Detail Information for IndEnz0002015278
IED ID IndEnz0002015278
Enzyme Type ID protease015278
Protein Name Interleukin-1 receptor type 1
IL-1R-1
IL-1RT-1
IL-1RT1
EC 3.2.2.6
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
Gene Name Il1r1 Il-1r1 Il1ra
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MENMKVLLGLICLMVPLLSLEIDVCTEYPNQIVLFLSVNEIDIRKCPLTPNKMHGDTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVLENDPGLCYSTQATFPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQYPVTRVIQFITIDENKRDRPVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQFYRYPFICVVKNTNIFESAHVQLIYPVPDFKNYLIGGFIILTATIVCCVCIYKVFKVDIVLWYRDSCSGFLPSKASDGKTYDAYILYPKTLGEGSFSDLDTFVFKLLPEVLEGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSWLGQSSEEQIAIYNALIQEGIKIVLLELEKIQDYEKMPDSIQFIKQKHGVICWSGDFQERPQSAKTRFWKNLRYQMPAQRRSPLSKHRLLTLDPVRDTKEKLPAATHLPLG
Enzyme Length 576
Uniprot Accession Number P13504
Absorption
Active Site ACT_SITE 473; /evidence=ECO:0000255|PROSITE-ProRule:PRU00204
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
DNA Binding
EC Number 3.2.2.6
Enzyme Function 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}.; FUNCTION: [Isoform 2]: Unable to mediate canonical IL-1 signaling. Cooperates with IL1RAP isoform 3 to mediate IL1B-induced neuronal activity including IL1B-potentiated NMDA-induced calcium influx mediated by Akt kinase activation. {ECO:0000269|PubMed:22778412}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (1); Chain (2); Disulfide bond (4); Domain (4); Glycosylation (7); Modified residue (2); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Alternative promoter usage;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Immunoglobulin domain;Inflammatory response;Membrane;NAD;Phosphoprotein;Receptor;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix
Interact With P22366
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}. Secreted {ECO:0000250}.
Modified Residue MOD_RES 499; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P14778; MOD_RES 556; /note=Phosphothreonine; by PKC; /evidence=ECO:0000269|PubMed:1828344
Post Translational Modification 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}.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2969618
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10198176; 10201952; 10435584; 10509653; 10595943; 10607711; 10721695; 10749768; 10763993; 10946764; 11015350; 11035056; 11122355; 11133507; 11238652; 11493610; 11673538; 11673547; 11756486; 11786971; 11791667; 11792633; 11796828; 11880380; 11890668; 11994477; 12010781; 12077269; 12093872; 12097396; 12122068; 12133972; 12135759; 12223557; 12414526; 12466851; 12504878; 12566416; 12614028; 12672065; 12697697; 12707352; 12759568; 12773775; 12927619; 12960098; 12975454; 1386414; 1387109; 1387148; 14620878; 14622131; 14635056; 14693705; 14966082; 14978111; 15044707; 15100310; 15161633; 15240711; 15277240; 15292196; 1532025; 1533388; 15353494; 15509550; 15664785; 15668736; 15678109; 15722603; 15797311; 15858027; 15893609; 15896328; 15939811; 15972657; 16029197; 16081822; 16126903; 16141072; 16179572; 16272281; 16272344; 16294221; 16301661; 16358337; 16365459; 16407889; 16413925; 16415102; 16426759; 16444258; 16477040; 16565512; 16569679; 16574667; 16602821; 16644674; 16645594; 16670325; 16688680; 1672292; 16818675; 16886064; 16941354; 16954498; 16983331; 17056530; 17122101; 17182684; 17192486; 17229673; 17283089; 17322383; 17339472; 17404295; 17500042; 17512577; 17549256; 17572686; 17575079; 17590392; 17617611; 17631139; 17675517; 17700577; 17728444; 17869478; 17881516; 17898219; 17908936; 17942936; 17976923; 17982084; 17992263; 18037570; 18096436; 18178625; 18178857; 18191113; 18211965; 18250441; 18256152; 18268142; 1828071; 18295350; 1832015; 18322211; 18329246; 1833184; 18434191; 18477692; 18480244; 18490717; 18495787; 18515164; 18535174; 18559949; 18562486; 18566426; 18617619; 18787019; 18805969; 18931327; 18941239; 18950689; 18996842; 19006696; 19074813; 19075023; 19079579; 19100239; 19158675; 19168746; 19196714; 19218193; 19229053; 19247983; 19289507; 19295146; 19342509; 19342666; 19347044; 19362022; 19389930; 19406986; 19414781; 19414802; 19429130; 19501000; 19501001; 19535637; 19541630; 19576795; 19587162; 19633315; 19652710; 19657352; 19724062; 19762681; 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31079916; 31141402; 31143178; 31167146; 31220272; 31228609; 31332247; 31393855; 31471109; 31499011; 31507610; 31524632; 31533918; 31738006; 31819009; 31836429; 31915130; 31935195; 32070376; 32269339; 32421904; 32433977; 32561755; 32573694; 32703941; 32719155; 32750316; 32758418; 32817286; 32973293; 32973802; 33020661; 33116136; 33619117; 33932339; 33952660; 33953267; 33958388; 34433045; 34603325; 7499265; 7578987; 7615010; 7683560; 7848516; 7877456; 7894170; 7916701; 7927486; 7953641; 7959748; 8007943; 8018912; 8020198; 8031998; 8034307; 8127400; 8276397; 8376789; 8432531; 8530075; 8581744; 8661203; 8662235; 8706893; 8751591; 8755642; 8770556; 8824815; 8875997; 8884266; 8953518; 9126479; 9166705; 9278338; 9292778; 9317135; 9399942; 9426216; 9449661; 9551933; 9555664; 9607815; 9651547; 9692874;
Motif
Gene Encoded By
Mass 66,698
Kinetics
Metal Binding
Rhea ID RHEA:16301; RHEA:16302
Cross Reference Brenda