IL18R_HUMAN
ID IL18R_HUMAN Reviewed; 541 AA.
AC Q13478; B2R9Y5; Q52LC9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Interleukin-18 receptor 1;
DE Short=IL-18R-1;
DE Short=IL-18R1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=CD218 antigen-like family member A;
DE AltName: Full=CDw218a;
DE AltName: Full=IL1 receptor-related protein;
DE Short=IL-1Rrp;
DE Short=IL1R-rp;
DE AltName: Full=Interleukin-18 receptor alpha {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
DE Short=IL-18R-alpha;
DE Short=IL-18Ralpha {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
DE AltName: CD_antigen=CD218a;
DE Flags: Precursor;
GN Name=IL18R1 {ECO:0000312|HGNC:HGNC:5988}; Synonyms=IL1RRP;
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], VARIANT ALA-317 DEL, LACK OF BINDING TO IL1A
RP AND IL1B, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=8626725; DOI=10.1074/jbc.271.8.3967;
RA Parnet P., Garka K.E., Bonnert T.P., Dower S.K., Sims J.E.;
RT "IL-1Rrp is a novel receptor-like molecule similar to the type I
RT interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP.";
RL J. Biol. Chem. 271:3967-3970(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 19-29; 55-58; 59-71; 211-221; 222-231; 269-275;
RP 276-280; 319-315 AND 524-535, AND CHARACTERIZATION.
RX PubMed=9325300; DOI=10.1074/jbc.272.41.25737;
RA Torigoe K., Ushio S., Okura T., Kobayashi S., Taniai M., Kunikata T.,
RA Murakami T., Sanou O., Kojima H., Fujii M., Ohta T., Ikeda M., Ikegami H.,
RA Kurimoto M.;
RT "Purification and characterization of the human interleukin-18 receptor.";
RL J. Biol. Chem. 272:25737-25742(1997).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY IL12/INTERLEUKIN-12.
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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY IL12/INTERLEUKIN-12.
RX PubMed=10925275; DOI=10.4049/jimmunol.165.4.1933;
RA Sareneva T., Julkunen I., Matikainen S.;
RT "IFN-alpha and IL-12 induce IL-18 receptor gene expression in human NK and
RT T cells.";
RL J. Immunol. 165:1933-1938(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11046021; DOI=10.4049/jimmunol.165.9.4950;
RA Debets R., Timans J.C., Churakowa T., Zurawski S., de Waal Malefyt R.,
RA Moore K.W., Abrams J.S., O'Garra A., Bazan J.F., Kastelein R.A.;
RT "IL-18 receptors, their role in ligand binding and function: anti-IL-1RAcPL
RT antibody, a potent antagonist of IL-18.";
RL J. Immunol. 165:4950-4956(2000).
RN [9]
RP SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14528293; DOI=10.1038/nsb993;
RA Kato Z., Jee J., Shikano H., Mishima M., Ohki I., Ohnishi H., Li A.,
RA Hashimoto K., Matsukuma E., Omoya K., Yamamoto Y., Yoneda T., Hara T.,
RA Kondo N., Shirakawa M.;
RT "The structure and binding mode of interleukin-18.";
RL Nat. Struct. Biol. 10:966-971(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 19-329, GLYCOSYLATION AT ASN-197;
RP ASN-203; ASN-236 AND ASN-297, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=25261253; DOI=10.1016/j.febslet.2014.09.019;
RA Wei H., Wang D., Qian Y., Liu X., Fan S., Yin H.S., Wang X.;
RT "Structural basis for the specific recognition of IL-18 by its alpha
RT receptor.";
RL FEBS Lett. 588:3838-3843(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-329, GLYCOSYLATION AT ASN-91;
RP ASN-102; ASN-150; ASN-197; ASN-203; ASN-236 AND ASN-297, DISULFIDE BONDS,
RP MUTAGENESIS OF ASN-297, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25500532; DOI=10.1038/ncomms6340;
RA Tsutsumi N., Kimura T., Arita K., Ariyoshi M., Ohnishi H., Yamamoto T.,
RA Zuo X., Maenaka K., Park E.Y., Kondo N., Shirakawa M., Tochio H., Kato Z.;
RT "The structural basis for receptor recognition of human interleukin-18.";
RL Nat. Commun. 5:5340-5340(2014).
CC -!- FUNCTION: Within the IL18 receptor complex, responsible for the binding
CC of the pro-inflammatory cytokine IL18, but not IL1A nor IL1B
CC (PubMed:8626725, PubMed:14528293, PubMed:25261253, PubMed:25500532).
CC Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells
CC (PubMed:10653850). Contributes to IL18-induced cytokine production,
CC either independently of SLC12A3, or as a complex with SLC12A3 (By
CC similarity). {ECO:0000250|UniProtKB:Q61098,
CC ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:14528293,
CC ECO:0000269|PubMed:25261253, ECO:0000269|PubMed:25500532,
CC ECO:0000269|PubMed:8626725}.
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: Forms a ternary complex with IL18 and IL18RAP
CC (PubMed:14528293, PubMed:25500532). Within this complex, IL18R1 is
CC involved in ligand-binding and IL18RAP in signaling leading to NF-
CC kappa-B and JNK activation (Probable). Interacts with SLC12A3 in
CC peritoneal macrophages; this interaction is increased by IL18 treatment
CC (By similarity). {ECO:0000250|UniProtKB:Q61098,
CC ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25500532, ECO:0000305}.
CC -!- INTERACTION:
CC Q13478; Q14116: IL18; NbExp=2; IntAct=EBI-9817499, EBI-3910835;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14528293}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leukocytes, spleen, lung. Also
CC expressed, but at lower levels, in liver, small intestine, colon,
CC prostate, thymus, placenta, and heart. Specifically coexpressed with
CC IL18R1 in Th1 cells (PubMed:10925275, PubMed:11046021,
CC PubMed:10653850). {ECO:0000269|PubMed:10653850,
CC ECO:0000269|PubMed:10925275, ECO:0000269|PubMed:11046021,
CC ECO:0000269|PubMed:8626725}.
CC -!- INDUCTION: Induced by IL12/interleukin-12 in T-cells. Proposed to be a
CC phenotypic marker for T-helper 1 (Th1) cells.
CC {ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:10925275}.
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: N-glycosylated. N-linked glycosyl chains contribute to ligand
CC recognition and intra-receptor interactions required for formation of
CC an active ternary receptor complex. {ECO:0000269|PubMed:25261253,
CC ECO:0000269|PubMed:25500532}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; U43672; AAC50390.1; -; mRNA.
DR EMBL; AK313967; BAG36682.1; -; mRNA.
DR EMBL; AC007248; AAY15048.1; -; Genomic_DNA.
DR EMBL; BC069575; AAH69575.1; -; mRNA.
DR EMBL; BC093975; AAH93975.1; -; mRNA.
DR EMBL; BC093977; AAH93977.1; -; mRNA.
DR CCDS; CCDS2060.1; -.
DR RefSeq; NP_001269328.1; NM_001282399.1.
DR RefSeq; NP_003846.1; NM_003855.3.
DR PDB; 3WO3; X-ray; 3.10 A; B/D/F/H/J/L=20-329.
DR PDB; 3WO4; X-ray; 3.10 A; B=20-329.
DR PDB; 4R6U; X-ray; 2.80 A; A/C=19-329.
DR PDBsum; 3WO3; -.
DR PDBsum; 3WO4; -.
DR PDBsum; 4R6U; -.
DR AlphaFoldDB; Q13478; -.
DR SASBDB; Q13478; -.
DR SMR; Q13478; -.
DR BioGRID; 114337; 6.
DR IntAct; Q13478; 5.
DR MINT; Q13478; -.
DR STRING; 9606.ENSP00000387211; -.
DR GlyGen; Q13478; 8 sites.
DR iPTMnet; Q13478; -.
DR PhosphoSitePlus; Q13478; -.
DR BioMuta; IL18R1; -.
DR EPD; Q13478; -.
DR jPOST; Q13478; -.
DR MassIVE; Q13478; -.
DR MaxQB; Q13478; -.
DR PaxDb; Q13478; -.
DR PeptideAtlas; Q13478; -.
DR PRIDE; Q13478; -.
DR ProteomicsDB; 59476; -.
DR ABCD; Q13478; 1 sequenced antibody.
DR Antibodypedia; 2363; 822 antibodies from 36 providers.
DR DNASU; 8809; -.
DR Ensembl; ENST00000233957.7; ENSP00000233957.1; ENSG00000115604.12.
DR Ensembl; ENST00000409599.5; ENSP00000387211.1; ENSG00000115604.12.
DR Ensembl; ENST00000410040.5; ENSP00000386663.1; ENSG00000115604.12.
DR GeneID; 8809; -.
DR KEGG; hsa:8809; -.
DR MANE-Select; ENST00000233957.7; ENSP00000233957.1; NM_003855.5; NP_003846.1.
DR UCSC; uc002tbw.6; human.
DR CTD; 8809; -.
DR DisGeNET; 8809; -.
DR GeneCards; IL18R1; -.
DR HGNC; HGNC:5988; IL18R1.
DR HPA; ENSG00000115604; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 604494; gene.
DR neXtProt; NX_Q13478; -.
DR OpenTargets; ENSG00000115604; -.
DR PharmGKB; PA29804; -.
DR VEuPathDB; HostDB:ENSG00000115604; -.
DR eggNOG; ENOG502QUAC; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_025552_3_1_1; -.
DR InParanoid; Q13478; -.
DR OMA; ECGPENG; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; Q13478; -.
DR TreeFam; TF325519; -.
DR PathwayCommons; Q13478; -.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR Reactome; R-HSA-9012546; Interleukin-18 signaling.
DR SignaLink; Q13478; -.
DR SIGNOR; Q13478; -.
DR BioGRID-ORCS; 8809; 15 hits in 1070 CRISPR screens.
DR GeneWiki; IL18R1; -.
DR GenomeRNAi; 8809; -.
DR Pharos; Q13478; Tbio.
DR PRO; PR:Q13478; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13478; protein.
DR Bgee; ENSG00000115604; Expressed in right lung and 121 other tissues.
DR ExpressionAtlas; Q13478; baseline and differential.
DR Genevisible; Q13478; HS.
DR GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0042007; F:interleukin-18 binding; IDA:UniProtKB.
DR GO; GO:0042008; F:interleukin-18 receptor activity; IDA:UniProtKB.
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:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
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; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunoglobulin domain; Inflammatory response; Membrane; NAD;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:9325300"
FT CHAIN 19..541
FT /note="Interleukin-18 receptor 1"
FT /id="PRO_0000015448"
FT TOPO_DOM 22..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..121
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..212
FT /note="Ig-like C2-type 2"
FT DOMAIN 220..312
FT /note="Ig-like C2-type 3"
FT DOMAIN 373..520
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO3, ECO:0007744|PDB:3WO4"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO3, ECO:0007744|PDB:3WO4"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO3, ECO:0007744|PDB:3WO4"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT DISULFID 22..41
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT DISULFID 43..81
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT DISULFID 119..158
FT /evidence="ECO:0000269|PubMed:25261253,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO3,
FT ECO:0007744|PDB:3WO4, ECO:0007744|PDB:4R6U"
FT DISULFID 140..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25261253, ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO3, ECO:0007744|PDB:3WO4,
FT ECO:0007744|PDB:4R6U"
FT DISULFID 237..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25261253, ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO3, ECO:0007744|PDB:3WO4,
FT ECO:0007744|PDB:4R6U"
FT VARIANT 210
FT /note="R -> H (in dbSNP:rs11465635)"
FT /id="VAR_053379"
FT VARIANT 232
FT /note="N -> K (in dbSNP:rs11465644)"
FT /id="VAR_053380"
FT VARIANT 310
FT /note="S -> N (in dbSNP:rs11465648)"
FT /id="VAR_053381"
FT VARIANT 317
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:8626725"
FT /id="VAR_014955"
FT VARIANT 423
FT /note="G -> R (in dbSNP:rs12619169)"
FT /id="VAR_053382"
FT MUTAGEN 297
FT /note="N->Q: Decreases the affinity for IL18 suggesting
FT that the N-linked glycosylation contributes to ligand
FT recognition."
FT /evidence="ECO:0000269|PubMed:25500532"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4R6U"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:3WO3"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4R6U"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:4R6U"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4R6U"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4R6U"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3WO3"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4R6U"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3WO3"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4R6U"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:4R6U"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:4R6U"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:4R6U"
SQ SEQUENCE 541 AA; 62304 MW; 7173DB9C7EA71D32 CRC64;
MNCRELPLTL WVLISVSTAE SCTSRPHITV VEGEPFYLKH CSCSLAHEIE TTTKSWYKSS
GSQEHVELNP RSSSRIALHD CVLEFWPVEL NDTGSYFFQM KNYTQKWKLN VIRRNKHSCF
TERQVTSKIV EVKKFFQITC ENSYYQTLVN STSLYKNCKK LLLENNKNPT IKKNAEFEDQ
GYYSCVHFLH HNGKLFNITK TFNITIVEDR SNIVPVLLGP KLNHVAVELG KNVRLNCSAL
LNEEDVIYWM FGEENGSDPN IHEEKEMRIM TPEGKWHASK VLRIENIGES NLNVLYNCTV
ASTGGTDTKS FILVRKADMA DIPGHVFTRG MIIAVLILVA VVCLVTVCVI YRVDLVLFYR
HLTRRDETLT DGKTYDAFVS YLKECRPENG EEHTFAVEIL PRVLEKHFGY KLCIFERDVV
PGGAVVDEIH SLIEKSRRLI IVLSKSYMSN EVRYELESGL HEALVERKIK IILIEFTPVT
DFTFLPQSLK LLKSHRVLKW KADKSLSYNS RFWKNLLYLM PAKTVKPGRD EPEVLPVLSE
S
