NP_000868.1. DR UCSC; uc002tbq.5; human. DR AGR; HGNC:5993; -. DR CTD; 3554; -. DR DisGeNET; 3554; -. DR GeneCards; IL1R1; -. DR HGNC; HGNC:5993; IL1R1. DR HPA; ENSG00000115594; Low tissue specificity. DR MalaCards; IL1R1; -. DR MIM; 147810; gene. DR MIM; 259680; phenotype. DR neXtProt; NX_P14778; -. DR OpenTargets; ENSG00000115594; -. DR PharmGKB; PA29809; -. DR VEuPathDB; HostDB:ENSG00000115594; -. DR eggNOG; ENOG502QWEU; Eukaryota. DR GeneTree; ENSGT01090000259985; -. DR HOGENOM; CLU_025552_3_1_1; -. DR InParanoid; P14778; -. DR OMA; HMPAQRQ; -. DR OrthoDB; 6132459at2759; -. DR PhylomeDB; P14778; -. DR TreeFam; TF325519; -. DR PathwayCommons; P14778; -. DR Reactome; R-HSA-6783783; Interleukin-10 signaling. DR Reactome; R-HSA-9020702; Interleukin-1 signaling. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; P14778; -. DR SIGNOR; P14778; -. DR BioGRID-ORCS; 3554; 20 hits in 1175 CRISPR screens. DR ChiTaRS; IL1R1; human. DR EvolutionaryTrace; P14778; -. DR GeneWiki; Interleukin_1_receptor,_type_I; -. DR GenomeRNAi; 3554; -. DR Pharos; P14778; Tclin. DR PRO; PR:P14778; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P14778; protein. DR Bgee; ENSG00000115594; Expressed in palpebral conjunctiva and 203 other cell types or tissues. DR ExpressionAtlas; P14778; baseline and differential. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProt. DR GO; GO:0019966; F:interleukin-1 binding; IEA:Ensembl. DR GO; GO:0004908; F:interleukin-1 receptor activity; IDA:BHF-UCL. DR GO; GO:0004909; F:interleukin-1, type I, activating receptor activity; TAS:ProtInc. 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; IPI:BHF-UCL. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:BHF-UCL. DR GO; GO:2000661; P:positive regulation of interleukin-1-mediated signaling pathway; IEA:Ensembl. DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL. DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central. DR GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL. DR GO; GO:0014805; P:smooth muscle adaptation; NAS:BHF-UCL. DR CDD; cd20991; Ig1_IL1R_like; 1. DR CDD; cd20994; Ig2_IL1R_like; 1. DR CDD; cd20932; Ig3_IL1R_like; 1. DR FunFam; 3.40.50.10140:FF:000002; Interleukin 1 receptor accessory protein; 1. DR FunFam; 2.60.40.10:FF:001064; Interleukin 1 receptor, type I; 1. DR FunFam; 2.60.40.10:FF:000188; Interleukin-1 receptor accessory protein-like 1; 1. DR FunFam; 2.60.40.10:FF:000284; interleukin-1 receptor accessory protein-like 1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 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; INTERLEUKIN-1 RECEPTOR FAMILY MEMBER; 1. DR PANTHER; PTHR11890:SF26; INTERLEUKIN-1 RECEPTOR TYPE 1; 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 PRINTS; PR01537; INTRLKN1R1F. DR SMART; SM00409; IG; 3. DR SMART; SM00255; TIR; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS50104; TIR; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disease variant; Disulfide bond; Glycoprotein; KW Hydrolase; Immunoglobulin domain; Inflammatory response; Membrane; NAD; KW Phosphoprotein; Proteomics identification; Receptor; Reference proteome; KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..17 FT CHAIN 18..569 FT /note="Interleukin-1 receptor type 1, membrane form" FT /id="PRO_0000015435" FT CHAIN 18..? FT /note="Interleukin-1 receptor type 1, soluble form" FT /id="PRO_0000415344" FT TOPO_DOM 18..336 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 337..356 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 357..569 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 23..110 FT /note="Ig-like C2-type 1" FT DOMAIN 118..210 FT /note="Ig-like C2-type 2" FT DOMAIN 226..328 FT /note="Ig-like C2-type 3" FT DOMAIN 383..538 FT /note="TIR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204" FT REGION 540..569 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 556..569 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 470 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204" FT MOD_RES 496 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:9821957" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 193 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 23..104 FT DISULFID 44..96 FT DISULFID 121..164 FT DISULFID 142..196 FT DISULFID 248..312 FT VARIANT 124 FT /note="A -> G (in dbSNP:rs2228139)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_019131" FT VARIANT 131 FT /note="K -> E (in CRMO3; likely pathogenic; results in FT increased function in positive regulation of interleukin-1- FT mediated signaling pathway due to lack of inhibition by FT IL1RN; severely decreased interaction with IL1RN; no effect FT on interaction with IL1A and IL1B)" FT /evidence="ECO:0000269|PubMed:37315560" FT /id="VAR_088970" FT VARIANT 344 FT /note="T -> M (in dbSNP:rs28362304)" FT /id="VAR_029189" FT MUTAGEN 131 FT /note="K->D: Severely decreased interaction with IL1RN." FT /evidence="ECO:0000269|PubMed:37315560" FT MUTAGEN 131 FT /note="K->H: No effect on interaction with IL1RN." FT /evidence="ECO:0000269|PubMed:37315560" FT MUTAGEN 131 FT /note="K->R: No effect on interaction with IL1RN." FT /evidence="ECO:0000269|PubMed:37315560" FT MUTAGEN 369 FT /note="D->A: Reduces NF-kappa-B activation." FT /evidence="ECO:0000269|PubMed:10671496" FT MUTAGEN 428 FT /note="R->A: Reduces NF-kappa-B activation and receptor- FT associated kinase activation." FT /evidence="ECO:0000269|PubMed:10671496" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1IRA" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:1ITB" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1G0Y" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:4GAF" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 171..177 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 192..202 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 205..218 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1ITB" FT STRAND 244..252 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 272..281 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 290..300 FT /evidence="ECO:0007829|PDB:4GAF" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:4GAF" FT STRAND 319..328 FT /evidence="ECO:0007829|PDB:4GAF" SQ SEQUENCE 569 AA; 65402 MW; 5BAA83F8F0225C25 CRC64; MKVLLRLICF IALLISSLEA DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKHMIG ICVTLTVIIV CSVFIYKIFK IDIVLWYRDS CYDFLPIKAS DGKTYDAYIL YPKTVGEGST SDCDIFVFKV LPEVLEKQCG YKLFIYGRDD YVGEDIVEVI NENVKKSRRL IIILVRETSG FSWLGGSSEE QIAMYNALVQ DGIKVVLLEL EKIQDYEKMP ESIKFIKQKH GAIRWSGDFT QGPQSAKTRF WKNVRYHMPV QRRSPSSKHQ LLSPATKEKL QREAHVPLG //