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 |