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   27-MAR-2024, entry version 242.
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).
CC   -!- FUNCTION: Receptor for IL1A, IL1B and IL1RN (PubMed:2950091). After
CC       binding to interleukin-1 associates with the coreceptor IL1RAP to form
CC       the 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 such
CC       as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of
CC       the receptor/coreceptor subunits. Binds ligands with comparable
CC       affinity and binding of antagonist IL1RN prevents association with
CC       IL1RAP to form a signaling complex. Involved in IL1B-mediated
CC       costimulation of IFNG production from T-helper 1 (Th1) cells
CC       (PubMed:10653850). {ECO:0000269|PubMed:10653850,
CC       ECO:0000269|PubMed:10671496, ECO:0000269|PubMed:2950091}.
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
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; 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   -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/il1r1/";
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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_000877.3.
DR   RefSeq; NP_001275635.1; NM_001288706.1.
DR   RefSeq; NP_001307907.1; NM_001320978.1.
DR   RefSeq; NP_001307909.1; NM_001320980.1.
DR   RefSeq; NP_001307910.1; NM_001320981.1.
DR   RefSeq; NP_001307911.1; NM_001320982.1.
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_005263934.4.
DR   RefSeq; XP_011509417.1; XM_011511115.2.
DR   RefSeq; XP_011509418.1; XM_011511116.1.
DR   RefSeq; XP_011509419.1; XM_011511117.1.
DR   RefSeq; XP_011509420.1; XM_011511118.2.
DR   RefSeq; XP_016859478.1; XM_017003989.1.
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; 30.
DR   DIP; DIP-93N; -.
DR   IntAct; P14778; 15.
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.
DR   iPTMnet; P14778; -.
DR   PhosphoSitePlus; P14778; -.
DR   BioMuta; IL1R1; -.
DR   DMDM; 124308; -.
DR   jPOST; P14778; -.
DR   MassIVE; P14778; -.
DR   MaxQB; P14778; -.
DR   PaxDb; 9606-ENSP00000386380; -.
DR   PeptideAtlas; P14778; -.
DR   ProteomicsDB; 53081; -.
DR   ABCD; P14778; 153 sequenced antibodies.
DR   Antibodypedia; 3576; 1146 antibodies from 41 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   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; CYDFLPK; -.
DR   OrthoDB; 4322253at2759; -.
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: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; IBA:GO_Central.
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: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; 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: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: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   CDD; cd20991; Ig1_IL1R_like; 1.
DR   CDD; cd20994; Ig2_IL1R_like; 1.
DR   CDD; cd20932; Ig3_IL1R_like; 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.
DR   Genevisible; P14778; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW   Immunoglobulin domain; Inflammatory response; Membrane; NAD;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW   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        555..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         344
FT                   /note="T -> M (in dbSNP:rs28362304)"
FT                   /id="VAR_029189"
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
FT                   receptor-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
//