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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.
13-FEB-2019, entry version 164.
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; 3.
MINT; Q13478; -.
STRING; 9606.ENSP00000233957; -.
iPTMnet; Q13478; -.
PhosphoSitePlus; Q13478; -.
BioMuta; IL18R1; -.
EPD; Q13478; -.
jPOST; 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; ENSGT00940000153660; -.
HOGENOM; HOG000113032; -.
HOVERGEN; HBG052098; -.
InParanoid; Q13478; -.
KO; K05173; -.
OMA; FTRGMII; -.
OrthoDB; 985064at2759; -.
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; Expressed in 131 organ(s), highest expression level in right lung.
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:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
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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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2328: Allograft rejection
WP2292: Chemokine signaling pathway
WP1004: Kit Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1014: Androgen receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1067: Toll-like receptor signaling pathway
WP1112: EPO Receptor Signaling
WP1121: Kit Receptor Signaling Pathway
WP1130: T Cell Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP1144: B Cell Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1183: Toll-like receptor signaling pathway
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1249: EPO Receptor Signaling
WP1271: Toll-like receptor signaling pathway
WP1284: EPO Receptor Signaling
WP1309: Toll-like receptor signaling pathway
WP1336: EPO Receptor Signaling

Related Genes :
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[Il18r1] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (CD218 antigen-like family member A) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il1r1 Il-1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[Il1rl2] Interleukin-1 receptor-like 2 (IL-36 receptor) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2)
[IL37 FIL1Z IL1F7 IL1H4 IL1RP1] Interleukin-37 (FIL1 zeta) (IL-1X) (Interleukin-1 family member 7) (IL-1F7) (Interleukin-1 homolog 4) (IL-1H) (IL-1H4) (Interleukin-1 zeta) (IL-1 zeta) (Interleukin-1-related protein) (IL-1RP1) (Interleukin-23) (IL-37)
[Sigirr Tir8] Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)
[IL36RN FIL1D IL1F5 IL1HY1 IL1L1 IL1RP3 UNQ1896/PRO4342] Interleukin-36 receptor antagonist protein (IL-36Ra) (FIL1 delta) (IL-1-related protein 3) (IL-1RP3) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 receptor antagonist homolog 1) (IL-1ra homolog 1) (Interleukin-1-like protein 1) (IL-1L1)
[IL18 IGIF IL1F4] Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL1RAPL1 OPHN4] Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (Interleukin-33 receptot beta chain)
[IL36G IL1E IL1F9 IL1H1 IL1RP2 UNQ2456/PRO5737] Interleukin-36 gamma (IL-1-related protein 2) (IL-1RP2) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 9) (IL-1F9) (Interleukin-1 homolog 1) (IL-1H1)
[IL36RN Fil1d Il1f5 Il1h3 Il1hy1] Interleukin-36 receptor antagonist protein (IL-36Ra) (Interleukin-1 HY1) (IL-1HY1) (Interleukin-1 delta) (IL-1 delta) (Interleukin-1 family member 5) (IL-1F5) (Interleukin-1 homolog 3) (IL-1H3) (Interleukin-1-like protein 1) (IL-1L1)
[IL36A FIL1E IL1E IL1F6] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6)
[IL1B IL1F2] Interleukin-1 beta (IL-1 beta) (Catabolin)
[Il36a Fil1e Il1e Il1f6 Il1h1] Interleukin-36 alpha (FIL1 epsilon) (Interleukin-1 epsilon) (IL-1 epsilon) (Interleukin-1 family member 6) (IL-1F6) (Interleukin-1 homolog 1) (IL-1H1)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL36B IL1F8 IL1H2] Interleukin-36 beta (FIL1 eta) (Interleukin-1 eta) (IL-1 eta) (Interleukin-1 family member 8) (IL-1F8) (Interleukin-1 homolog 2) (IL-1H2)
[IL1A IL1F1] Interleukin-1 alpha (IL-1 alpha) (Hematopoietin-1)
[IL1RAP] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP)
[IL33 C9orf26 IL1F11 NFHEV] Interleukin-33 (IL-33) (Interleukin-1 family member 11) (IL-1F11) (Nuclear factor from high endothelial venules) (NF-HEV) [Cleaved into: Interleukin-33 (95-270); Interleukin-33 (99-270); Interleukin-33 (109-270)]
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP)
[Irak1 Il1rak] Interleukin-1 receptor-associated kinase 1 (IRAK) (IRAK-1) (EC 2.7.11.1) (Pelle-like protein kinase) (mPLK)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)

Bibliography :
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