IL1AP_RAT
ID IL1AP_RAT Reviewed; 570 AA.
AC Q63621;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Interleukin-1 receptor accessory protein;
DE Short=IL-1 receptor accessory protein;
DE Short=IL-1RAcP;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE Flags: Precursor;
GN Name=Il1rap;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Cervical ganglion;
RX PubMed=8964912; DOI=10.1016/0165-5728(96)00016-1;
RA Liu C., Chalmers D., Maki R., De Souza E.B.;
RT "Rat homolog of mouse interleukin-1 receptor accessory protein: cloning,
RT localization and modulation studies.";
RL J. Neuroimmunol. 66:41-48(1996).
CC -!- FUNCTION: Coreceptor for IL1RL2 in the IL-36 signaling system (By
CC similarity). Coreceptor with IL1R1 in the IL-1 signaling system.
CC Associates with IL1R1 bound to IL1B to form the high affinity
CC interleukin-1 receptor complex which mediates interleukin-1-dependent
CC activation of NF-kappa-B and other pathways. Signaling involves the
CC recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or
CC IRAK2 via the respective TIR domains of the receptor/coreceptor
CC subunits. Recruits TOLLIP to the signaling complex. Does not bind to
CC interleukin-1 alone; binding of IL1RN to IL1R1, prevents its
CC association with IL1R1 to form a signaling complex. The cellular
CC response is modulated through a non-signaling association with the
CC membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33
CC signaling system (By similarity). Can bidirectionally induce pre- and
CC postsynaptic differentiation of neurons by trans-synaptically binding
CC to PTPRD (By similarity). May play a role in IL1B-mediated
CC costimulation of IFNG production from T-helper 1 (Th1) cells (By
CC similarity). {ECO:0000250|UniProtKB:Q61730,
CC ECO:0000250|UniProtKB:Q9NPH3}.
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: The interleukin-36 receptor complex is a heterodimer of IL1RL2
CC and IL1RAP; the association is inhibited by IL36RN (By similarity). The
CC interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP.
CC Associates with IL1R2 to form a non-signaling interleukin-1 receptor
CC complex (By similarity). Interacts with IL-33-bound IL1RL1 to form the
CC minimal interleukin-33 signaling complex with a 1:1:1 stoichiometry.
CC Interacts with KIT (independently of stimulation with KITLG/SCF). A
CC mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex
CC contains IL1RL1, IL1RAP, KIT and MYD88 (By similarity). Interacts (via
CC the first immunoglobilin domain) with PTPRD (via the third
CC immunoglobilin domain); induces pre- and postsynaptic differentiation
CC of neurons (By similarity). {ECO:0000250|UniProtKB:Q61730,
CC ECO:0000250|UniProtKB:Q9NPH3}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in hypothalamus, in the dentate
CC gyrus of hippocampus, cerebral cortex, cerebellum, liver and lung.
CC {ECO:0000269|PubMed:8964912}.
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; U48592; AAB03502.1; -; mRNA.
DR RefSeq; NP_037100.1; NM_012968.1.
DR AlphaFoldDB; Q63621; -.
DR SMR; Q63621; -.
DR BioGRID; 247499; 2.
DR IntAct; Q63621; 1.
DR MINT; Q63621; -.
DR GlyGen; Q63621; 7 sites.
DR PRIDE; Q63621; -.
DR GeneID; 25466; -.
DR KEGG; rno:25466; -.
DR UCSC; RGD:2893; rat.
DR CTD; 3556; -.
DR RGD; 2893; Il1rap.
DR InParanoid; Q63621; -.
DR PhylomeDB; Q63621; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-9014826; Interleukin-36 pathway.
DR Reactome; R-RNO-9014843; Interleukin-33 signaling.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR PRO; PR:Q63621; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019966; F:interleukin-1 binding; TAS:RGD.
DR GO; GO:0004908; F:interleukin-1 receptor activity; ISO:RGD.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IPI:RGD.
DR GO; GO:0002114; F:interleukin-33 receptor activity; ISO:RGD.
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:0030674; F:protein-macromolecule adaptor activity; TAS:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0038172; P:interleukin-33-mediated signaling pathway; ISO:RGD.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:RGD.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:RGD.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; ISO: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; 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; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Inflammatory response; Membrane; NAD; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..570
FT /note="Interleukin-1 receptor accessory protein"
FT /id="PRO_0000015453"
FT TOPO_DOM 21..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 243..348
FT /note="Ig-like C2-type 3"
FT DOMAIN 403..546
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 69..85
FT /note="Essential for interaction with PTPRD"
FT /evidence="ECO:0000250|UniProtKB:Q61730"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPH3"
FT CARBOHYD 57
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 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 47..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 266..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 570 AA; 65599 MW; 20C3A5478127AABE CRC64;
MGLPWCLMSL FFCGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKYNYST
AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT
YCSKVAFPLE VVQKDSCFNS PMRLPVHRLY IEQGIHNITC PNVDGYFPSS VKPSVTWYKG
CTEIVNFHNV QPKGMNLSFF IPLVSNNGNY TCVVTYLENG RLFHLTRTMT VKVVGSPKDA
VPPHIYSPND RVVYEKEPGE ELVIPCKVYF SFIMDSHNEI WWTIDGKKPD DVPVDITIIE
SVSYSSTEDE TRTQILSIKK VTPEDLKRNY VCHARNAEGE AEQAAKVKQK VIPPRYTVEL
ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNAEEEEF
VLLTLRGVLE NEFGYKLCIF DRDSFPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL
LELKAGLENM ASRGNINVIL VQYKAVKDLK VKELKRAKSV LTVIKWKGEK SKYPQGRFWK
QLQVAMPVKK SPRWSSSDKQ GLSYSSLKNV
