| IED ID | IndEnz0005000508 |
| Enzyme Type ID | lipase000508 |
| Protein Name |
Oxysterols receptor LXR-alpha Liver X receptor alpha Nuclear receptor subfamily 1 group H member 3 |
| Gene Name | NR1H3 LXRA |
| 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 | MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPMAPDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE |
| Enzyme Length | 447 |
| Uniprot Accession Number | Q13133 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 95..170; /note=Nuclear receptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00407 |
| EC Number | |
| Enzyme Function | FUNCTION: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:19481530, PubMed:25661920). Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES (By similarity). LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides (By similarity). Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8 (PubMed:19481530). Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles. Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). {ECO:0000250|UniProtKB:Q9Z0Y9, ECO:0000269|PubMed:19481530, ECO:0000269|PubMed:25661920}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (3); Chain (1); DNA binding (1); Domain (1); Helix (11); Mutagenesis (2); Natural variant (1); Region (5); Sequence conflict (1); Turn (2); Zinc finger (2) |
| Keywords | 3D-structure;Activator;Alternative splicing;Cytoplasm;DNA-binding;Metal-binding;Nucleus;Receptor;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger |
| Interact With | O60869; O60341; Q99750; Q15788; O75376; Q07869; Q07869-1; Q03181; P37231; P19793; P28702; P48443; O43463; P42858; Q99750; O95817; G5E9A7; O95872; P02545; Q99750; P28702; P28702-3; P48443; Q7Z699 |
| Induction | INDUCTION: By 9-cis retinoic acid (9CRA). |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:25661920}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z0Y9}. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q9Z0Y9}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1UHL; 3IPQ; 3IPS; 3IPU; 5AVI; 5AVL; 5HJS; |
| Mapped Pubmed ID | 10235266; 10542397; 10858438; 11149950; 11287605; 11414710; 11500512; 11604492; 11790787; 11865025; 11875109; 12032151; 12040021; 12054659; 12117567; 12150943; 12161442; 12198243; 12454263; 12470296; 12518032; 12612088; 12932788; 12957674; 12970175; 14572640; 14699103; 14703507; 14764426; 15147902; 15175151; 15319359; 15353176; 15539633; 15548517; 15625283; 15896744; 16054077; 16106051; 16170053; 16249184; 16354658; 16482468; 16567856; 16751179; 16758300; 16871576; 16904112; 16920108; 16941683; 16973760; 17108812; 17110595; 17135302; 17186944; 17217555; 17218271; 17255360; 17272748; 17296605; 17391100; 17396233; 17405904; 17416342; 17452725; 17628006; 17644777; 17684114; 17724434; 17766241; 17845217; 17960176; 18007013; 18024509; 18182682; 18209740; 18250151; 18276933; 18327405; 18372238; 18511497; 18562803; 18636124; 18660489; 18669643; 18789440; 18854425; 19060910; 19105208; 19119143; 19164445; 19201410; 19211025; 19261092; 19292929; 19360318; 19366697; 19426978; 19520913; 19645823; 19697157; 19710929; 19796621; 19798078; 19837721; 19913121; 19933273; 20005944; 20037595; 20057170; 20080977; 20118482; 20139031; 20190811; 20219900; 20237496; 20364260; 20382159; 20410489; 20427281; 20494359; 20506155; 20628086; 20655109; 20682316; 20711500; 20837115; 20855565; 20868688; 20945144; 21030586; 21042792; 21125317; 21136146; 21187453; 21245992; 21266776; 21310851; 21315073; 21316679; 21349840; 21350215; 21356276; 21440016; 21516116; 21562465; 21625070; 21775116; 21889884; 21903943; 21937108; 21951066; 21988832; 22027013; 22257474; 22311022; 22367754; 22399489; 22503545; 22510808; 22541735; 22547570; 22569763; 22610535; 22634718; 22641099; 22707265; 22723445; 22749359; 22766509; 22916038; 22936343; 22939624; 22984430; 22990668; 23018104; 23041609; 23099324; 23163651; 23185273; 23393188; 23416078; 23451202; 23455924; 23496987; 23564066; 23680128; 23686114; 23732298; 23733886; 23790976; 23812424; 23838803; 23867395; 24036496; 24100084; 24118845; 24180251; 24265317; 24278306; 24289152; 24533572; 24618263; 24713062; 24832115; 24842676; 24886807; 24996838; 25005769; 25028566; 25035925; 25036637; 25073010; 25102981; 25187371; 25255963; 25264165; 25283515; 25332231; 25416956; 25437875; 25450400; 25600616; 25659329; 25729942; 25779847; 25867319; 25962847; 25980575; 26120082; 26160456; 26238323; 26379423; 26595172; 26602218; 26635040; 26669941; 26692490; 26756785; 26814197; 26964694; 26984517; 26991262; 27011007; 27016616; 27253448; 27343431; 27351826; 27401066; 27489081; 27490478; 27614433; 27736929; 27743553; 27832630; 28011707; 28082258; 28091828; 28178657; 28270440; 28361293; 28420650; 28508927; 28617824; 28676625; 28739689; 28842423; 28869506; 29230000; 29367626; 29420090; 29446839; 29577901; 29801879; 30393020; 30413149; 30623435; 30770793; 30964702; 31104333; 31243309; 31417573; 31432166; 31670283; 31931135; 32144382; 32208992; 32210962; 32413192; 32557804; 32594829; 32711110; 32745694; 32754282; 33031595; 33073697; 33141061; 33426085; 33742124; 34006637; 34085098; 34153683; 34512667; 8402897; 9653119; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,396 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |