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Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]

 IL1R1_RAT               Reviewed;         576 AA.
Q02955;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
18-JUL-2018, entry version 147.
RecName: Full=Interleukin-1 receptor type 1;
Short=IL-1R-1;
Short=IL-1RT-1;
Short=IL-1RT1;
AltName: Full=CD121 antigen-like family member A;
AltName: Full=Interleukin-1 receptor alpha;
Short=IL-1R-alpha;
AltName: Full=Interleukin-1 receptor type I;
AltName: Full=p80;
AltName: CD_antigen=CD121a;
Contains:
RecName: Full=Interleukin-1 receptor type 1, membrane form;
Short=mIL-1R1;
Short=mIL-1RI;
Contains:
RecName: Full=Interleukin-1 receptor type 1, soluble form;
Short=sIL-1R1;
Short=sIL-1RI;
Flags: Precursor;
Name=Il1r1; Synonyms=Il1ra;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ganglion;
PubMed=7684399; DOI=10.1016/0165-5728(93)90267-3;
Hart R.P., Liu C., Shadiack A.M., McCormack R.J., Jonakait G.M.;
"An mRNA homologous to interleukin-1 receptor type I is expressed in
cultured rat sympathetic ganglia.";
J. Neuroimmunol. 44:49-56(1993).
-!- FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to
interleukin-1 associates with the coreceptor IL1RAP to form the
high affinity interleukin-1 receptor complex which mediates
interleukin-1-dependent activation of NF-kappa-B, MAPK and other
pathways. Signaling involves the recruitment of adapter molecules
such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR
domains of the receptor/coreceptor subunits. Binds ligands with
comparable affinity and binding of antagonist IL1RN prevents
association with IL1RAP to form a signaling complex. Involved in
IL1B-mediated costimulation of IFNG production from T-helper 1
(Th1) cells (By similarity). {ECO:0000250|UniProtKB:P14778}.
-!- SUBUNIT: The interleukin-1 receptor complex is a heterodimer of
IL1R1 and IL1RAP. Interacts with PIK3R1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell membrane {ECO:0000305}. Secreted {ECO:0000250}.
-!- PTM: A soluble form (sIL1R1) is probably produced by proteolytic
cleavage at the cell surface (shedding). {ECO:0000250}.
-!- PTM: Rapidly phosphorylated on Tyr-499 in response to IL-1, which
creates a SH2 binding site for the PI 3-kinase regulatory subunit
PIK3R1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA16196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M95578; AAA16196.1; ALT_INIT; mRNA.
PIR; I56526; I56526.
UniGene; Rn.9758; -.
ProteinModelPortal; Q02955; -.
SMR; Q02955; -.
STRING; 10116.ENSRNOP00000019673; -.
PaxDb; Q02955; -.
PRIDE; Q02955; -.
UCSC; RGD:2892; rat.
RGD; 2892; Il1r1.
eggNOG; ENOG410IQBC; Eukaryota.
eggNOG; ENOG410Z3W1; LUCA.
HOVERGEN; HBG052103; -.
InParanoid; Q02955; -.
PhylomeDB; Q02955; -.
PRO; PR:Q02955; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0004909; F:interleukin-1, Type I, activating receptor activity; IEA:InterPro.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0010286; P:heat acclimation; IMP:RGD.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:RGD.
GO; GO:0030728; P:ovulation; IEP:RGD.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; IMP:RGD.
GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0071731; P:response to nitric oxide; IEP:RGD.
GO; GO:1990834; P:response to odorant; IEP:RGD.
GO; GO:0009314; P:response to radiation; IMP:RGD.
GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004076; IL-1_rcpt_I-typ.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF01582; TIR; 1.
PRINTS; PR01538; INTRLEUKN1R1.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS50104; TIR; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Inflammatory response; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 576 Interleukin-1 receptor type 1, membrane
form.
/FTId=PRO_0000015437.
CHAIN 20 ? Interleukin-1 receptor type 1, soluble
form.
/FTId=PRO_0000415346.
TOPO_DOM 20 338 Extracellular. {ECO:0000255}.
TRANSMEM 339 359 Helical. {ECO:0000255}.
TOPO_DOM 360 576 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 115 Ig-like C2-type 1.
DOMAIN 121 217 Ig-like C2-type 2.
DOMAIN 229 331 Ig-like C2-type 3.
DOMAIN 386 544 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOD_RES 499 499 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14778}.
MOD_RES 556 556 Phosphothreonine; by PKC.
{ECO:0000250|UniProtKB:P13504}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 46 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 145 199 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 251 315 {ECO:0000255|PROSITE-ProRule:PRU00114}.
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


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