IL1R1_RAT
ID IL1R1_RAT Reviewed; 576 AA.
AC Q02955;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Interleukin-1 receptor type 1;
DE Short=IL-1R-1;
DE Short=IL-1RT-1;
DE Short=IL-1RT1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=CD121 antigen-like family member A;
DE AltName: Full=Interleukin-1 receptor alpha;
DE Short=IL-1R-alpha;
DE AltName: Full=Interleukin-1 receptor type I;
DE AltName: Full=p80;
DE AltName: CD_antigen=CD121a;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 1, membrane form;
DE Short=mIL-1R1;
DE Short=mIL-1RI;
DE Contains:
DE RecName: Full=Interleukin-1 receptor type 1, soluble form;
DE Short=sIL-1R1;
DE Short=sIL-1RI;
DE Flags: Precursor;
GN Name=Il1r1; Synonyms=Il1ra;
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].
RC TISSUE=Ganglion;
RX PubMed=7684399; DOI=10.1016/0165-5728(93)90267-3;
RA Hart R.P., Liu C., Shadiack A.M., McCormack R.J., Jonakait G.M.;
RT "An mRNA homologous to interleukin-1 receptor type I is expressed in
RT cultured rat sympathetic ganglia.";
RL J. Neuroimmunol. 44:49-56(1993).
CC -!- FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to
CC interleukin-1 associates with the coreceptor IL1RAP to form the high
CC affinity interleukin-1 receptor complex which mediates interleukin-1-
CC dependent activation of NF-kappa-B, MAPK and other pathways. Signaling
CC involves the recruitment of adapter molecules such as TOLLIP, MYD88,
CC and IRAK1 or IRAK2 via the respective TIR domains of the
CC receptor/coreceptor subunits. Binds ligands with comparable affinity
CC and binding of antagonist IL1RN prevents association with IL1RAP to
CC form a signaling complex. Involved in IL1B-mediated costimulation of
CC IFNG production from T-helper 1 (Th1) cells (By similarity).
CC {ECO:0000250|UniProtKB:P14778}.
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-1 receptor complex is a heterodimer of IL1R1
CC and IL1RAP. Interacts with PIK3R1. Interacts with IL1A (By similarity).
CC {ECO:0000250|UniProtKB:P14778}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000305}. Secreted {ECO:0000250}.
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 -!- PTM: A soluble form (sIL1R1) is probably produced by proteolytic
CC cleavage at the cell surface (shedding). {ECO:0000250}.
CC -!- PTM: Rapidly phosphorylated on Tyr-499 in response to IL-1, which
CC creates a SH2 binding site for the PI 3-kinase regulatory subunit
CC PIK3R1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M95578; AAA16196.1; ALT_INIT; mRNA.
DR PIR; I56526; I56526.
DR AlphaFoldDB; Q02955; -.
DR SMR; Q02955; -.
DR STRING; 10116.ENSRNOP00000019673; -.
DR GlyGen; Q02955; 5 sites.
DR PaxDb; Q02955; -.
DR PRIDE; Q02955; -.
DR UCSC; RGD:2892; rat.
DR RGD; 2892; Il1r1.
DR eggNOG; ENOG502QWEU; Eukaryota.
DR InParanoid; Q02955; -.
DR PhylomeDB; Q02955; -.
DR Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR PRO; PR:Q02955; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019966; F:interleukin-1 binding; ISO:RGD.
DR GO; GO:0004908; F:interleukin-1 receptor activity; ISO:RGD.
DR GO; GO:0004909; F:interleukin-1, type I, activating receptor activity; IEA:InterPro.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI: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:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010286; P:heat acclimation; IMP:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:RGD.
DR GO; GO:0030728; P:ovulation; IEP:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:2000661; P:positive regulation of interleukin-1-mediated signaling pathway; ISO:RGD.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:RGD.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISO:RGD.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0071731; P:response to nitric oxide; IEP:RGD.
DR GO; GO:1990834; P:response to odorant; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IMP:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; 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; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004076; IL-1_rcpt_I-typ.
DR InterPro; IPR004074; IL-1_rcpt_I/II-typ.
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; PF01582; TIR; 1.
DR PRINTS; PR01538; INTRLEUKN1R1.
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; 3.
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;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..576
FT /note="Interleukin-1 receptor type 1, membrane form"
FT /id="PRO_0000015437"
FT CHAIN 20..?
FT /note="Interleukin-1 receptor type 1, soluble form"
FT /id="PRO_0000415346"
FT TOPO_DOM 20..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..217
FT /note="Ig-like C2-type 2"
FT DOMAIN 229..331
FT /note="Ig-like C2-type 3"
FT DOMAIN 386..541
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14778"
FT MOD_RES 556
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P13504"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 46..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 251..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 576 AA; 66759 MW; 55BE20C92385A34A CRC64;
MENMKVLLGF ICLIVPLLSL ETDKCTEYPN EVISFSSVNE IDIRSCPLTP NEMHGGTIIW
YKNDSKTPIS ADKDSRIHQQ NEHLWFVPAK MEDSGYYYCI MRNSTYCLKT KITMSVLEND
PGLCYNTQAS FIQRLHVAGD GSLVCPYLDF FKDENNELPK VQWYKNCKPL PLDDGNFFGF
KNKLMVMNVA EEHRGNYTCR TSYTYQGKQY PVTRVITFIT IDDSKRDRPV IMSPRNETME
ADPGSTIQLI CNVTGQFTDL VYWKWNGSEI EWDDPILAED YQFLEHPSAK RKYTLITTLN
VSEVKSQFYR YPFICFVKNT HILETAHVRL VYPVPDFKNY LIGGFAIFTA TAVFCACIYK
VFKVDIVLWY RDSCSDFLPR KASDGRTYDA YVLYPKTYGE GSFAYLDTFV FKLLPEVLEG
QFGYKLFICG RDDYVGEDTI EVTNENVKRS RRLIIILVRD MGSFSCLGQS SEEQIAIYDA
LIREGIKIIL LELEKIQDYE KMPESIQFIK QKHGAICWSG DFKERPQSAK TRFWKNLRYQ
MPAQRRSPLS KHHLLTLDPV LDTKEKLQAE THLPLG
