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Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (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)

 IL18R_HUMAN             Reviewed;         541 AA.
Q13478; B2R9Y5; Q52LC9;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-AUG-2020, entry version 175.
RecName: Full=Interleukin-18 receptor 1;
Short=IL-18R-1;
Short=IL-18R1;
EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
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; DOI=10.1093/intimm/12.2.151;
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}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
-!- 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:
Q13478; 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}.
-!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
Self-association of TIR domains is required for NADase activity.
{ECO:0000255|PROSITE-ProRule:PRU00204}.
-!- 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.
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; -.
SMR; Q13478; -.
BioGRID; 114337; 2.
IntAct; Q13478; 3.
MINT; Q13478; -.
STRING; 9606.ENSP00000387211; -.
GlyGen; Q13478; 8 sites.
iPTMnet; Q13478; -.
PhosphoSitePlus; Q13478; -.
BioMuta; IL18R1; -.
EPD; Q13478; -.
jPOST; Q13478; -.
MassIVE; Q13478; -.
MaxQB; Q13478; -.
PaxDb; Q13478; -.
PeptideAtlas; Q13478; -.
PRIDE; Q13478; -.
ProteomicsDB; 59476; -.
ABCD; Q13478; 1 sequenced antibody.
Antibodypedia; 2363; 757 antibodies.
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; ENSG00000115604; Tissue enhanced (lung).
MIM; 604494; gene.
neXtProt; NX_Q13478; -.
OpenTargets; ENSG00000115604; -.
PharmGKB; PA29804; -.
eggNOG; ENOG502QUAC; Eukaryota.
GeneTree; ENSGT01000000214361; -.
HOGENOM; CLU_025552_3_1_1; -.
InParanoid; Q13478; -.
KO; K05173; -.
OMA; NFLEFWP; -.
OrthoDB; 985064at2759; -.
PhylomeDB; Q13478; -.
TreeFam; TF325519; -.
PathwayCommons; Q13478; -.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
Reactome; R-HSA-9012546; Interleukin-18 signaling.
SIGNOR; Q13478; -.
BioGRID-ORCS; 8809; 5 hits in 872 CRISPR screens.
GeneWiki; IL18R1; -.
GenomeRNAi; 8809; -.
Pharos; Q13478; Tbio.
PRO; PR:Q13478; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q13478; protein.
Bgee; ENSG00000115604; Expressed in right lung and 146 other tissues.
ExpressionAtlas; Q13478; baseline and differential.
Genevisible; Q13478; HS.
GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
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; IPR041416; Ig_6.
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; PF18452; Ig_6; 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; Direct protein sequencing; Disulfide bond; Glycoprotein;
Hydrolase; Immunoglobulin domain; Inflammatory response; Membrane; NAD;
Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1..18
/evidence="ECO:0000269|PubMed:9325300"
CHAIN 19..541
/note="Interleukin-18 receptor 1"
/id="PRO_0000015448"
TOPO_DOM 22..329
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 330..350
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 351..541
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 33..121
/note="Ig-like C2-type 1"
DOMAIN 133..212
/note="Ig-like C2-type 2"
DOMAIN 220..312
/note="Ig-like C2-type 3"
DOMAIN 373..520
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
ACT_SITE 455
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
CARBOHYD 91
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
CARBOHYD 102
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
CARBOHYD 150
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
CARBOHYD 197
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
CARBOHYD 203
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
CARBOHYD 236
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
CARBOHYD 255
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 297
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
DISULFID 22..41
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
DISULFID 43..81
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
DISULFID 119..158
/evidence="ECO:0000244|PDB:3WO3, ECO:0000244|PDB:3WO4,
ECO:0000244|PDB:4R6U, ECO:0000269|PubMed:25261253,
ECO:0000269|PubMed:25500532"
DISULFID 140..185
/evidence="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
/evidence="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
/note="R -> H (in dbSNP:rs11465635)"
/id="VAR_053379"
VARIANT 232
/note="N -> K (in dbSNP:rs11465644)"
/id="VAR_053380"
VARIANT 310
/note="S -> N (in dbSNP:rs11465648)"
/id="VAR_053381"
VARIANT 317
/note="Missing"
/evidence="ECO:0000269|PubMed:8626725"
/id="VAR_014955"
VARIANT 423
/note="G -> R (in dbSNP:rs12619169)"
/id="VAR_053382"
MUTAGEN 297
/note="N->Q: Decreases the affinity for IL18 suggesting
that the N-linked glycosylation contributes to ligand
recognition."
/evidence="ECO:0000269|PubMed:25500532"
STRAND 26..31
/evidence="ECO:0000244|PDB:4R6U"
STRAND 36..39
/evidence="ECO:0000244|PDB:4R6U"
TURN 43..47
/evidence="ECO:0000244|PDB:3WO3"
STRAND 55..59
/evidence="ECO:0000244|PDB:4R6U"
STRAND 76..79
/evidence="ECO:0000244|PDB:4R6U"
STRAND 82..87
/evidence="ECO:0000244|PDB:4R6U"
HELIX 90..92
/evidence="ECO:0000244|PDB:4R6U"
STRAND 94..100
/evidence="ECO:0000244|PDB:4R6U"
STRAND 103..112
/evidence="ECO:0000244|PDB:4R6U"
STRAND 116..120
/evidence="ECO:0000244|PDB:4R6U"
HELIX 122..124
/evidence="ECO:0000244|PDB:4R6U"
STRAND 125..131
/evidence="ECO:0000244|PDB:4R6U"
STRAND 134..139
/evidence="ECO:0000244|PDB:4R6U"
TURN 143..145
/evidence="ECO:0000244|PDB:4R6U"
HELIX 146..148
/evidence="ECO:0000244|PDB:4R6U"
STRAND 149..156
/evidence="ECO:0000244|PDB:4R6U"
STRAND 166..168
/evidence="ECO:0000244|PDB:3WO3"
STRAND 170..174
/evidence="ECO:0000244|PDB:4R6U"
HELIX 177..179
/evidence="ECO:0000244|PDB:4R6U"
STRAND 181..191
/evidence="ECO:0000244|PDB:4R6U"
STRAND 194..207
/evidence="ECO:0000244|PDB:4R6U"
STRAND 216..219
/evidence="ECO:0000244|PDB:3WO4"
STRAND 221..226
/evidence="ECO:0000244|PDB:4R6U"
STRAND 233..241
/evidence="ECO:0000244|PDB:4R6U"
STRAND 246..250
/evidence="ECO:0000244|PDB:4R6U"
STRAND 261..263
/evidence="ECO:0000244|PDB:3WO3"
STRAND 266..270
/evidence="ECO:0000244|PDB:4R6U"
TURN 272..274
/evidence="ECO:0000244|PDB:3WO4"
STRAND 276..284
/evidence="ECO:0000244|PDB:4R6U"
TURN 290..292
/evidence="ECO:0000244|PDB:4R6U"
STRAND 296..302
/evidence="ECO:0000244|PDB:4R6U"
STRAND 305..314
/evidence="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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