I18RA_HUMAN
ID I18RA_HUMAN Reviewed; 599 AA.
AC O95256; B2RPJ3; Q2QDE5; Q3KPE7; Q3KPE8; Q53TT4; Q53TU5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Interleukin-18 receptor accessory protein;
DE Short=IL-18 receptor accessory protein;
DE Short=IL-18RAcP;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Accessory protein-like;
DE Short=AcPL;
DE AltName: Full=CD218 antigen-like family member B;
DE AltName: Full=CDw218b;
DE AltName: Full=IL-1R accessory protein-like {ECO:0000303|PubMed:10653850};
DE Short=IL-1RAcPL;
DE AltName: Full=Interleukin-1 receptor 7;
DE Short=IL-1R-7;
DE Short=IL-1R7;
DE AltName: Full=Interleukin-18 receptor accessory protein-like;
DE AltName: Full=Interleukin-18 receptor beta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
DE Short=IL-18R-beta;
DE Short=IL-18Rbeta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
DE AltName: CD_antigen=CD218b;
DE Flags: Precursor;
GN Name=IL18RAP {ECO:0000312|HGNC:HGNC:5989}; Synonyms=IL1R7;
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=9792649; DOI=10.1074/jbc.273.45.29445;
RA Born T.L., Thomassen E., Bird T.A., Sims J.E.;
RT "Cloning of a novel receptor subunit, AcPL, required for interleukin-18
RT signaling.";
RL J. Biol. Chem. 273:29445-29450(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
RX PubMed=17897836; DOI=10.1016/j.cyto.2007.07.186;
RA Fiszer D., Rozwadowska N., Rychlewski L., Kosicki W., Kurpisz M.;
RT "Identification of IL-18RAP mRNA truncated splice variants in human testis
RT and the other human tissues.";
RL Cytokine 39:178-183(2007).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY IFN-ALPHA AND 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 [9]
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 [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 15-356, GLYCOSYLATION AT ASN-119;
RP ASN-152 AND ASN-345, DISULFIDE BONDS, MUTAGENESIS OF LEU-167; GLU-210;
RP TYR-212; TYR-214; LYS-313 AND 15-GLU--PRO-176, SUBUNIT, 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, does not mediate IL18-
CC binding, but involved in IL18-dependent signal transduction, leading to
CC NF-kappa-B and JNK activation (PubMed:9792649, PubMed:14528293,
CC PubMed:25500532). May play a role in IL18-mediated IFNG synthesis from
CC T-helper 1 (Th1) cells (Probable). {ECO:0000269|PubMed:14528293,
CC ECO:0000269|PubMed:25500532, ECO:0000269|PubMed:9792649,
CC ECO:0000305|PubMed:10653850}.
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 IL18R1 (PubMed:14528293,
CC PubMed:25500532). Within this complex, IL18R1 is involved in ligand-
CC binding and IL18RAP in signaling leading to NF-kappa-B and JNK
CC activation (Probable). {ECO:0000269|PubMed:14528293,
CC ECO:0000269|PubMed:25500532, ECO:0000305}.
CC -!- INTERACTION:
CC O95256; O76024: WFS1; NbExp=4; IntAct=EBI-21018056, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14528293};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95256-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95256-2; Sequence=VSP_056295;
CC Name=3; Synonyms=IL-18RAPshort {ECO:0000303|PubMed:17897836};
CC IsoId=O95256-3; Sequence=VSP_059116, VSP_059117;
CC Name=4;
CC IsoId=O95256-4; Sequence=VSP_059114, VSP_059115;
CC -!- TISSUE SPECIFICITY: Detected in adrenal gland, bone marrow, brain,
CC fetal brain, fetal liver, heart, kidney, lung, liver, peripheral blood
CC leukocytes, placenta, prostate, salivary gland, skeletal muscle, spinal
CC cord, testis, thymus, thyroid, trachea and uterus (PubMed:17897836).
CC Strongly expressed in peripheral blood leukocytes and spleen and, to a
CC lesser extent, in colon (PubMed:9792649). Specifically coexpressed with
CC IL18R1 in T-helper 1 (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:17897836, ECO:0000269|PubMed:9792649}.
CC -!- INDUCTION: Induced by IFN-alpha and IL12/interleukin-12 in natural
CC killer (NK) cells and T-cells. {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. {ECO:0000269|PubMed:25500532}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; AF077346; AAC72196.1; -; mRNA.
DR EMBL; DQ116957; AAZ52551.1; -; mRNA.
DR EMBL; AC007278; AAY15080.1; -; Genomic_DNA.
DR EMBL; AC007248; AAY15049.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01791.1; -; Genomic_DNA.
DR EMBL; AK300026; BAG61837.1; -; mRNA.
DR EMBL; BC069630; AAH69630.1; -; mRNA.
DR EMBL; BC106764; AAI06765.1; -; mRNA.
DR EMBL; BC106765; AAI06766.1; -; mRNA.
DR EMBL; BC137474; AAI37475.1; -; mRNA.
DR EMBL; BC137475; AAI37476.1; -; mRNA.
DR CCDS; CCDS2061.1; -. [O95256-1]
DR RefSeq; NP_003844.1; NM_003853.3. [O95256-1]
DR RefSeq; XP_011510389.1; XM_011512087.2. [O95256-2]
DR RefSeq; XP_011510390.1; XM_011512088.2. [O95256-2]
DR PDB; 3WO4; X-ray; 3.10 A; C=15-356.
DR PDB; 6KN9; X-ray; 3.30 A; A/B/C=20-356.
DR PDBsum; 3WO4; -.
DR PDBsum; 6KN9; -.
DR AlphaFoldDB; O95256; -.
DR SASBDB; O95256; -.
DR SMR; O95256; -.
DR BioGRID; 114335; 20.
DR IntAct; O95256; 5.
DR STRING; 9606.ENSP00000264260; -.
DR GlyGen; O95256; 4 sites.
DR iPTMnet; O95256; -.
DR PhosphoSitePlus; O95256; -.
DR BioMuta; IL18RAP; -.
DR PaxDb; O95256; -.
DR PeptideAtlas; O95256; -.
DR PRIDE; O95256; -.
DR ProteomicsDB; 50750; -. [O95256-1]
DR ProteomicsDB; 61717; -.
DR ABCD; O95256; 3 sequenced antibodies.
DR Antibodypedia; 17791; 388 antibodies from 30 providers.
DR DNASU; 8807; -.
DR Ensembl; ENST00000264260.6; ENSP00000264260.2; ENSG00000115607.10. [O95256-1]
DR Ensembl; ENST00000409369.1; ENSP00000387201.1; ENSG00000115607.10. [O95256-2]
DR Ensembl; ENST00000687160.1; ENSP00000510345.1; ENSG00000115607.10. [O95256-1]
DR GeneID; 8807; -.
DR KEGG; hsa:8807; -.
DR MANE-Select; ENST00000687160.1; ENSP00000510345.1; NM_001393487.1; NP_001380416.1.
DR UCSC; uc002tbx.4; human. [O95256-1]
DR CTD; 8807; -.
DR DisGeNET; 8807; -.
DR GeneCards; IL18RAP; -.
DR HGNC; HGNC:5989; IL18RAP.
DR HPA; ENSG00000115607; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 604509; gene.
DR neXtProt; NX_O95256; -.
DR OpenTargets; ENSG00000115607; -.
DR PharmGKB; PA29805; -.
DR VEuPathDB; HostDB:ENSG00000115607; -.
DR eggNOG; ENOG502QUSU; Eukaryota.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_2_0_1; -.
DR InParanoid; O95256; -.
DR OMA; EPQKSHF; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; O95256; -.
DR TreeFam; TF325519; -.
DR PathwayCommons; O95256; -.
DR Reactome; R-HSA-9012546; Interleukin-18 signaling.
DR SignaLink; O95256; -.
DR BioGRID-ORCS; 8807; 5 hits in 1076 CRISPR screens.
DR GeneWiki; IL18RAP; -.
DR GenomeRNAi; 8807; -.
DR Pharos; O95256; Tbio.
DR PRO; PR:O95256; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95256; protein.
DR Bgee; ENSG00000115607; Expressed in granulocyte and 107 other tissues.
DR ExpressionAtlas; O95256; baseline and differential.
DR Genevisible; O95256; HS.
DR GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
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; 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; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Inflammatory response;
KW Membrane; NAD; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..599
FT /note="Interleukin-18 receptor accessory protein"
FT /id="PRO_0000042185"
FT TOPO_DOM 20..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 149..235
FT /note="Ig-like C2-type 1"
FT DOMAIN 251..353
FT /note="Ig-like C2-type 2"
FT DOMAIN 406..559
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT DISULFID 46..126
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT DISULFID 155..180
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT DISULFID 175..221
FT /evidence="ECO:0000269|PubMed:25500532,
FT ECO:0007744|PDB:3WO4"
FT DISULFID 180..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 273..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO4"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056295"
FT VAR_SEQ 118..126
FT /note="VNNSGSYIC -> LGHIFVDPR (in isoform 4)"
FT /evidence="ECO:0000269|PubMed:17897836"
FT /id="VSP_059114"
FT VAR_SEQ 127..599
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000269|PubMed:17897836"
FT /id="VSP_059115"
FT VAR_SEQ 133..149
FT /note="SPYDVACCVKMILEVKP -> YDPNTFLSENISKSSII (in isoform
FT 3)"
FT /evidence="ECO:0000269|PubMed:17897836"
FT /id="VSP_059116"
FT VAR_SEQ 150..599
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000269|PubMed:17897836"
FT /id="VSP_059117"
FT VARIANT 350
FT /note="V -> I (in dbSNP:rs11465716)"
FT /id="VAR_034005"
FT MUTAGEN 15..176
FT /note="Missing: Impairs IL18 receptor signaling via NF-
FT kappa-B."
FT /evidence="ECO:0000269|PubMed:25500532"
FT MUTAGEN 167
FT /note="L->A: Decreases binding to the preformed binary
FT complex of IL18 and IL18R1."
FT /evidence="ECO:0000269|PubMed:25500532"
FT MUTAGEN 210
FT /note="E->A: Decreases binding to the preformed binary
FT complex of IL18 and IL18R1. Impairs IL18 receptor signaling
FT via NF-kappa-B; when associated with A-212 and A-214."
FT /evidence="ECO:0000269|PubMed:25500532"
FT MUTAGEN 212
FT /note="Y->A: Abolishes binding to the preformed binary
FT complex of IL18 and IL18R1. Impairs IL18 receptor signaling
FT via NF-kappa-B; when associated with A-210 and A-214."
FT /evidence="ECO:0000269|PubMed:25500532"
FT MUTAGEN 214
FT /note="Y->A: Decreases binding to the preformed binary
FT complex of IL18 and IL18R1. Impairs IL18 receptor signaling
FT via NF-kappa-B; when associated with A-210 and A-212."
FT /evidence="ECO:0000269|PubMed:25500532"
FT MUTAGEN 313
FT /note="K->A: Decreases binding to the preformed binary
FT complex of IL18 and IL18R1. Decreases IL18 receptor
FT signaling via NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:25500532"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3WO4"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3WO4"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6KN9"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3WO4"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 233..243
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 312..325
FT /evidence="ECO:0007829|PDB:3WO4"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:3WO4"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:3WO4"
SQ SEQUENCE 599 AA; 68310 MW; 54807DA3E05462F1 CRC64;
MLCLGWIFLW LVAGERIKGF NISGCSTKKL LWTYSTRSEE EFVLFCDLPE PQKSHFCHRN
RLSPKQVPEH LPFMGSNDLS DVQWYQQPSN GDPLEDIRKS YPHIIQDKCT LHFLTPGVNN
SGSYICRPKM IKSPYDVACC VKMILEVKPQ TNASCEYSAS HKQDLLLGST GSISCPSLSC
QSDAQSPAVT WYKNGKLLSV ERSNRIVVDE VYDYHQGTYV CDYTQSDTVS SWTVRAVVQV
RTIVGDTKLK PDILDPVEDT LEVELGKPLT ISCKARFGFE RVFNPVIKWY IKDSDLEWEV
SVPEAKSIKS TLKDEIIERN IILEKVTQRD LRRKFVCFVQ NSIGNTTQSV QLKEKRGVVL
LYILLGTIGT LVAVLAASAL LYRHWIEIVL LYRTYQSKDQ TLGDKKDFDA FVSYAKWSSF
PSEATSSLSE EHLALSLFPD VLENKYGYSL CLLERDVAPG GVYAEDIVSI IKRSRRGIFI
LSPNYVNGPS IFELQAAVNL ALDDQTLKLI LIKFCYFQEP ESLPHLVKKA LRVLPTVTWR
GLKSVPPNSR FWAKMRYHMP VKNSQGFTWN QLRITSRIFQ WKGLSRTETT GRSSQPKEW
