ILRL1_HUMAN
ID ILRL1_HUMAN Reviewed; 556 AA.
AC Q01638; A8K6B3; B4E0I3; Q53TU7; Q8NEJ3; Q9ULV7; Q9UQ44;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Interleukin-1 receptor-like 1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein ST2;
DE Flags: Precursor;
GN Name=IL1RL1; Synonyms=DER4, ST2, T1;
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 [GENOMIC DNA / MRNA] (ISOFORM B), AND VARIANT GLU-78.
RC TISSUE=Lymphocyte;
RX PubMed=1482686; DOI=10.1016/0167-4781(92)90125-j;
RA Tominaga S., Yokota T., Yanagisawa K., Tsukamoto T., Takagi T., Tetsuka T.;
RT "Nucleotide sequence of a complementary DNA for human ST2.";
RL Biochim. Biophys. Acta 1171:215-218(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND VARIANT GLU-78.
RX PubMed=10527832; DOI=10.1006/bbrc.1999.1469;
RA Tominaga S., Kuroiwa K., Tago K., Iwahana H., Yanagisawa K., Komatsu N.;
RT "Presence and expression of a novel variant form of ST2 gene product in
RT human leukemic cell line UT-7/GM.";
RL Biochem. Biophys. Res. Commun. 264:14-18(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANTS GLU-78 AND THR-433.
RC TISSUE=Megakaryoblast;
RX PubMed=10936050; DOI=10.1006/geno.2000.6269;
RA Li H., Tago K., Io K., Kuroiwa K., Arai T., Iwahana H., Tominaga S.,
RA Yanagisawa K.;
RT "The cloning and nucleotide sequence of human ST2L cDNA.";
RL Genomics 67:284-290(2000).
RN [4]
RP SEQUENCE REVISION TO 433.
RA Yanagisawa K.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND 4).
RC TISSUE=Placenta, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Placenta;
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 [9]
RP PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11478810; DOI=10.1006/bbrc.2001.5306;
RA Tago K., Noda T., Hayakawa M., Iwahana H., Yanagisawa K., Yashiro T.,
RA Tominaga S.;
RT "Tissue distribution and subcellular localization of a variant form of the
RT human ST2 gene product, ST2V.";
RL Biochem. Biophys. Res. Commun. 285:1377-1383(2001).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015;
RA Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K.,
RA Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F.,
RA Kastelein R.A.;
RT "IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-
RT related protein ST 2 and induces T helper type 2-associated cytokines.";
RL Immunity 23:479-490(2005).
RN [12]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [13]
RP FUNCTION, AND MODEL OF THE IL-33 SIGNALING COMPLEX.
RX PubMed=19836339; DOI=10.1016/j.str.2009.08.009;
RA Lingel A., Weiss T.M., Niebuhr M., Pan B., Appleton B.A., Wiesmann C.,
RA Bazan J.F., Fairbrother W.J.;
RT "Structure of IL-33 and its interaction with the ST2 and IL-1RAcP
RT receptors--insight into heterotrimeric IL-1 signaling complexes.";
RL Structure 17:1398-1410(2009).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=19508382; DOI=10.1111/j.1582-4934.2009.00801.x;
RA Marvie P., Lisbonne M., L'helgoualc'h A., Rauch M., Turlin B., Preisser L.,
RA Bourd-Boittin K., Theret N., Gascan H., Piquet-Pellorce C., Samson M.;
RT "Interleukin-33 overexpression is associated with liver fibrosis in mice
RT and humans.";
RL J. Cell. Mol. Med. 14:1726-1739(2010).
RN [15]
RP INTERACTION WITH TMED1.
RX PubMed=23319592; DOI=10.1074/jbc.m112.403899;
RA Connolly D.J., O'Neill L.A., McGettrick A.F.;
RT "The GOLD domain-containing protein TMED1 is involved in interleukin-33
RT signaling.";
RL J. Biol. Chem. 288:5616-5623(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 19-321 IN COMPLEX WITH IL33,
RP GLYCOSYLATION AT ASN-95; ASN-140 AND ASN-191, AND DISULFIDE BONDS.
RX PubMed=23980170; DOI=10.1073/pnas.1308651110;
RA Liu X., Hammel M., He Y., Tainer J.A., Jeng U.S., Zhang L., Wang S.,
RA Wang X.;
RT "Structural insights into the interaction of IL-33 with its receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14918-14923(2013).
CC -!- FUNCTION: Receptor for interleukin-33 (IL-33); signaling requires
CC association of the coreceptor IL1RAP. Its stimulation recruits MYD88,
CC IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1
CC and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-
CC cell function. {ECO:0000269|PubMed:16286016,
CC ECO:0000305|PubMed:19836339}.
CC -!- FUNCTION: [Isoform B]: Inhibits IL-33 signaling.
CC {ECO:0000250|UniProtKB:P14719}.
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: Interacts with MYD88, IRAK1, IRAK4, and TRAF6. Bound to its
CC ligand IL-33, interacts with IL1RAP to form the minimal interleukin-33
CC signaling complex with a 1:1:1 stoichiometry. Interacts with KIT (bound
CC to KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33
CC signaling complex contains IL1RL1, IL1RAP, KIT and MYD88. Interacts
CC with TMED1 (PubMed:23319592). {ECO:0000250|UniProtKB:P14719,
CC ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:23319592,
CC ECO:0000269|PubMed:23980170, ECO:0000305|PubMed:19836339}.
CC -!- INTERACTION:
CC Q01638; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-993762, EBI-3939278;
CC Q01638; O95760: IL33; NbExp=2; IntAct=EBI-993762, EBI-724057;
CC Q01638-2; P07307-3: ASGR2; NbExp=3; IntAct=EBI-12838366, EBI-12808270;
CC Q01638-2; Q2HXU8-2: CLEC12B; NbExp=3; IntAct=EBI-12838366, EBI-12811991;
CC Q01638-2; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-12838366, EBI-11749983;
CC Q01638-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12838366, EBI-6942903;
CC Q01638-2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12838366, EBI-13345167;
CC Q01638-2; O15529: GPR42; NbExp=3; IntAct=EBI-12838366, EBI-18076404;
CC Q01638-2; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-12838366, EBI-2689785;
CC Q01638-2; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-12838366, EBI-17640454;
CC Q01638-2; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-12838366, EBI-9978441;
CC Q01638-2; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-12838366, EBI-17670824;
CC Q01638-2; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-12838366, EBI-751210;
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Cell membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Secreted.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11478810};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11478810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=ST2L;
CC IsoId=Q01638-1; Sequence=Displayed;
CC Name=B; Synonyms=ST2S;
CC IsoId=Q01638-2; Sequence=VSP_002666, VSP_002667;
CC Name=C; Synonyms=ST2V;
CC IsoId=Q01638-3; Sequence=VSP_002664, VSP_002665;
CC Name=4;
CC IsoId=Q01638-4; Sequence=VSP_054933, VSP_002666, VSP_002667;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung, placenta,
CC stomach, skeletal muscle, colon and small intestine. Isoform A is
CC prevalently expressed in the lung, testis, placenta, stomach and colon.
CC Isoform B is more abundant in the brain, kidney and the liver. Isoform
CC C is not detected in brain, heart, liver, kidney and skeletal muscle.
CC Expressed on T-cells in fibrotic liver; at protein level. Overexpressed
CC in fibrotic and cirrhotic liver. {ECO:0000269|PubMed:11478810,
CC ECO:0000269|PubMed:19508382}.
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 -!- MISCELLANEOUS: [Isoform C]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; D12763; BAA02233.1; -; mRNA.
DR EMBL; D12764; BAA20539.1; -; Genomic_DNA.
DR EMBL; AB029084; BAA85894.1; -; mRNA.
DR EMBL; AB012701; BAA82405.2; -; mRNA.
DR EMBL; AK291578; BAF84267.1; -; mRNA.
DR EMBL; AK303389; BAG64445.1; -; mRNA.
DR EMBL; AC007248; AAY15047.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01795.1; -; Genomic_DNA.
DR EMBL; BC030975; AAH30975.1; -; mRNA.
DR CCDS; CCDS2057.1; -. [Q01638-1]
DR CCDS; CCDS2058.1; -. [Q01638-2]
DR CCDS; CCDS74548.1; -. [Q01638-4]
DR PIR; JC7109; JC7109.
DR PIR; S30444; S30444.
DR RefSeq; NP_001269337.1; NM_001282408.1. [Q01638-4]
DR RefSeq; NP_003847.2; NM_003856.3. [Q01638-2]
DR RefSeq; NP_057316.3; NM_016232.4. [Q01638-1]
DR RefSeq; XP_006712902.1; XM_006712839.3. [Q01638-1]
DR RefSeq; XP_011510453.1; XM_011512151.1. [Q01638-2]
DR PDB; 4KC3; X-ray; 3.27 A; B=19-321.
DR PDBsum; 4KC3; -.
DR AlphaFoldDB; Q01638; -.
DR SMR; Q01638; -.
DR BioGRID; 114613; 21.
DR CORUM; Q01638; -.
DR DIP; DIP-37861N; -.
DR IntAct; Q01638; 16.
DR STRING; 9606.ENSP00000233954; -.
DR GlyConnect; 1948; 10 N-Linked glycans (5 sites).
DR GlyGen; Q01638; 8 sites, 10 N-linked glycans (5 sites).
DR iPTMnet; Q01638; -.
DR PhosphoSitePlus; Q01638; -.
DR BioMuta; IL1RL1; -.
DR DMDM; 116242527; -.
DR EPD; Q01638; -.
DR jPOST; Q01638; -.
DR MassIVE; Q01638; -.
DR PaxDb; Q01638; -.
DR PeptideAtlas; Q01638; -.
DR PRIDE; Q01638; -.
DR ProteomicsDB; 57975; -. [Q01638-1]
DR ProteomicsDB; 57976; -. [Q01638-2]
DR ProteomicsDB; 57977; -. [Q01638-3]
DR TopDownProteomics; Q01638-2; -. [Q01638-2]
DR ABCD; Q01638; 14 sequenced antibodies.
DR Antibodypedia; 2362; 572 antibodies from 39 providers.
DR DNASU; 9173; -.
DR Ensembl; ENST00000233954.6; ENSP00000233954.1; ENSG00000115602.17. [Q01638-1]
DR Ensembl; ENST00000311734.6; ENSP00000310371.2; ENSG00000115602.17. [Q01638-2]
DR Ensembl; ENST00000404917.6; ENSP00000384822.2; ENSG00000115602.17. [Q01638-4]
DR Ensembl; ENST00000427077.1; ENSP00000391120.1; ENSG00000115602.17. [Q01638-3]
DR GeneID; 9173; -.
DR KEGG; hsa:9173; -.
DR MANE-Select; ENST00000233954.6; ENSP00000233954.1; NM_016232.5; NP_057316.3.
DR UCSC; uc002tbu.1; human. [Q01638-1]
DR CTD; 9173; -.
DR DisGeNET; 9173; -.
DR GeneCards; IL1RL1; -.
DR HGNC; HGNC:5998; IL1RL1.
DR HPA; ENSG00000115602; Group enriched (kidney, lung, placenta).
DR MIM; 601203; gene.
DR neXtProt; NX_Q01638; -.
DR OpenTargets; ENSG00000115602; -.
DR PharmGKB; PA29814; -.
DR VEuPathDB; HostDB:ENSG00000115602; -.
DR eggNOG; ENOG502RU6H; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_025552_3_1_1; -.
DR InParanoid; Q01638; -.
DR OMA; MQGTIKW; -.
DR OrthoDB; 1109920at2759; -.
DR PhylomeDB; Q01638; -.
DR TreeFam; TF325519; -.
DR PathwayCommons; Q01638; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-9014843; Interleukin-33 signaling. [Q01638-2]
DR SignaLink; Q01638; -.
DR BioGRID-ORCS; 9173; 9 hits in 1069 CRISPR screens.
DR GeneWiki; IL1RL1; -.
DR GenomeRNAi; 9173; -.
DR Pharos; Q01638; Tbio.
DR PRO; PR:Q01638; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q01638; protein.
DR Bgee; ENSG00000115602; Expressed in upper lobe of left lung and 135 other tissues.
DR ExpressionAtlas; Q01638; baseline and differential.
DR Genevisible; Q01638; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004896; F:cytokine receptor activity; TAS:UniProtKB.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0002113; F:interleukin-33 binding; IBA:GO_Central.
DR GO; GO:0002114; F:interleukin-33 receptor activity; IBA:GO_Central.
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:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; IPR003598; Ig_sub2.
DR InterPro; IPR015621; IL-1_rcpt_fam.
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; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 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; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 19..556
FT /note="Interleukin-1 receptor-like 1"
FT /id="PRO_0000015442"
FT TOPO_DOM 19..328
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..103
FT /note="Ig-like C2-type 1"
FT DOMAIN 114..197
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..319
FT /note="Ig-like C2-type 3"
FT DOMAIN 375..535
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 198..211
FT /note="Flexible linker"
FT ACT_SITE 461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23980170"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23980170"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23980170"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23980170"
FT DISULFID 111..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23980170"
FT DISULFID 133..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23980170"
FT DISULFID 235..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23980170"
FT DISULFID 238..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23980170"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054933"
FT VAR_SEQ 204..259
FT /note="DEQGFSLFPVIGAPAQNEIKEVEIGKNANLTCSACFGKGTQFLAAVLWQLNG
FT TKIT -> VWCQSFCKLKKSLIFSNTHWIQSLMRGFVMVYYGVHKCCRVVFNLCLQYFQ
FT HHQWP (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10527832"
FT /id="VSP_002664"
FT VAR_SEQ 260..556
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10527832"
FT /id="VSP_002665"
FT VAR_SEQ 324..328
FT /note="IDHHS -> SKECF (in isoform B and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1482686, ECO:0000303|PubMed:15489334"
FT /id="VSP_002666"
FT VAR_SEQ 329..556
FT /note="Missing (in isoform B and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1482686, ECO:0000303|PubMed:15489334"
FT /id="VSP_002667"
FT VARIANT 78
FT /note="A -> E (in dbSNP:rs1041973)"
FT /evidence="ECO:0000269|PubMed:10527832,
FT ECO:0000269|PubMed:10936050, ECO:0000269|PubMed:1482686"
FT /id="VAR_023749"
FT VARIANT 433
FT /note="A -> T (in dbSNP:rs4988956)"
FT /evidence="ECO:0000269|PubMed:10936050"
FT /id="VAR_053373"
FT VARIANT 501
FT /note="Q -> K (in dbSNP:rs10192036)"
FT /id="VAR_053374"
FT VARIANT 501
FT /note="Q -> R (in dbSNP:rs10204137)"
FT /id="VAR_053375"
FT VARIANT 549
FT /note="T -> I (in dbSNP:rs10192157)"
FT /id="VAR_053376"
FT VARIANT 551
FT /note="L -> S (in dbSNP:rs10206753)"
FT /id="VAR_053377"
FT CONFLICT 70
FT /note="Q -> R (in Ref. 2; BAA85894)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4KC3"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4KC3"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4KC3"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:4KC3"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 177..189
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 191..202
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:4KC3"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4KC3"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:4KC3"
SQ SEQUENCE 556 AA; 63358 MW; CB3E444A2DD477B5 CRC64;
MGFWILAILT ILMYSTAAKF SKQSWGLENE ALIVRCPRQG KPSYTVDWYY SQTNKSIPTQ
ERNRVFASGQ LLKFLPAAVA DSGIYTCIVR SPTFNRTGYA NVTIYKKQSD CNVPDYLMYS
TVSGSEKNSK IYCPTIDLYN WTAPLEWFKN CQALQGSRYR AHKSFLVIDN VMTEDAGDYT
CKFIHNENGA NYSVTATRSF TVKDEQGFSL FPVIGAPAQN EIKEVEIGKN ANLTCSACFG
KGTQFLAAVL WQLNGTKITD FGEPRIQQEE GQNQSFSNGL ACLDMVLRIA DVKEEDLLLQ
YDCLALNLHG LRRHTVRLSR KNPIDHHSIY CIIAVCSVFL MLINVLVIIL KMFWIEATLL
WRDIAKPYKT RNDGKLYDAY VVYPRNYKSS TDGASRVEHF VHQILPDVLE NKCGYTLCIY
GRDMLPGEDV VTAVETNIRK SRRHIFILTP QITHNKEFAY EQEVALHCAL IQNDAKVILI
EMEALSELDM LQAEALQDSL QHLMKVQGTI KWREDHIANK RSLNSKFWKH VRYQMPVPSK
IPRKASSLTP LAAQKQ
