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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)

 I18RA_HUMAN             Reviewed;         599 AA.
O95256; B2RPJ3; Q2QDE5; Q3KPE7; Q3KPE8; Q53TT4; Q53TU5;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
17-JUN-2020, entry version 171.
RecName: Full=Interleukin-18 receptor accessory protein;
Short=IL-18 receptor accessory protein;
Short=IL-18RAcP;
EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
AltName: Full=Accessory protein-like;
Short=AcPL;
AltName: Full=CD218 antigen-like family member B;
AltName: Full=CDw218b;
AltName: Full=IL-1R accessory protein-like {ECO:0000303|PubMed:10653850};
Short=IL-1RAcPL;
AltName: Full=Interleukin-1 receptor 7;
Short=IL-1R-7;
Short=IL-1R7;
AltName: Full=Interleukin-18 receptor accessory protein-like;
AltName: Full=Interleukin-18 receptor beta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
Short=IL-18R-beta;
Short=IL-18Rbeta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
AltName: CD_antigen=CD218b;
Flags: Precursor;
Name=IL18RAP {ECO:0000312|HGNC:HGNC:5989}; Synonyms=IL1R7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=9792649; DOI=10.1074/jbc.273.45.29445;
Born T.L., Thomassen E., Bird T.A., Sims J.E.;
"Cloning of a novel receptor subunit, AcPL, required for interleukin-18
signaling.";
J. Biol. Chem. 273:29445-29450(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
PubMed=17897836; DOI=10.1016/j.cyto.2007.07.186;
Fiszer D., Rozwadowska N., Rychlewski L., Kosicki W., Kurpisz M.;
"Identification of IL-18RAP mRNA truncated splice variants in human testis
and the other human tissues.";
Cytokine 39:178-183(2007).
[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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
Sugano S., Nomura N., Isogai T.;
"NEDO human cDNA sequencing project focused on splicing variants.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
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).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
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).
[8]
TISSUE SPECIFICITY, AND INDUCTION BY IFN-ALPHA AND 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).
[9]
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).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
[11]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 15-356, GLYCOSYLATION AT ASN-119;
ASN-152 AND ASN-345, DISULFIDE BONDS, MUTAGENESIS OF LEU-167; GLU-210;
TYR-212; TYR-214; LYS-313 AND 15-GLU--PRO-176, SUBUNIT, 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, does not mediate IL18-
binding, but involved in IL18-dependent signal transduction, leading to
NF-kappa-B and JNK activation (PubMed:9792649, PubMed:14528293,
PubMed:25500532). May play a role in IL18-mediated IFNG synthesis from
T-helper 1 (Th1) cells (Probable). {ECO:0000269|PubMed:14528293,
ECO:0000269|PubMed:25500532, ECO:0000269|PubMed:9792649,
ECO:0000305|PubMed:10653850}.
-!- 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 IL18R1 (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). {ECO:0000269|PubMed:14528293,
ECO:0000269|PubMed:25500532, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14528293};
Single-pass type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95256-1; Sequence=Displayed;
Name=2;
IsoId=O95256-2; Sequence=VSP_056295;
Name=3; Synonyms=IL-18RAPshort {ECO:0000303|PubMed:17897836};
IsoId=O95256-3; Sequence=VSP_059116, VSP_059117;
Name=4;
IsoId=O95256-4; Sequence=VSP_059114, VSP_059115;
-!- TISSUE SPECIFICITY: Detected in adrenal gland, bone marrow, brain,
fetal brain, fetal liver, heart, kidney, lung, liver, peripheral blood
leukocytes, placenta, prostate, salivary gland, skeletal muscle, spinal
cord, testis, thymus, thyroid, trachea and uterus (PubMed:17897836).
Strongly expressed in peripheral blood leukocytes and spleen and, to a
lesser extent, in colon (PubMed:9792649). Specifically coexpressed with
IL18R1 in T-helper 1 (Th1)cells (PubMed:10925275, PubMed:11046021,
PubMed:10653850). {ECO:0000269|PubMed:10653850,
ECO:0000269|PubMed:10925275, ECO:0000269|PubMed:11046021,
ECO:0000269|PubMed:17897836, ECO:0000269|PubMed:9792649}.
-!- INDUCTION: Induced by IFN-alpha and IL12/interleukin-12 in natural
killer (NK) cells and T-cells. {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. {ECO:0000269|PubMed:25500532}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
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EMBL; AF077346; AAC72196.1; -; mRNA.
EMBL; DQ116957; AAZ52551.1; -; mRNA.
EMBL; AC007278; AAY15080.1; -; Genomic_DNA.
EMBL; AC007248; AAY15049.1; -; Genomic_DNA.
EMBL; CH471127; EAX01791.1; -; Genomic_DNA.
EMBL; AK300026; BAG61837.1; -; mRNA.
EMBL; BC069630; AAH69630.1; -; mRNA.
EMBL; BC106764; AAI06765.1; -; mRNA.
EMBL; BC106765; AAI06766.1; -; mRNA.
EMBL; BC137474; AAI37475.1; -; mRNA.
EMBL; BC137475; AAI37476.1; -; mRNA.
CCDS; CCDS2061.1; -. [O95256-1]
RefSeq; NP_003844.1; NM_003853.3. [O95256-1]
RefSeq; XP_011510389.1; XM_011512087.2. [O95256-2]
RefSeq; XP_011510390.1; XM_011512088.2. [O95256-2]
PDB; 3WO4; X-ray; 3.10 A; C=15-356.
PDB; 6KN9; X-ray; 3.30 A; A/B/C=20-356.
PDBsum; 3WO4; -.
PDBsum; 6KN9; -.
SMR; O95256; -.
BioGRID; 114335; 3.
IntAct; O95256; 4.
STRING; 9606.ENSP00000264260; -.
iPTMnet; O95256; -.
PhosphoSitePlus; O95256; -.
BioMuta; IL18RAP; -.
PaxDb; O95256; -.
PeptideAtlas; O95256; -.
PRIDE; O95256; -.
ProteomicsDB; 50750; -. [O95256-1]
ProteomicsDB; 61717; -.
Antibodypedia; 17791; 354 antibodies.
Ensembl; ENST00000264260; ENSP00000264260; ENSG00000115607. [O95256-1]
Ensembl; ENST00000409369; ENSP00000387201; ENSG00000115607. [O95256-2]
GeneID; 8807; -.
KEGG; hsa:8807; -.
UCSC; uc002tbx.4; human. [O95256-1]
CTD; 8807; -.
DisGeNET; 8807; -.
EuPathDB; HostDB:ENSG00000115607.9; -.
GeneCards; IL18RAP; -.
HGNC; HGNC:5989; IL18RAP.
HPA; ENSG00000115607; Tissue enhanced (blood, bone marrow, lymphoid tissue).
MIM; 604509; gene.
neXtProt; NX_O95256; -.
OpenTargets; ENSG00000115607; -.
PharmGKB; PA29805; -.
eggNOG; ENOG410IGUG; Eukaryota.
eggNOG; ENOG410Y9SN; LUCA.
GeneTree; ENSGT00990000203602; -.
HOGENOM; CLU_025552_2_0_1; -.
InParanoid; O95256; -.
KO; K05174; -.
OMA; YVCDYTQ; -.
OrthoDB; 985064at2759; -.
PhylomeDB; O95256; -.
TreeFam; TF325519; -.
Reactome; R-HSA-9012546; Interleukin-18 signaling.
BioGRID-ORCS; 8807; 2 hits in 787 CRISPR screens.
GeneWiki; IL18RAP; -.
GenomeRNAi; 8807; -.
Pharos; O95256; Tbio.
PRO; PR:O95256; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; O95256; protein.
Bgee; ENSG00000115607; Expressed in bone marrow and 111 other tissues.
ExpressionAtlas; O95256; baseline and differential.
Genevisible; O95256; HS.
GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0032609; P:interferon-gamma production; IEA:Ensembl.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0032635; P:interleukin-6 production; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
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; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF18452; Ig_6; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00409; IG; 2.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
Glycoprotein; Hydrolase; Immunoglobulin domain; Inflammatory response;
Membrane; NAD; Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..19
/evidence="ECO:0000255"
CHAIN 20..599
/note="Interleukin-18 receptor accessory protein"
/id="PRO_0000042185"
TOPO_DOM 20..356
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 357..377
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 378..599
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 149..235
/note="Ig-like C2-type 1"
DOMAIN 251..353
/note="Ig-like C2-type 2"
DOMAIN 406..559
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
ACT_SITE 493
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
CARBOHYD 21
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 119
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
CARBOHYD 152
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
CARBOHYD 345
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
DISULFID 46..126
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
DISULFID 155..180
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
DISULFID 175..221
/evidence="ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532"
DISULFID 180..221
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 273..337
/evidence="ECO:0000244|PDB:3WO4, ECO:0000255|PROSITE-
ProRule:PRU00114, ECO:0000269|PubMed:25500532"
VAR_SEQ 1..142
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_056295"
VAR_SEQ 118..126
/note="VNNSGSYIC -> LGHIFVDPR (in isoform 4)"
/evidence="ECO:0000269|PubMed:17897836"
/id="VSP_059114"
VAR_SEQ 127..599
/note="Missing (in isoform 4)"
/evidence="ECO:0000269|PubMed:17897836"
/id="VSP_059115"
VAR_SEQ 133..149
/note="SPYDVACCVKMILEVKP -> YDPNTFLSENISKSSII (in isoform
3)"
/evidence="ECO:0000269|PubMed:17897836"
/id="VSP_059116"
VAR_SEQ 150..599
/note="Missing (in isoform 3)"
/evidence="ECO:0000269|PubMed:17897836"
/id="VSP_059117"
VARIANT 350
/note="V -> I (in dbSNP:rs11465716)"
/id="VAR_034005"
MUTAGEN 15..176
/note="Missing: Impairs IL18 receptor signaling via NF-
kappa-B."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 167
/note="L->A: Decreases binding to the preformed binary
complex of IL18 and IL18R1."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 210
/note="E->A: Decreases binding to the preformed binary
complex of IL18 and IL18R1. Impairs IL18 receptor signaling
via NF-kappa-B; when associated with A-212 and A-214."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 212
/note="Y->A: Abolishes binding to the preformed binary
complex of IL18 and IL18R1. Impairs IL18 receptor signaling
via NF-kappa-B; when associated with A-210 and A-214."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 214
/note="Y->A: Decreases binding to the preformed binary
complex of IL18 and IL18R1. Impairs IL18 receptor signaling
via NF-kappa-B; when associated with A-210 and A-212."
/evidence="ECO:0000269|PubMed:25500532"
MUTAGEN 313
/note="K->A: Decreases binding to the preformed binary
complex of IL18 and IL18R1. Decreases IL18 receptor
signaling via NF-kappa-B."
/evidence="ECO:0000269|PubMed:25500532"
STRAND 32..36
/evidence="ECO:0000244|PDB:3WO4"
STRAND 41..44
/evidence="ECO:0000244|PDB:3WO4"
STRAND 110..115
/evidence="ECO:0000244|PDB:3WO4"
STRAND 117..120
/evidence="ECO:0000244|PDB:3WO4"
STRAND 122..126
/evidence="ECO:0000244|PDB:3WO4"
STRAND 141..149
/evidence="ECO:0000244|PDB:3WO4"
STRAND 154..157
/evidence="ECO:0000244|PDB:3WO4"
STRAND 161..166
/evidence="ECO:0000244|PDB:3WO4"
STRAND 171..174
/evidence="ECO:0000244|PDB:3WO4"
HELIX 176..178
/evidence="ECO:0000244|PDB:3WO4"
TURN 180..183
/evidence="ECO:0000244|PDB:3WO4"
STRAND 189..193
/evidence="ECO:0000244|PDB:3WO4"
STRAND 203..210
/evidence="ECO:0000244|PDB:3WO4"
HELIX 213..215
/evidence="ECO:0000244|PDB:3WO4"
STRAND 217..224
/evidence="ECO:0000244|PDB:3WO4"
STRAND 233..243
/evidence="ECO:0000244|PDB:3WO4"
STRAND 252..255
/evidence="ECO:0000244|PDB:3WO4"
STRAND 258..263
/evidence="ECO:0000244|PDB:3WO4"
STRAND 269..278
/evidence="ECO:0000244|PDB:3WO4"
STRAND 286..293
/evidence="ECO:0000244|PDB:3WO4"
STRAND 296..299
/evidence="ECO:0000244|PDB:3WO4"
STRAND 306..310
/evidence="ECO:0000244|PDB:3WO4"
STRAND 312..325
/evidence="ECO:0000244|PDB:3WO4"
HELIX 328..331
/evidence="ECO:0000244|PDB:3WO4"
STRAND 333..341
/evidence="ECO:0000244|PDB:3WO4"
STRAND 344..354
/evidence="ECO:0000244|PDB:3WO4"
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


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