Detail Information for IndEnz0002015277
IED ID IndEnz0002015277
Enzyme Type ID protease015277
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 IL1R IL1RA IL1RT1
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG
Enzyme Length 569
Uniprot Accession Number P14778
Absorption
Active Site ACT_SITE 470; /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 (PubMed:10653850). {ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:10671496}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (27); Chain (2); Compositional bias (1); Disulfide bond (5); Domain (4); Glycosylation (6); Helix (7); Modified residue (1); Mutagenesis (2); Natural variant (2); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1)
Keywords 3D-structure;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Immunoglobulin domain;Inflammatory response;Membrane;NAD;Phosphoprotein;Receptor;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix
Interact With P09619; Q9Y4K3
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597}; Single-pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell membrane {ECO:0000305|PubMed:8142597}. Secreted {ECO:0000269|PubMed:8142597}.
Modified Residue MOD_RES 496; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:9821957
Post Translational Modification PTM: A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000269|PubMed:8142597}.; PTM: Rapidly phosphorylated on Tyr-496 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1. {ECO:0000269|PubMed:9821957}.
Signal Peptide SIGNAL 1..17
Structure 3D X-ray crystallography (5)
Cross Reference PDB 1G0Y; 1IRA; 1ITB; 4DEP; 4GAF;
Mapped Pubmed ID 10854325; 11027520; 11040178; 11083263; 11094434; 11127457; 11197691; 11220627; 11233912; 11380474; 11380940; 11390630; 11427627; 11506478; 11508575; 11527622; 11578018; 11665666; 11742191; 11752505; 11762793; 11790645; 11820460; 11838837; 11846196; 11849463; 11851889; 11956022; 11960013; 12028539; 12038885; 12082592; 12095061; 12133437; 12136897; 12138282; 12145738; 12164325; 12212456; 12240899; 12363051; 12412204; 12425801; 12472674; 12477576; 12538665; 12558814; 12595908; 12721283; 12729621; 12752101; 12804791; 12890860; 14557872; 14563376; 14625308; 14644395; 14680589; 14734209; 14735144; 14758530; 14872281; 15170937; 15188516; 15190266; 15300624; 15361128; 15375600; 15388348; 15472211; 15481335; 15653174; 15723707; 15789892; 15797878; 15866876; 15919456; 16100774; 16258158; 16286467; 16301860; 16323614; 16354686; 16564702; 16573560; 16911713; 16937503; 16938461; 17083033; 17141195; 17257312; 17324958; 17413037; 17477815; 17480058; 17507369; 17517439; 17584583; 17607501; 17622942; 17627763; 17688691; 17703412; 17889143; 17890055; 18052726; 1828071; 18321953; 18322311; 18438411; 18484169; 18576303; 18624935; 18632425; 18773331; 18810365; 18818748; 18996842; 19019335; 19064572; 19076825; 19117745; 19141860; 19142372; 19180518; 19211154; 19232518; 19258923; 19290009; 19332120; 19339270; 1940369; 1940799; 19408823; 19428986; 19431193; 19453261; 19470040; 19488045; 19527514; 19573080; 19594368; 19683555; 19684156; 19702713; 19716405; 19729601; 19738620; 19773279; 19773451; 19819943; 19822442; 19844779; 19860911; 19913121; 19940113; 19948975; 19950169; 19965648; 20066156; 20120526; 20140262; 20213229; 20237496; 20349753; 20353565; 20400062; 20452482; 20503287; 20523065; 20568250; 20602615; 20603050; 20628086; 20628624; 20673868; 20709104; 20799037; 20800603; 20802483; 20806065; 20811626; 20816195; 20818961; 20956022; 20959405; 21083841; 21086908; 21281963; 2139180; 21435443; 2147937; 21787753; 21858107; 21998454; 22031183; 22173128; 22262840; 22267087; 22285486; 22385245; 22417897; 22426547; 22435759; 22509941; 22515947; 22574108; 22594576; 23022958; 23253688; 23375040; 23431173; 23634226; 23722873; 24080160; 24315345; 24328419; 24356554; 24458711; 24818754; 24842757; 24976267; 24988285; 25014791; 25108563; 25240697; 25425640; 25453823; 25697140; 25749018; 26076982; 26098632; 26279140; 26590148; 26902320; 26975823; 27072893; 27327966; 27418552; 27466718; 27717726; 27980229; 28027994; 28164491; 28659487; 29103994; 29284683; 2946959; 29548280; 30093707; 30120937; 30256493; 30623603; 31021479; 31317192; 31476928; 32252823; 32573694; 32628975; 32707076; 32739831; 32778144; 33956941; 34156282; 34865658; 7512027; 7516408; 7687627; 7902377; 8102388; 8186324; 8327496; 8599092; 8837778; 8911996; 8946277; 9430229;
Motif
Gene Encoded By
Mass 65,402
Kinetics
Metal Binding
Rhea ID RHEA:16301; RHEA:16302
Cross Reference Brenda