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Q9Z0Y9 (NR1H3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxysterols receptor LXR-alpha
Alternative name(s):
Liver X receptor alpha
Nuclear receptor subfamily 1 group H member 3
Gene names
Name:Nr1h3
Synonyms:Lxra
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear receptor. Interaction with 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. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism. Ref.4 Ref.5 Ref.6

Subunit structure

Heterodimer of LXRA and RXR.

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Inferred from direct assay PubMed 14739254. Source: MGI

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 21187453. Source: BHF-UCL

cholesterol homeostasis

Inferred from genetic interaction PubMed 17657314. Source: BHF-UCL

fatty acid biosynthetic process

Traceable author statement PubMed 11090130. Source: BHF-UCL

intracellular receptor signaling pathway

Inferred from direct assay PubMed 14739254. Source: GOC

lipid homeostasis

Inferred from mutant phenotype PubMed 18806227. Source: BHF-UCL

negative regulation of cholesterol storage

Inferred from genetic interaction PubMed 17657314. Source: BHF-UCL

negative regulation of inflammatory response

Inferred from direct assay PubMed 21187453. Source: BHF-UCL

negative regulation of lipid transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of macrophage activation

Inferred from direct assay PubMed 21187453. Source: BHF-UCL

negative regulation of pancreatic juice secretion

Inferred from mutant phenotype PubMed 18806227. Source: BHF-UCL

negative regulation of pinocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteolysis

Inferred from mutant phenotype PubMed 18806227. Source: BHF-UCL

negative regulation of secretion of lysosomal enzymes

Inferred from mutant phenotype PubMed 18806227. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21187453. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 12815040. Source: MGI

positive regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol efflux

Inferred from direct assay PubMed 16825483. Source: BHF-UCL

positive regulation of cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipoprotein lipase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of toll-like receptor 4 signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16141411PubMed 16825483PubMed 17107947. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 11090130. Source: BHF-UCL

positive regulation of triglyceride biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of cholesterol homeostasis

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14739254. Source: MGI

response to progesterone

Inferred from electronic annotation. Source: Ensembl

sterol homeostasis

Inferred from mutant phenotype PubMed 16325781. Source: BHF-UCL

triglyceride homeostasis

Inferred from mutant phenotype PubMed 16325781. Source: BHF-UCL

   Cellular_componentnuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 14739254. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 14739254PubMed 15319426. Source: MGI

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 14739254. Source: MGI

protein binding

Inferred from physical interaction PubMed 17936707. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 14739254. Source: MGI

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

sterol response element binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT1Q96EB62EBI-5276764,EBI-1802965From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Oxysterols receptor LXR-alpha
PRO_0000053536

Regions

DNA binding93 – 16876Nuclear receptor
Zinc finger96 – 11621NR C4-type
Zinc finger132 – 15625NR C4-type
Region213 – 432220Ligand-binding Potential

Experimental info

Sequence conflict3991P → R in CAB51952. Ref.1
Sequence conflict3991P → R in CAB51923. Ref.1

Secondary structure

............................ 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Z0Y9 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 1A426DF38D935731

FASTA44550,418
        10         20         30         40         50         60 
MSLWLEASMP DVSPDSATEL WKTEPQDAGD QGGNTCILRE EARMPQSTGV ALGIGLESAE 

        70         80         90        100        110        120 
PTALLPRAET LPEPTELRPQ KRKKGPAPKM LGNELCSVCG DKASGFHYNV LSCEGCKGFF 

       130        140        150        160        170        180 
RRSVIKGARY VCHSGGHCPM DTYMRRKCQE CRLRKCRQAG MREECVLSEE QIRLKKLKRQ 

       190        200        210        220        230        240 
EEEQAQATSV SPRVSSPPQV LPQLSPEQLG MIEKLVAAQQ QCNRRSFSDR LRVTPWPIAP 

       250        260        270        280        290        300 
DPQSREARQQ RFAHFTELAI VSVQEIVDFA KQLPGFLQLS REDQIALLKT SAIEVMLLET 

       310        320        330        340        350        360 
SRRYNPGSES ITFLKDFSYN REDFAKAGLQ VEFINPIFEF SRAMNELQLN DAEFALLIAI 

       370        380        390        400        410        420 
SIFSADRPNV QDQLQVERLQ HTYVEALHAY VSINHPHDPL MFPRMLMKLV SLRTLSSVHS 

       430        440 
EQVFALRLQD KKLPPLLSEI WDVHE 

« Hide

References

« Hide 'large scale' references
[1]"Structural characterisation of the mouse nuclear oxysterol receptor genes LXRalpha and LXRbeta."
Alberti S., Steffensen K.R., Gustafsson J.-A.
Gene 243:93-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
Tissue: Liver.
[2]"LXRalpha functions as a cAMP-responsive transcriptional regulator of gene expression."
Tamura K., Chen Y.E., Horiuchi M., Chen Q., Daviet L., Yang Z., Lopez-Ilasaca M., Mu H., Pratt R.E., Dzau V.J.
Proc. Natl. Acad. Sci. U.S.A. 97:8513-8518(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Identification of oxysterol 7alpha-hydroxylase (Cyp7b1) as a novel retinoid-related orphan receptor alpha (RORalpha) (NR1F1) target gene and a functional cross-talk between RORalpha and liver X receptor (NR1H3)."
Wada T., Kang H.S., Angers M., Gong H., Bhatia S., Khadem S., Ren S., Ellis E., Strom S.C., Jetten A.M., Xie W.
Mol. Pharmacol. 73:891-899(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN METABOLISM REGULATION.
[5]"LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor."
Zelcer N., Hong C., Boyadjian R., Tontonoz P.
Science 325:100-104(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2."
Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V., Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.
J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132599, AJ132600 Genomic DNA. Translation: CAB51952.1.
AJ132601 mRNA. Translation: CAB51923.1.
AF085745 mRNA. Translation: AAD16050.1.
AL691450 Genomic DNA. No translation available.
CCDSCCDS16426.1.
RefSeqNP_001171201.1. NM_001177730.1.
NP_038867.2. NM_013839.4.
XP_006499229.1. XM_006499166.1.
XP_006499230.1. XM_006499167.1.
XP_006499231.1. XM_006499168.1.
UniGeneMm.22690.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ACLX-ray2.80B/D/F/H203-445[»]
3FALX-ray2.36B/D200-445[»]
3FC6X-ray2.06B/D200-445[»]
ProteinModelPortalQ9Z0Y9.
SMRQ9Z0Y9. Positions 83-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204449. 7 interactions.
IntActQ9Z0Y9. 2 interactions.

Chemistry

ChEMBLCHEMBL2189152.

PTM databases

PhosphoSiteQ9Z0Y9.

Proteomic databases

PRIDEQ9Z0Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002177; ENSMUSP00000002177; ENSMUSG00000002108.
ENSMUST00000111354; ENSMUSP00000106986; ENSMUSG00000002108.
ENSMUST00000111356; ENSMUSP00000106988; ENSMUSG00000002108.
GeneID22259.
KEGGmmu:22259.
UCSCuc008kvc.2. mouse.

Organism-specific databases

CTD10062.
MGIMGI:1352462. Nr1h3.

Phylogenomic databases

eggNOGNOG285805.
GeneTreeENSGT00720000108423.
HOGENOMHOG000220845.
HOVERGENHBG108655.
InParanoidQ9Z0Y9.
KOK08536.
OMACILREEA.
OrthoDBEOG7DC25S.
TreeFamTF352167.

Gene expression databases

ArrayExpressQ9Z0Y9.
BgeeQ9Z0Y9.
CleanExMM_NR1H3.
GenevestigatorQ9Z0Y9.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR023257. Liver_X_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR02034. LIVERXRECPTR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Z0Y9.
NextBio302349.
PROQ9Z0Y9.
SOURCESearch...

Entry information

Entry nameNR1H3_MOUSE
AccessionPrimary (citable) accession number: Q9Z0Y9
Secondary accession number(s): Q9QUH7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot