| IED ID | IndEnz0005000940 |
| Enzyme Type ID | lipase000940 |
| Protein Name |
Oxysterols receptor LXR-beta Liver X receptor beta Nuclear receptor subfamily 1 group H member 2 Retinoid X receptor-interacting protein No.15 Ubiquitously-expressed nuclear receptor |
| Gene Name | Nr1h2 Lxrb Rip15 Unr Unr2 |
| 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 | MSSPTSSLDTPVPGNGSPQPSTSATSPTIKEEGQETDPPPGSEGSSSAYIVVILEPEDEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNVLSCEGCKGFFRRSVVHGGAGRYACRGSGTCQMDAFMRRKCQLCRLRKCKEAGMREQCVLSEEQIRKKRIQKQQQQQPPPPSEPAASSSGRPAASPGTSEASSQGSGEGEGIQLTAAQELMIQQLVAAQLQCNKRSFSDQPKVTPWPLGADPQSRDARQQRFAHFTELAIISVQEIVDFAKQVPGFLQLGREDQIALLKASTIEIMLLETARRYNHETECITFLKDFTYSKDDFHRAGLQVEFINPIFEFSRAMRRLGLDDAEYALLIAINIFSADRPNVQEPSRVEALQQPYVEALLSYTRIKRPQDQLRFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE |
| Enzyme Length | 446 |
| Uniprot Accession Number | Q60644 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 75..152; /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:18055760, PubMed:19520913, PubMed:20427281). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4) (PubMed:18055760, PubMed:19520913, PubMed:20427281). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8 (PubMed:18055760, PubMed:19520913, PubMed:20427281). Interplays functionally with RORA for the regulation of genes involved in liver metabolism (PubMed:18055760, PubMed:19520913, PubMed:20427281, PubMed:24206663, PubMed:28846071). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (PubMed:28846071, PubMed:25806685). 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 (PubMed:25806685). 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 (PubMed:24206663). 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 (By similarity). {ECO:0000250|UniProtKB:P55055, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:20427281, ECO:0000269|PubMed:24206663, ECO:0000269|PubMed:25806685, ECO:0000269|PubMed:28846071}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (3); Cross-link (2); DNA binding (1); Domain (1); Region (4); Zinc finger (2) |
| Keywords | Activator;DNA-binding;Isopeptide bond;Metal-binding;Nucleus;Receptor;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger |
| Interact With | Q96EB6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. |
| Modified Residue | |
| Post Translational Modification | PTM: Sumoylated by SUMO2 at Lys-395 and Lys-433 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000250|UniProtKB:P55055}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10968783; 11090130; 11149950; 11238557; 11781314; 11792716; 11851872; 12193651; 12196343; 12368482; 12466851; 12520002; 12524534; 12610110; 12730332; 12819202; 12897148; 12970362; 14521951; 14610273; 14699103; 14703507; 14739254; 14993927; 15052659; 15146238; 15292368; 15479645; 15525595; 15561926; 15591022; 15601766; 15618518; 15674823; 15738425; 15752369; 15761042; 15831500; 15930522; 16007255; 16054068; 16141072; 16141411; 16325781; 16505352; 16511593; 16524875; 16644917; 16823488; 16825483; 16869726; 16876124; 16895745; 16971476; 16973760; 17107947; 17166844; 17218271; 17256725; 17341595; 17369526; 17439953; 17496333; 17563384; 17657314; 17726195; 17873880; 17936707; 17967808; 18077828; 18096827; 18160655; 18195045; 18238900; 18242221; 18276933; 18292813; 18450964; 18566121; 18614014; 18639878; 18768805; 18769020; 18772483; 18806227; 18820007; 18840761; 18949453; 18981139; 18981140; 18983830; 19032342; 19122149; 19136075; 19196952; 19218241; 19238156; 19325005; 19327357; 19342446; 19380774; 19395734; 19406833; 19436111; 19487338; 19556420; 19608643; 19646905; 19690071; 19714646; 19717840; 19721697; 19741146; 19787047; 19796621; 19878653; 19996385; 20044803; 20059953; 20079709; 20080977; 20110577; 20133709; 20159957; 20175894; 20375256; 20388921; 20412781; 20467332; 20566868; 20679224; 20739291; 20932939; 21103366; 21123945; 21134374; 21173252; 21187453; 21266776; 21267068; 21349840; 21398609; 21521718; 21525287; 21593381; 21609322; 21715627; 21784849; 22073227; 22156197; 22158963; 22323586; 22454476; 22481067; 22529354; 22547570; 22580900; 22610535; 22673513; 22723445; 22728933; 22826221; 22891211; 22931956; 22969086; 22984598; 22988430; 23021221; 23029557; 23063693; 23073827; 23077096; 23085633; 23099324; 23110859; 23185273; 23292650; 23348573; 23554947; 23675307; 23686490; 23706740; 23770640; 23788762; 23823481; 23867501; 23931754; 24074869; 24201575; 24333430; 24368671; 24438183; 24618263; 24671012; 24695360; 24803164; 24934178; 24947527; 24952961; 24994901; 25271621; 25277999; 25708389; 25724563; 25755249; 25825525; 25946408; 25962847; 26023184; 26075824; 26076474; 26324101; 26402841; 26440226; 26504234; 26602218; 26792941; 26814197; 26846362; 27053774; 27180240; 27251289; 27335465; 27382175; 27394190; 27520356; 28034754; 28041958; 28052875; 28082258; 28147278; 28231341; 28270440; 28324010; 28386023; 28420650; 28432199; 28732092; 28778663; 28971895; 29033131; 29336888; 29410501; 29431742; 29447944; 29507185; 29507213; 29688375; 29739800; 29915246; 30018108; 30127022; 30304667; 30455459; 30590048; 30602495; 31301160; 31371497; 31501273; 31783409; 31882567; 31980500; 32072744; 32097464; 32286429; 32297184; 33284790; 33373442; 33862368; 34122329; 34259574; 34297734; 9244354; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,720 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |