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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) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)

 I18RA_MOUSE             Reviewed;         614 AA.
Q9Z2B1;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
17-JUN-2020, entry version 149.
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=IL-1R accessory protein-like;
Short=IL-1RAcPL;
AltName: Full=Interleukin-18 receptor accessory protein-like;
AltName: Full=Interleukin-18 receptor beta;
Short=IL-18R-beta;
Short=IL-18Rbeta;
AltName: CD_antigen=CD218b;
Flags: Precursor;
Name=Il18rap {ECO:0000312|MGI:MGI:1338888};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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]
FUNCTION.
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).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15843532; DOI=10.4049/jimmunol.174.9.5351;
Cheung H., Chen N.-J., Cao Z., Ono N., Ohashi P.S., Yeh W.-C.;
"Accessory protein-like is essential for IL-18-mediated signaling.";
J. Immunol. 174:5351-5357(2005).
-!- 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:11046021, PubMed:15843532,
PubMed:9792649). May play a role in IL18-mediated IFNG synthesis from
T-helper 1 (Th1) cells (By similarity). {ECO:0000250|UniProtKB:O95256,
ECO:0000269|PubMed:11046021, ECO:0000269|PubMed:15843532,
ECO:0000269|PubMed:9792649}.
-!- 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. Within this
complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling
leading to NF-kappa-B and JNK activation.
{ECO:0000250|UniProtKB:O95256}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95256};
Single-pass type I membrane protein {ECO:0000305}.
-!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
Self-association of TIR domains is required for NADase activity.
{ECO:0000255|PROSITE-ProRule:PRU00204}.
-!- DISRUPTION PHENOTYPE: Impaired IL-18 signaling.
{ECO:0000269|PubMed:15843532}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
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EMBL; AF077347; AAC72197.1; -; mRNA.
CCDS; CCDS14912.1; -.
RefSeq; NP_034683.1; NM_010553.4.
STRING; 10090.ENSMUSP00000027237; -.
iPTMnet; Q9Z2B1; -.
PhosphoSitePlus; Q9Z2B1; -.
EPD; Q9Z2B1; -.
jPOST; Q9Z2B1; -.
PaxDb; Q9Z2B1; -.
PRIDE; Q9Z2B1; -.
Antibodypedia; 17791; 354 antibodies.
Ensembl; ENSMUST00000027237; ENSMUSP00000027237; ENSMUSG00000026068.
GeneID; 16174; -.
KEGG; mmu:16174; -.
UCSC; uc007auk.2; mouse.
CTD; 8807; -.
MGI; MGI:1338888; Il18rap.
eggNOG; ENOG410IGUG; Eukaryota.
eggNOG; ENOG410Y9SN; LUCA.
GeneTree; ENSGT00990000203602; -.
HOGENOM; CLU_025552_2_0_1; -.
InParanoid; Q9Z2B1; -.
KO; K05174; -.
OMA; YVCDYTQ; -.
OrthoDB; 985064at2759; -.
PhylomeDB; Q9Z2B1; -.
TreeFam; TF325519; -.
BioGRID-ORCS; 16174; 0 hits in 12 CRISPR screens.
PRO; PR:Q9Z2B1; -.
Proteomes; UP000000589; Chromosome 1.
RNAct; Q9Z2B1; protein.
Bgee; ENSMUSG00000026068; Expressed in blood and 42 other tissues.
Genevisible; Q9Z2B1; MM.
GO; GO:0045092; C:interleukin-18 receptor complex; ISO:MGI.
GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
GO; GO:0042008; F:interleukin-18 receptor activity; ISS: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; IMP:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071351; P:cellular response to interleukin-18; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0032609; P:interferon-gamma production; IMP:MGI.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IMP:MGI.
GO; GO:0032635; P:interleukin-6 production; IMP:MGI.
GO; GO:0042119; P:neutrophil activation; IMP:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IMP:MGI.
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; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF00047; ig; 1.
Pfam; PF18452; Ig_6; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01536; INTRLKN1R12F.
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.
2: Evidence at transcript level;
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..614
/note="Interleukin-18 receptor accessory protein"
/id="PRO_0000042186"
TOPO_DOM 20..356
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 357..377
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 378..614
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 148..234
/note="Ig-like C2-type 1"
DOMAIN 250..352
/note="Ig-like C2-type 2"
DOMAIN 405..558
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
ACT_SITE 492
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
CARBOHYD 21
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 151
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 227
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 344
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 46..126
/evidence="ECO:0000250|UniProtKB:O95256"
DISULFID 154..179
/evidence="ECO:0000250|UniProtKB:O95256"
DISULFID 174..220
/evidence="ECO:0000250|UniProtKB:O95256"
DISULFID 179..220
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 272..336
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SEQUENCE 614 AA; 70094 MW; B71D005E4FA99BA1 CRC64;
MLCLGWVFLW FVAGEKTTGF NHSACATKKL LWTYSARGAE NFVLFCDLQE LQEQKFSHAS
QLSPTQSPAH KPCSGSQKDL SDVQWYMQPR SGSPLEEISR NSPHMQSEGM LHILAPQTNS
IWSYICRPRI RSPQDMACCI KTVLEVKPQR NVSCGNTAQD EQVLLLGSTG SIHCPSLSCQ
SDVQSPEMTW YKDGRLLPEH KKNPIEMADI YVFNQGLYVC DYTQSDNVSS WTVRAVVKVR
TIGKDINVKP EILDPITDTL DVELGKPLTL PCRVQFGFQR LSKPVIKWYV KESTQEWEMS
VFEEKRIQST FKNEVIERTI FLREVTQRDL SRKFVCFAQN SIGNTTRTIR LRKKEEVVFV
YILLGTALML VGVLVAAAFL YWYWIEVVLL CRTYKNKDET LGDKKEFDAF VSYSNWSSPE
TDAVGSLSEE HLALNLFPEV LEDTYGYRLC LLDRDVTPGG VYADDIVSII KKSRRGIFIL
SPSYLNGPRV FELQAAVNLA LVDQTLKLIL IKFCSFQEPE SLPYLVKKAL RVLPTVTWKG
LKSVHASSRF WTQIRYHMPV KNSNRFMFNG LRIFLKGFSP EKDLVTQKPL EGMPKSGNDH
GAQNLLLYSD QKRC


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