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Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (CD antigen CD218a)

 IL18R_HUMAN             Reviewed;         541 AA.
Q13478; B2R9Y5; Q52LC9;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=Interleukin-18 receptor 1;
Short=IL-18R-1;
Short=IL-18R1;
AltName: Full=CD218 antigen-like family member A;
AltName: Full=CDw218a;
AltName: Full=IL1 receptor-related protein;
Short=IL-1Rrp;
Short=IL1R-rp;
AltName: Full=Interleukin-18 receptor alpha {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
Short=IL-18R-alpha;
Short=IL-18Ralpha {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25261253, ECO:0000303|PubMed:25500532};
AltName: CD_antigen=CD218a;
Flags: Precursor;
Name=IL18R1 {ECO:0000312|HGNC:HGNC:5988}; Synonyms=IL1RRP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-317 DEL, LACK OF BINDING TO
IL1A AND IL1B, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=8626725; DOI=10.1074/jbc.271.8.3967;
Parnet P., Garka K.E., Bonnert T.P., Dower S.K., Sims J.E.;
"IL-1Rrp is a novel receptor-like molecule similar to the type I
interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP.";
J. Biol. Chem. 271:3967-3970(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 19-29; 55-58; 59-71; 211-221; 222-231; 269-275;
276-280; 319-315 AND 524-535, AND CHARACTERIZATION.
PubMed=9325300; DOI=10.1074/jbc.272.41.25737;
Torigoe K., Ushio S., Okura T., Kobayashi S., Taniai M., Kunikata T.,
Murakami T., Sanou O., Kojima H., Fujii M., Ohta T., Ikeda M.,
Ikegami H., Kurimoto M.;
"Purification and characterization of the human interleukin-18
receptor.";
J. Biol. Chem. 272:25737-25742(1997).
[6]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY IL12/INTERLEUKIN-12.
PubMed=10653850;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K.,
Hada T., Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[7]
TISSUE SPECIFICITY, AND INDUCTION BY IL12/INTERLEUKIN-12.
PubMed=10925275; DOI=10.4049/jimmunol.165.4.1933;
Sareneva T., Julkunen I., Matikainen S.;
"IFN-alpha and IL-12 induce IL-18 receptor gene expression in human NK
and T cells.";
J. Immunol. 165:1933-1938(2000).
[8]
TISSUE SPECIFICITY.
PubMed=11046021; DOI=10.4049/jimmunol.165.9.4950;
Debets R., Timans J.C., Churakowa T., Zurawski S., de Waal Malefyt R.,
Moore K.W., Abrams J.S., O'Garra A., Bazan J.F., Kastelein R.A.;
"IL-18 receptors, their role in ligand binding and function: anti-IL-
1RAcPL antibody, a potent antagonist of IL-18.";
J. Immunol. 165:4950-4956(2000).
[9]
SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=14528293; DOI=10.1038/nsb993;
Kato Z., Jee J., Shikano H., Mishima M., Ohki I., Ohnishi H., Li A.,
Hashimoto K., Matsukuma E., Omoya K., Yamamoto Y., Yoneda T., Hara T.,
Kondo N., Shirakawa M.;
"The structure and binding mode of interleukin-18.";
Nat. Struct. Biol. 10:966-971(2003).
[10]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 19-329, GLYCOSYLATION AT
ASN-197; ASN-203; ASN-236 AND ASN-297, DISULFIDE BONDS, AND FUNCTION.
PubMed=25261253; DOI=10.1016/j.febslet.2014.09.019;
Wei H., Wang D., Qian Y., Liu X., Fan S., Yin H.S., Wang X.;
"Structural basis for the specific recognition of IL-18 by its alpha
receptor.";
FEBS Lett. 588:3838-3843(2014).
[11]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-329, GLYCOSYLATION AT
ASN-91; ASN-102; ASN-150; ASN-197; ASN-203; ASN-236 AND ASN-297,
DISULFIDE BONDS, MUTAGENESIS OF ASN-297, SUBUNIT, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=25500532; DOI=10.1038/ncomms6340;
Tsutsumi N., Kimura T., Arita K., Ariyoshi M., Ohnishi H.,
Yamamoto T., Zuo X., Maenaka K., Park E.Y., Kondo N., Shirakawa M.,
Tochio H., Kato Z.;
"The structural basis for receptor recognition of human interleukin-
18.";
Nat. Commun. 5:5340-5340(2014).
-!- FUNCTION: Within the IL18 receptor complex, responsible for the
binding of the proinflammatory cytokine IL18, but not IL1A nor
IL1B (PubMed:8626725, PubMed:14528293, PubMed:25261253,
PubMed:25500532). Involved in IL18-mediated IFNG synthesis from T-
helper 1 (Th1) cells (PubMed:10653850). Contributes to IL18-
induced cytokine production, either independently of SLC12A3, or
as a complex with SLC12A3 (By similarity).
{ECO:0000250|UniProtKB:Q61098, ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532, ECO:0000269|PubMed:8626725}.
-!- SUBUNIT: Forms a ternary complex with IL18 and IL18RAP
(PubMed:14528293, PubMed:25500532). Within this complex, IL18R1 is
involved in ligand-binding and IL18RAP in signaling leading to NF-
kappa-B and JNK activation (Probable). Interacts with SLC12A3 in
peritoneal macrophages; this interaction is increased by IL18
treatment (By similarity). {ECO:0000250|UniProtKB:Q61098,
ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25500532,
ECO:0000305}.
-!- INTERACTION:
Q14116:IL18; NbExp=2; IntAct=EBI-9817499, EBI-3910835;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14528293};
Single-pass type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in leukocytes, spleen, lung.
Also expressed, but at lower levels, in liver, small intestine,
colon, prostate, thymus, placenta, and heart. Specifically
coexpressed with IL18R1 in Th1 cells (PubMed:10925275,
PubMed:11046021, PubMed:10653850). {ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:10925275, ECO:0000269|PubMed:11046021,
ECO:0000269|PubMed:8626725}.
-!- INDUCTION: Induced by IL12/interleukin-12 in T-cells. Proposed to
be a phenotypic marker for T-helper 1 (Th1) cells.
{ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:10925275}.
-!- PTM: N-glycosylated. N-linked glycosyl chains contribute to ligand
recognition and intra-receptor interactions required for formation
of an active ternary receptor complex.
{ECO:0000269|PubMed:25261253, ECO:0000269|PubMed:25500532}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
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EMBL; U43672; AAC50390.1; -; mRNA.
EMBL; AK313967; BAG36682.1; -; mRNA.
EMBL; AC007248; AAY15048.1; -; Genomic_DNA.
EMBL; BC069575; AAH69575.1; -; mRNA.
EMBL; BC093975; AAH93975.1; -; mRNA.
EMBL; BC093977; AAH93977.1; -; mRNA.
CCDS; CCDS2060.1; -.
RefSeq; NP_001269328.1; NM_001282399.1.
RefSeq; NP_003846.1; NM_003855.3.
UniGene; Hs.469521; -.
PDB; 3WO3; X-ray; 3.10 A; B/D/F/H/J/L=20-329.
PDB; 3WO4; X-ray; 3.10 A; B=20-329.
PDB; 4R6U; X-ray; 2.80 A; A/C=19-329.
PDBsum; 3WO3; -.
PDBsum; 3WO4; -.
PDBsum; 4R6U; -.
ProteinModelPortal; Q13478; -.
SMR; Q13478; -.
BioGrid; 114337; 2.
IntAct; Q13478; 1.
MINT; Q13478; -.
STRING; 9606.ENSP00000233957; -.
iPTMnet; Q13478; -.
PhosphoSitePlus; Q13478; -.
EPD; Q13478; -.
MaxQB; Q13478; -.
PaxDb; Q13478; -.
PeptideAtlas; Q13478; -.
PRIDE; Q13478; -.
ProteomicsDB; 59476; -.
Ensembl; ENST00000233957; ENSP00000233957; ENSG00000115604.
Ensembl; ENST00000409599; ENSP00000387211; ENSG00000115604.
Ensembl; ENST00000410040; ENSP00000386663; ENSG00000115604.
GeneID; 8809; -.
KEGG; hsa:8809; -.
UCSC; uc002tbw.6; human.
CTD; 8809; -.
DisGeNET; 8809; -.
EuPathDB; HostDB:ENSG00000115604.10; -.
GeneCards; IL18R1; -.
HGNC; HGNC:5988; IL18R1.
HPA; HPA007615; -.
MIM; 604494; gene.
neXtProt; NX_Q13478; -.
OpenTargets; ENSG00000115604; -.
PharmGKB; PA29804; -.
eggNOG; ENOG410IH1W; Eukaryota.
eggNOG; ENOG410ZKHN; LUCA.
GeneTree; ENSGT00760000119071; -.
HOGENOM; HOG000113032; -.
HOVERGEN; HBG052098; -.
InParanoid; Q13478; -.
KO; K05173; -.
OMA; VLEFWPV; -.
OrthoDB; EOG091G0GXW; -.
PhylomeDB; Q13478; -.
TreeFam; TF325519; -.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
Reactome; R-HSA-9012546; Interleukin-18 signaling.
SIGNOR; Q13478; -.
GeneWiki; IL18R1; -.
GenomeRNAi; 8809; -.
PRO; PR:Q13478; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115604; -.
CleanEx; HS_IL18R1; -.
ExpressionAtlas; Q13478; baseline and differential.
Genevisible; Q13478; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
GO; GO:0042007; F:interleukin-18 binding; IDA:UniProtKB.
GO; GO:0042008; F:interleukin-18 receptor activity; IEA:Ensembl.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Inflammatory response; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 18 {ECO:0000269|PubMed:9325300}.
CHAIN 19 541 Interleukin-18 receptor 1.
/FTId=PRO_0000015448.
TOPO_DOM 22 329 Extracellular. {ECO:0000255}.
TRANSMEM 330 350 Helical. {ECO:0000255}.
TOPO_DOM 351 541 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 121 Ig-like C2-type 1.
DOMAIN 133 212 Ig-like C2-type 2.
DOMAIN 220 312 Ig-like C2-type 3.
DOMAIN 373 523 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
DISULFID 22 41 {ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
DISULFID 43 81 {ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
DISULFID 119 158 {ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
DISULFID 140 185 {ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
DISULFID 237 298 {ECO:0000244|PDB:3WO3,
ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532}.
VARIANT 210 210 R -> H (in dbSNP:rs11465635).
/FTId=VAR_053379.
VARIANT 232 232 N -> K (in dbSNP:rs11465644).
/FTId=VAR_053380.
VARIANT 310 310 S -> N (in dbSNP:rs11465648).
/FTId=VAR_053381.
VARIANT 317 317 Missing. {ECO:0000269|PubMed:8626725}.
/FTId=VAR_014955.
VARIANT 423 423 G -> R (in dbSNP:rs12619169).
/FTId=VAR_053382.
MUTAGEN 297 297 N->Q: Decreases the affinity for IL18
suggesting that the N-linked
glycosylation contributes to ligand
recognition.
{ECO:0000269|PubMed:25500532}.
STRAND 26 31 {ECO:0000244|PDB:4R6U}.
STRAND 36 39 {ECO:0000244|PDB:4R6U}.
TURN 43 47 {ECO:0000244|PDB:3WO3}.
STRAND 55 59 {ECO:0000244|PDB:4R6U}.
STRAND 76 79 {ECO:0000244|PDB:4R6U}.
STRAND 82 87 {ECO:0000244|PDB:4R6U}.
HELIX 90 92 {ECO:0000244|PDB:4R6U}.
STRAND 94 100 {ECO:0000244|PDB:4R6U}.
STRAND 103 112 {ECO:0000244|PDB:4R6U}.
STRAND 116 120 {ECO:0000244|PDB:4R6U}.
HELIX 122 124 {ECO:0000244|PDB:4R6U}.
STRAND 125 131 {ECO:0000244|PDB:4R6U}.
STRAND 134 139 {ECO:0000244|PDB:4R6U}.
TURN 143 145 {ECO:0000244|PDB:4R6U}.
HELIX 146 148 {ECO:0000244|PDB:4R6U}.
STRAND 149 156 {ECO:0000244|PDB:4R6U}.
STRAND 166 168 {ECO:0000244|PDB:3WO3}.
STRAND 170 174 {ECO:0000244|PDB:4R6U}.
HELIX 177 179 {ECO:0000244|PDB:4R6U}.
STRAND 181 191 {ECO:0000244|PDB:4R6U}.
STRAND 194 207 {ECO:0000244|PDB:4R6U}.
STRAND 216 219 {ECO:0000244|PDB:3WO4}.
STRAND 221 226 {ECO:0000244|PDB:4R6U}.
STRAND 233 241 {ECO:0000244|PDB:4R6U}.
STRAND 246 250 {ECO:0000244|PDB:4R6U}.
STRAND 261 263 {ECO:0000244|PDB:3WO3}.
STRAND 266 270 {ECO:0000244|PDB:4R6U}.
TURN 272 274 {ECO:0000244|PDB:3WO4}.
STRAND 276 284 {ECO:0000244|PDB:4R6U}.
TURN 290 292 {ECO:0000244|PDB:4R6U}.
STRAND 296 302 {ECO:0000244|PDB:4R6U}.
STRAND 305 314 {ECO:0000244|PDB:4R6U}.
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


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