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   24-JAN-2024, entry version 189.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   CCDS; CCDS92824.1; -. [O95256-2]
DR   RefSeq; NP_003844.1; NM_003853.3. [O95256-1]
DR   RefSeq; XP_011510389.1; XM_011512087.2.
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   PDB; 7FCH; X-ray; 1.88 A; A/B/C/D=406-562.
DR   PDBsum; 3WO4; -.
DR   PDBsum; 6KN9; -.
DR   PDBsum; 7FCH; -.
DR   AlphaFoldDB; O95256; -.
DR   SASBDB; O95256; -.
DR   SMR; O95256; -.
DR   BioGRID; 114335; 20.
DR   IntAct; O95256; 5.
DR   STRING; 9606.ENSP00000264260; -.
DR   ChEMBL; CHEMBL4804253; -.
DR   GlyCosmos; O95256; 4 sites, No reported glycans.
DR   GlyGen; O95256; 4 sites.
DR   iPTMnet; O95256; -.
DR   PhosphoSitePlus; O95256; -.
DR   BioMuta; IL18RAP; -.
DR   MassIVE; O95256; -.
DR   PaxDb; 9606-ENSP00000264260; -.
DR   PeptideAtlas; O95256; -.
DR   ProteomicsDB; 50750; -. [O95256-1]
DR   ProteomicsDB; 61717; -.
DR   ABCD; O95256; 3 sequenced antibodies.
DR   Antibodypedia; 17791; 431 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   AGR; HGNC:5989; -.
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; ENSGT01090000259985; -.
DR   HOGENOM; CLU_025552_2_0_1; -.
DR   InParanoid; O95256; -.
DR   OMA; EPQKSHF; -.
DR   OrthoDB; 5350760at2759; -.
DR   PhylomeDB; O95256; -.
DR   TreeFam; TF325519; -.
DR   PathwayCommons; O95256; -.
DR   Reactome; R-HSA-9012546; Interleukin-18 signaling.
DR   SignaLink; O95256; -.
DR   BioGRID-ORCS; 8807; 6 hits in 1154 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 108 other cell types or tissues.
DR   ExpressionAtlas; O95256; baseline and differential.
DR   GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0015026; F:coreceptor activity; IDA:UniProt.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
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:0042119; P:neutrophil activation; IEA:Ensembl.
DR   GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 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; INTERLEUKIN-1 RECEPTOR FAMILY MEMBER; 1.
DR   PANTHER; PTHR11890:SF23; INTERLEUKIN-18 RECEPTOR ACCESSORY PROTEIN; 1.
DR   Pfam; PF18452; Ig_6; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR01537; INTRLKN1R1F.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS50104; TIR; 1.
DR   Genevisible; O95256; HS.
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
FT                   NF-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"
FT   STRAND          408..413
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           430..435
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           437..442
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   TURN            443..446
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           453..456
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   STRAND          459..461
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           463..472
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   STRAND          474..481
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           483..486
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           491..501
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   STRAND          508..513
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           525..533
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   STRAND          536..538
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   TURN            541..544
FT                   /evidence="ECO:0007829|PDB:7FCH"
FT   HELIX           550..558
FT                   /evidence="ECO:0007829|PDB:7FCH"
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
//