I18RA_MOUSE
ID I18RA_MOUSE Reviewed; 614 AA.
AC Q9Z2B1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
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=IL-1R accessory protein-like;
DE Short=IL-1RAcPL;
DE AltName: Full=Interleukin-18 receptor accessory protein-like;
DE AltName: Full=Interleukin-18 receptor beta;
DE Short=IL-18R-beta;
DE Short=IL-18Rbeta;
DE AltName: CD_antigen=CD218b;
DE Flags: Precursor;
GN Name=Il18rap {ECO:0000312|MGI:MGI:1338888};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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 FUNCTION.
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15843532; DOI=10.4049/jimmunol.174.9.5351;
RA Cheung H., Chen N.-J., Cao Z., Ono N., Ohashi P.S., Yeh W.-C.;
RT "Accessory protein-like is essential for IL-18-mediated signaling.";
RL J. Immunol. 174:5351-5357(2005).
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:11046021, PubMed:15843532,
CC PubMed:9792649). May play a role in IL18-mediated IFNG synthesis from
CC T-helper 1 (Th1) cells (By similarity). {ECO:0000250|UniProtKB:O95256,
CC ECO:0000269|PubMed:11046021, ECO:0000269|PubMed:15843532,
CC ECO:0000269|PubMed:9792649}.
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. Within this
CC complex, IL18R1 is involved in ligand-binding and IL18RAP in signaling
CC leading to NF-kappa-B and JNK activation.
CC {ECO:0000250|UniProtKB:O95256}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95256};
CC Single-pass type I membrane protein {ECO:0000305}.
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 -!- DISRUPTION PHENOTYPE: Impaired IL-18 signaling.
CC {ECO:0000269|PubMed:15843532}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; AF077347; AAC72197.1; -; mRNA.
DR CCDS; CCDS14912.1; -.
DR RefSeq; NP_034683.1; NM_010553.4.
DR AlphaFoldDB; Q9Z2B1; -.
DR SMR; Q9Z2B1; -.
DR STRING; 10090.ENSMUSP00000027237; -.
DR GlyGen; Q9Z2B1; 4 sites.
DR iPTMnet; Q9Z2B1; -.
DR PhosphoSitePlus; Q9Z2B1; -.
DR EPD; Q9Z2B1; -.
DR jPOST; Q9Z2B1; -.
DR PaxDb; Q9Z2B1; -.
DR PRIDE; Q9Z2B1; -.
DR Antibodypedia; 17791; 388 antibodies from 30 providers.
DR DNASU; 16174; -.
DR Ensembl; ENSMUST00000027237; ENSMUSP00000027237; ENSMUSG00000026068.
DR GeneID; 16174; -.
DR KEGG; mmu:16174; -.
DR UCSC; uc007auk.2; mouse.
DR CTD; 8807; -.
DR MGI; MGI:1338888; Il18rap.
DR VEuPathDB; HostDB:ENSMUSG00000026068; -.
DR eggNOG; ENOG502QUSU; Eukaryota.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_2_0_1; -.
DR InParanoid; Q9Z2B1; -.
DR OMA; EPQKSHF; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; Q9Z2B1; -.
DR TreeFam; TF325519; -.
DR BioGRID-ORCS; 16174; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9Z2B1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9Z2B1; protein.
DR Bgee; ENSMUSG00000026068; Expressed in granulocyte and 32 other tissues.
DR ExpressionAtlas; Q9Z2B1; baseline and differential.
DR Genevisible; Q9Z2B1; MM.
DR GO; GO:0045092; C:interleukin-18 receptor complex; ISO:MGI.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0042008; F:interleukin-18 receptor activity; ISS: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; IMP:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071351; P:cellular response to interleukin-18; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IMP:MGI.
DR GO; GO:0042119; P:neutrophil activation; IMP:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR004074; IL-1_rcpt_I/II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Inflammatory response; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..614
FT /note="Interleukin-18 receptor accessory protein"
FT /id="PRO_0000042186"
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..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 148..234
FT /note="Ig-like C2-type 1"
FT DOMAIN 250..352
FT /note="Ig-like C2-type 2"
FT DOMAIN 405..558
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..126
FT /evidence="ECO:0000250|UniProtKB:O95256"
FT DISULFID 154..179
FT /evidence="ECO:0000250|UniProtKB:O95256"
FT DISULFID 174..220
FT /evidence="ECO:0000250|UniProtKB:O95256"
FT DISULFID 179..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
