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Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (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.
02-JUN-2021, entry version 177.
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}.
-!- INTERACTION:
O95256; O76024: WFS1; NbExp=4; IntAct=EBI-21018056, EBI-720609;
-!- 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; -.
SASBDB; O95256; -.
SMR; O95256; -.
BioGRID; 114335; 4.
IntAct; O95256; 5.
STRING; 9606.ENSP00000264260; -.
GlyGen; O95256; 4 sites.
iPTMnet; O95256; -.
PhosphoSitePlus; O95256; -.
BioMuta; IL18RAP; -.
PaxDb; O95256; -.
PeptideAtlas; O95256; -.
PRIDE; O95256; -.
ProteomicsDB; 50750; -. [O95256-1]
ProteomicsDB; 61717; -.
ABCD; O95256; 3 sequenced antibodies.
Antibodypedia; 17791; 385 antibodies.
DNASU; 8807; -.
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; -.
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; -.
VEuPathDB; HostDB:ENSG00000115607.9; -.
eggNOG; ENOG502QUSU; Eukaryota.
GeneTree; ENSGT01030000234568; -.
HOGENOM; CLU_025552_2_0_1; -.
InParanoid; O95256; -.
OMA; YVCDYTQ; -.
OrthoDB; 985064at2759; -.
PhylomeDB; O95256; -.
TreeFam; TF325519; -.
PathwayCommons; O95256; -.
Reactome; R-HSA-9012546; Interleukin-18 signaling.
BioGRID-ORCS; 8807; 3 hits in 996 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 130 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:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
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.
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; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR041416; IL-1RAcP-like_ig.
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; 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:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
CARBOHYD 152
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
CARBOHYD 345
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
DISULFID 46..126
/evidence="ECO:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
DISULFID 155..180
/evidence="ECO:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
DISULFID 175..221
/evidence="ECO:0000269|PubMed:25500532,
ECO:0007744|PDB:3WO4"
DISULFID 180..221
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 273..337
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:25500532, ECO:0007744|PDB:3WO4"
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:0007829|PDB:3WO4"
STRAND 41..44
/evidence="ECO:0007829|PDB:3WO4"
STRAND 110..115
/evidence="ECO:0007829|PDB:3WO4"
STRAND 117..120
/evidence="ECO:0007829|PDB:3WO4"
STRAND 122..126
/evidence="ECO:0007829|PDB:3WO4"
STRAND 141..149
/evidence="ECO:0007829|PDB:3WO4"
STRAND 154..157
/evidence="ECO:0007829|PDB:3WO4"
STRAND 161..166
/evidence="ECO:0007829|PDB:3WO4"
STRAND 171..174
/evidence="ECO:0007829|PDB:3WO4"
HELIX 176..178
/evidence="ECO:0007829|PDB:3WO4"
TURN 180..183
/evidence="ECO:0007829|PDB:3WO4"
STRAND 189..193
/evidence="ECO:0007829|PDB:3WO4"
STRAND 196..199
/evidence="ECO:0007829|PDB:6KN9"
STRAND 203..210
/evidence="ECO:0007829|PDB:3WO4"
HELIX 213..215
/evidence="ECO:0007829|PDB:3WO4"
STRAND 217..224
/evidence="ECO:0007829|PDB:3WO4"
STRAND 233..243
/evidence="ECO:0007829|PDB:3WO4"
STRAND 252..255
/evidence="ECO:0007829|PDB:3WO4"
STRAND 258..263
/evidence="ECO:0007829|PDB:3WO4"
STRAND 269..278
/evidence="ECO:0007829|PDB:3WO4"
STRAND 286..293
/evidence="ECO:0007829|PDB:3WO4"
STRAND 296..299
/evidence="ECO:0007829|PDB:3WO4"
STRAND 306..310
/evidence="ECO:0007829|PDB:3WO4"
STRAND 312..325
/evidence="ECO:0007829|PDB:3WO4"
HELIX 328..331
/evidence="ECO:0007829|PDB:3WO4"
STRAND 333..341
/evidence="ECO:0007829|PDB:3WO4"
STRAND 344..354
/evidence="ECO:0007829|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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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP2328: Allograft rejection
WP210: Cytoplasmic Ribosomal Proteins
WP566: canonical wnt - zebrafish
WP362: TGF-beta Receptor Signaling Pathway
WP2218: sGC
WP258: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1566: Citrate cycle (TCA cycle)
WP1367: TGF-beta Receptor Signaling Pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP138: Androgen receptor signaling pathway
WP1675: Nitrogen metabolism
WP1939: Unfolded Protein Response
WP1004: Kit Receptor Signaling Pathway
WP774: Kit Receptor Signaling Pathway
WP2199: Seed Development
WP68: Androgen Receptor Signaling Pathway
WP908: B Cell Receptor Signaling Pathway
WP1625: Base excision repair
WP732: Serotonin Receptor 2 and ELK-SRF/GATA4 signaling

Related Genes :
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (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)
[IL18R1 IL1RRP] 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)
[Il18r1] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (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)
[IL1RAP C3orf13 IL1R3] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (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) (EC 3.2.2.6) (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) (EC 3.2.2.6) (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] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[IL1RAPL1 OPHN4] Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (EC 3.2.2.6) (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) (EC 3.2.2.6)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6)
[Il1rl2] Interleukin-1 receptor-like 2 (EC 3.2.2.6) (IL-36 receptor) (Interleukin-1 receptor-related protein 2) (IL-1Rrp2) (IL1R-rp2)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[Il1rl1 Ly84 St2 Ste2] Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL13RA1 IL13R IL13RA] Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL37 FIL1Z IL1F7 IL1H4 IL1RP1] Interleukin-37 (IL-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-23)
[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)
[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)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL6R] Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[IL7R] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CDw127) (CD antigen CD127)
[IL17RD IL17RLM SEF UNQ6115/PRO20026] Interleukin-17 receptor D (IL-17 receptor D) (IL-17RD) (IL17Rhom) (Interleukin-17 receptor-like protein) (Sef homolog) (hSef)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)

Bibliography :
No related Items