ILRL1_RAT
ID ILRL1_RAT Reviewed; 566 AA.
AC Q62611; Q62612;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Interleukin-1 receptor-like 1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Fit-1;
DE AltName: Full=Fos-responsive gene 1 protein;
DE Flags: Precursor;
GN Name=Il1rl1; Synonyms=Fit1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=8131748; DOI=10.1002/j.1460-2075.1994.tb06367.x;
RA Bergers G., Reikersdorfer A., Braselmann S., Graninger P., Busslinger M.;
RT "Alternative promoter usage of the Fos-responsive gene Fit-1 generates mRNA
RT isoforms coding for either secreted or membrane-bound proteins related to
RT the IL-1 receptor.";
RL EMBO J. 13:1176-1188(1994).
CC -!- FUNCTION: Receptor for interleukin-33 (IL-33), its stimulation recruits
CC MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of
CC MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in
CC helper T-cell function (By similarity). {ECO:0000250|UniProtKB:Q01638}.
CC -!- FUNCTION: [Isoform B]: Inhibits IL-33 signaling.
CC {ECO:0000250|UniProtKB:P14719}.
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: Interacts with MYD88, IRAK1, IRAK4, and TRAF6 (By similarity).
CC Bound to its ligand IL-33, interacts with IL1RAP to form the minimal
CC interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts
CC with KIT (bound to KITLG/SCF). A mast cell-specific KITLG/SCF-induced
CC interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88
CC (By similarity). Interacts with TMED1 (By similarity).
CC {ECO:0000250|UniProtKB:P14719, ECO:0000250|UniProtKB:Q01638}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Membrane-bound, Fit-1M;
CC IsoId=Q62611-1; Sequence=Displayed;
CC Name=B; Synonyms=Soluble, Fit-1S;
CC IsoId=Q62611-2; Sequence=VSP_002670, VSP_002671;
CC -!- TISSUE SPECIFICITY: Isoform A is detected in spleen, lung, bone marrow
CC and lymh node. Isoform B is predominant in fibroblasts.
CC -!- INDUCTION: By FOS.
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; U04317; AAA18480.1; -; mRNA.
DR EMBL; U04319; AAA67172.1; -; mRNA.
DR PIR; S42632; S42632.
DR PIR; S42633; S42633.
DR RefSeq; NP_001121161.1; NM_001127689.1. [Q62611-1]
DR RefSeq; NP_037169.1; NM_013037.1. [Q62611-2]
DR AlphaFoldDB; Q62611; -.
DR SMR; Q62611; -.
DR STRING; 10116.ENSRNOP00000020144; -.
DR GlyGen; Q62611; 6 sites.
DR PhosphoSitePlus; Q62611; -.
DR PaxDb; Q62611; -.
DR PRIDE; Q62611; -.
DR GeneID; 25556; -.
DR KEGG; rno:25556; -.
DR UCSC; RGD:2894; rat. [Q62611-1]
DR CTD; 9173; -.
DR RGD; 2894; Il1rl1.
DR eggNOG; ENOG502RU6H; Eukaryota.
DR InParanoid; Q62611; -.
DR PhylomeDB; Q62611; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-9014843; Interleukin-33 signaling.
DR PRO; PR:Q62611; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004908; F:interleukin-1 receptor activity; IEA:InterPro.
DR GO; GO:0002113; F:interleukin-33 binding; ISO:RGD.
DR GO; GO:0002114; F:interleukin-33 receptor activity; IBA:GO_Central.
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:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; ISO:RGD.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; ISO:RGD.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
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; IPR003598; Ig_sub2.
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; 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 PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW NAD; Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..566
FT /note="Interleukin-1 receptor-like 1"
FT /id="PRO_0000015444"
FT TOPO_DOM 27..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..109
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..207
FT /note="Ig-like C2-type 2"
FT DOMAIN 217..323
FT /note="Ig-like C2-type 3"
FT DOMAIN 379..539
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 204..216
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT ACT_SITE 465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
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 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 117..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 240..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 328..336
FT /note="IDHQSTYYI -> SKECLSQIA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8131748"
FT /id="VSP_002670"
FT VAR_SEQ 337..566
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8131748"
FT /id="VSP_002671"
SQ SEQUENCE 566 AA; 64406 MW; 50554A29437A0C31 CRC64;
MIGKWRMGLW ALAILTVPMY FIVTEGRKTS WGLENEALIV RCPQRGGAIN PVEWYYSNTN
ERIPTQKRNR IFVSRDRLKF LPAKVEDSGI YTCVIRSPES IKTGSLNVTI YKRPPNCKIP
DYMMYSTVDG SDKNSKITCP TIALYNWTAP VQWFKNCKAL QGPRFRAHMS YLFIDKVSHV
DEGDYTCRFT HTENGTNYIV TATRSFTVEE KGFSTFPVIT NPPHNYTVEV EIGKTANIAC
SACFGTASQF VAVLWQINKT RIGSFGKARI QEEKGPNKSS SNGMICLTSL LRITGVTDKD
FSLKYDCVAM NHHGVIRHPV RLRRKQPIDH QSTYYIVAGC SLLLMFINVL VIVLKVFWIE
VALFWRDIMA PYKTQNDGKL YDAYIIYPRV FRGSAAGTGS VEYFVHYTLP DVLENKCGYK
LCIYGRDLLP GQDAATVVES SIQNSRRQVF VLAPHMMHSK EFAYEQEIAL HSALIQNNSK
VILIEMEPMG EASRLQLGDL QDSLQHLVKM QGTIKWREDH VADKQSLSSK FWKHVRYQMP
VPKRPPKMAS VAAPLSGKVC LDLKHF
