IL18R_MOUSE
ID IL18R_MOUSE Reviewed; 537 AA.
AC Q61098;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Interleukin-18 receptor 1;
DE Short=IL-18R-1;
DE Short=IL-18R1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=CD218 antigen-like family member A;
DE AltName: Full=IL1 receptor-related protein;
DE Short=IL-1Rrp;
DE Short=IL1R-rp;
DE AltName: Full=Interleukin-18 receptor alpha;
DE Short=IL-18R-alpha;
DE Short=IL-18Ralpha;
DE AltName: CD_antigen=CD218a;
DE Flags: Precursor;
GN Name=Il18r1 {ECO:0000312|MGI:MGI:105383};
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 VARIANT ALA-317 DEL.
RX PubMed=8626725; DOI=10.1074/jbc.271.8.3967;
RA Parnet P., Garka K.E., Bonnert T.P., Dower S.K., Sims J.E.;
RT "IL-1Rrp is a novel receptor-like molecule similar to the type I
RT interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP.";
RL J. Biol. Chem. 271:3967-3970(1996).
RN [2]
RP INTERACTION WITH SLC12A3.
RX PubMed=26099046; DOI=10.1038/nm.3890;
RA Wang J., Sun C., Gerdes N., Liu C., Liao M., Liu J., Shi M.A., He A.,
RA Zhou Y., Sukhova G.K., Chen H., Cheng X.W., Kuzuya M., Murohara T.,
RA Zhang J., Cheng X., Jiang M., Shull G.E., Rogers S., Yang C.L., Ke Q.,
RA Jelen S., Bindels R., Ellison D.H., Jarolim P., Libby P., Shi G.P.;
RT "Interleukin 18 function in atherosclerosis is mediated by the interleukin
RT 18 receptor and the Na-Cl co-transporter.";
RL Nat. Med. 21:820-826(2015).
CC -!- FUNCTION: Within the IL18 receptor complex, responsible for the binding
CC of the pro-inflammatory cytokine IL18, but not IL1A nor IL1B. Involved
CC in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (By
CC similarity). Contributes to IL18-induced cytokine production, either
CC independently of SLC12A3, or as a complex with SLC12A3
CC (PubMed:26099046). {ECO:0000250|UniProtKB:Q13478,
CC ECO:0000269|PubMed:26099046}.
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 IL18RAP (By similarity).
CC Within this complex, IL18R1 is involved in ligand-binding and IL18RAP
CC in signaling leading to NF-kappa-B and JNK activation (By similarity).
CC Interacts with SLC12A3 in peritoneal macrophages; this interaction is
CC increased by IL18 treatment (PubMed:26099046).
CC {ECO:0000250|UniProtKB:Q13478, ECO:0000269|PubMed:26099046}.
CC -!- INTERACTION:
CC Q61098; P59158: Slc12a3; NbExp=5; IntAct=EBI-13612516, EBI-8366645;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q13478}; Single-
CC 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 -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; U43673; AAC52437.1; -; mRNA.
DR CCDS; CCDS35549.1; -.
DR RefSeq; NP_032391.1; NM_008365.2.
DR RefSeq; XP_006495790.1; XM_006495727.3.
DR RefSeq; XP_006495791.1; XM_006495728.3.
DR RefSeq; XP_006495792.1; XM_006495729.3.
DR RefSeq; XP_006495793.1; XM_006495730.3.
DR RefSeq; XP_006495795.1; XM_006495732.3.
DR RefSeq; XP_006495797.1; XM_006495734.3.
DR AlphaFoldDB; Q61098; -.
DR SMR; Q61098; -.
DR IntAct; Q61098; 1.
DR STRING; 10090.ENSMUSP00000103679; -.
DR GlyGen; Q61098; 10 sites.
DR PhosphoSitePlus; Q61098; -.
DR EPD; Q61098; -.
DR MaxQB; Q61098; -.
DR PaxDb; Q61098; -.
DR PRIDE; Q61098; -.
DR ProteomicsDB; 269468; -.
DR Antibodypedia; 2363; 822 antibodies from 36 providers.
DR DNASU; 16182; -.
DR Ensembl; ENSMUST00000087983; ENSMUSP00000085298; ENSMUSG00000026070.
DR Ensembl; ENSMUST00000108044; ENSMUSP00000103679; ENSMUSG00000026070.
DR Ensembl; ENSMUST00000195684; ENSMUSP00000142070; ENSMUSG00000026070.
DR GeneID; 16182; -.
DR KEGG; mmu:16182; -.
DR UCSC; uc011wjz.1; mouse.
DR CTD; 8809; -.
DR MGI; MGI:105383; Il18r1.
DR VEuPathDB; HostDB:ENSMUSG00000026070; -.
DR eggNOG; ENOG502QUAC; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_025552_3_1_1; -.
DR InParanoid; Q61098; -.
DR OMA; ECGPENG; -.
DR OrthoDB; 985064at2759; -.
DR PhylomeDB; Q61098; -.
DR TreeFam; TF325519; -.
DR BioGRID-ORCS; 16182; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Il18r1; mouse.
DR PRO; PR:Q61098; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61098; protein.
DR Bgee; ENSMUSG00000026070; Expressed in right lung lobe and 52 other tissues.
DR ExpressionAtlas; Q61098; baseline and differential.
DR Genevisible; Q61098; MM.
DR GO; GO:0045092; C:interleukin-18 receptor complex; ISO:MGI.
DR GO; GO:0042007; F:interleukin-18 binding; ISS:UniProtKB.
DR GO; GO:0042008; F:interleukin-18 receptor activity; IMP:MGI.
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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IMP:MGI.
DR GO; GO:0030101; P:natural killer cell activation; IMP:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Inflammatory response; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..537
FT /note="Interleukin-18 receptor 1"
FT /id="PRO_0000015449"
FT TOPO_DOM 20..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..102
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..189
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..312
FT /note="Ig-like C2-type 3"
FT DOMAIN 370..516
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..41
FT /evidence="ECO:0000250|UniProtKB:Q13478"
FT DISULFID 120..159
FT /evidence="ECO:0000250|UniProtKB:Q13478"
FT DISULFID 141..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 317
FT /note="Missing"
SQ SEQUENCE 537 AA; 61601 MW; B119FEA403355458 CRC64;
MHHEELILTL CILIVKSASK SCIHRSQIHV VEGEPFYLKP CGISAPVHRN ETATMRWFKG
SASHEYRELN NRSSPRVTFH DHTLEFWPVE MEDEGTYISQ VGNDRRNWTL NVTKRNKHSC
FSDKLVTSRD VEVNKSLHIT CKNPNYEELI QDTWLYKNCK EISKTPRILK DAEFGDEGYY
SCVFSVHHNG TRYNITKTVN ITVIEGRSKV TPAILGPKCE KVGVELGKDV ELNCSASLNK
DDLFYWSIRK EDSSDPNVQE DRKETTTWIS EGKLHASKIL RFQKITENYL NVLYNCTVAN
EEAIDTKSFV LVRKEIPDIP GHVFTGGVTV LVLASVAAVC IVILCVIYKV DLVLFYRRIA
ERDETLTDGK TYDAFVSYLK ECHPENKEEY TFAVETLPRV LEKQFGYKLC IFERDVVPGG
AVVEEIHSLI EKSRRLIIVL SQSYLTNGAR RELESGLHEA LVERKIKIIL IEFTPASNIT
FLPPSLKLLK SYRVLKWRAD SPSMNSRFWK NLVYLMPAKA VKPWREESEA RSVLSAP
