Detail Information for IndEnz0005000626
IED ID IndEnz0005000626
Enzyme Type ID lipase000626
Protein Name Oxysterols receptor LXR-beta
Liver X receptor beta
Nuclear receptor NER
Nuclear receptor subfamily 1 group H member 2
Ubiquitously-expressed nuclear receptor
Gene Name NR1H2 LXRB NER UNR
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 MSSPTTSSLDTPLPGNGPPQPGAPSSSPTVKEEGPEPWPGGPDPDVPGTDEASSACSTDWVIPDPEEEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNVLSCEGCKGFFRRSVVRGGARRYACRGGGTCQMDAFMRRKCQQCRLRKCKEAGMREQCVLSEEQIRKKKIRKQQQESQSQSQSPVGPQGSSSSASGPGASPGGSEAGSQGSGEGEGVQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPGRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Enzyme Length 460
Uniprot Accession Number P55055
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 84..161; /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:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. 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 (By similarity). 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). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). {ECO:0000250|UniProtKB:Q60644, ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (7); Chain (1); Compositional bias (2); Cross-link (2); DNA binding (1); Domain (1); Helix (16); Mutagenesis (2); Natural variant (1); Region (4); Sequence conflict (9); Turn (5); Zinc finger (2)
Keywords 3D-structure;Activator;Alternative splicing;DNA-binding;Isopeptide bond;Metal-binding;Nucleus;Receptor;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger
Interact With Q92828; Q99750; O75376; P19793; P48443; Q07869-1; Q03181; P37231; P19793
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Modified Residue
Post Translational Modification PTM: Sumoylated by SUMO2 at Lys-409 and Lys-447 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000269|PubMed:20159957}.
Signal Peptide
Structure 3D X-ray crystallography (25)
Cross Reference PDB 1P8D; 1PQ6; 1PQ9; 1PQC; 1UPV; 1UPW; 3KFC; 3L0E; 4DK7; 4DK8; 4NQA; 4RAK; 5HJP; 5I4V; 5JY3; 5KYA; 5KYJ; 6JIO; 6K9G; 6K9H; 6K9M; 6S4N; 6S4T; 6S4U; 6S5K;
Mapped Pubmed ID 10235266; 10542397; 10858438; 11149950; 11287605; 11414710; 11500512; 11604492; 11790787; 11865025; 11875109; 12032151; 12150943; 12393874; 12454263; 12518032; 12612088; 12736258; 12957674; 14572640; 14643652; 14699103; 14703507; 14764426; 15147902; 15175151; 15539633; 15548517; 15896744; 16189514; 16298468; 16354658; 16482468; 16524875; 16567856; 16751179; 16871576; 16904112; 16973760; 17045963; 17108812; 17110595; 17135302; 17186944; 17218271; 17391100; 17396233; 17405904; 17626048; 17684114; 17724434; 17845217; 17900622; 18026184; 18081155; 18182682; 18221307; 18597895; 18636124; 18660489; 18782758; 18854425; 19060904; 19105208; 19242521; 19292929; 19303409; 19426978; 19481530; 19520913; 19710929; 19796621; 19837721; 19913121; 19932617; 19933273; 19948975; 20176747; 20219900; 20345102; 20427281; 20494359; 20628086; 20655109; 20711500; 20836841; 20855565; 20939869; 21030586; 21042792; 21187453; 21315073; 21331046; 21356276; 21507939; 21900206; 21937108; 21951066; 21988832; 22027013; 22029530; 22257474; 22367754; 22406115; 22510808; 22541735; 22610535; 22723445; 22766509; 22936343; 22990668; 23018104; 23223141; 23455924; 23686114; 23790976; 23838803; 23987069; 24100084; 24398515; 24561505; 24618263; 24832115; 24842676; 24863943; 25124554; 25435151; 25659329; 25962847; 25980575; 26009170; 26019035; 26120082; 26263968; 26434697; 26450852; 26602218; 26814197; 26936655; 26984517; 26990539; 27011007; 27342281; 27401066; 27404023; 27437943; 27489081; 27599745; 27846372; 27994765; 28082258; 28115302; 28167281; 28178657; 28676625; 28842423; 28869506; 28982861; 29181837; 29367626; 29778664; 30266104; 30338932; 30623435; 31104333; 31202993; 31432185; 31664073; 31799433; 31882567; 31931135; 32248003; 32711110; 32814418; 32961480; 32997975; 33862368; 34085098; 34153683; 8402897; 9053861; 9653119;
Motif
Gene Encoded By
Mass 50,974
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda