IL1R1_HUMAN
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 03-AUG-2022, entry version 233.
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 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; P14778; -.
DR PeptideAtlas; P14778; -.
DR PRIDE; P14778; -.
DR ProteomicsDB; 53081; -.
DR ABCD; P14778; 16 sequenced antibodies.
DR Antibodypedia; 3576; 980 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 CTD; 3554; -.
DR DisGeNET; 3554; -.
DR GeneCards; IL1R1; -.
DR HGNC; HGNC:5993; IL1R1.
DR HPA; ENSG00000115594; Low tissue specificity.
DR MIM; 147810; gene.
DR neXtProt; NX_P14778; -.
DR OpenTargets; ENSG00000115594; -.
DR PharmGKB; PA29809; -.
DR VEuPathDB; HostDB:ENSG00000115594; -.
DR eggNOG; ENOG502QWEU; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_025552_3_1_1; -.
DR InParanoid; P14778; -.
DR OMA; EISGFSW; -.
DR OrthoDB; 1109920at2759; -.
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; 15 hits in 1075 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 201 other tissues.
DR ExpressionAtlas; P14778; baseline and differential.
DR Genevisible; P14778; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
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:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0070555; P:response to interleukin-1; IDA:BHF-UCL.
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 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 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
