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P51448

- RORA_MOUSE

UniProt

P51448 - RORA_MOUSE

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Protein

Nuclear receptor ROR-alpha

Gene

Rora

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development, regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium-mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, ARNTL/BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4+ T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti-inflammatory role by inducing CHUK expression and inhibiting NF-kappa-B signaling.14 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi73 – 13866Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri73 – 9321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri109 – 13325NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. direct ligand regulated sequence-specific DNA binding transcription factor activity Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: InterPro
  5. oxysterol binding Source: UniProtKB
  6. sequence-specific DNA binding Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. steroid hormone receptor activity Source: InterPro
  9. transcription coactivator binding Source: UniProtKB
  10. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. cellular response to hypoxia Source: UniProtKB
  3. cellular response to sterol Source: UniProtKB
  4. cerebellar granule cell precursor proliferation Source: UniProtKB
  5. cerebellar Purkinje cell differentiation Source: MGI
  6. cGMP metabolic process Source: MGI
  7. circadian regulation of gene expression Source: UniProtKB
  8. intracellular receptor signaling pathway Source: UniProtKB
  9. muscle cell differentiation Source: UniProtKB
  10. negative regulation of fat cell differentiation Source: UniProtKB
  11. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  12. negative regulation of inflammatory response Source: UniProtKB
  13. nitric oxide biosynthetic process Source: MGI
  14. positive regulation of circadian rhythm Source: UniProtKB
  15. positive regulation of transcription, DNA-templated Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  17. positive regulation vascular endothelial growth factor production Source: UniProtKB
  18. regulation of cholesterol homeostasis Source: UniProtKB
  19. regulation of circadian rhythm Source: UniProtKB
  20. regulation of glucose metabolic process Source: UniProtKB
  21. regulation of macrophage activation Source: MGI
  22. regulation of smoothened signaling pathway Source: UniProtKB
  23. regulation of steroid metabolic process Source: UniProtKB
  24. regulation of transcription, DNA-templated Source: UniProtKB
  25. regulation of transcription involved in cell fate commitment Source: UniProtKB
  26. T-helper 17 cell differentiation Source: UniProtKB
  27. triglyceride homeostasis Source: UniProtKB
  28. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118837. Rora activates circadian gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_24972. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor ROR-alpha
Alternative name(s):
Nuclear receptor RZR-alpha
Nuclear receptor subfamily 1 group F member 1
RAR-related orphan receptor A
Retinoid-related orphan receptor-alpha
Gene namesi
Name:Rora
Synonyms:Nr1f1, Rzra
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:104661. Rora.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in Rora are the cause of the staggerer (SG) mutant phenotype which is characterized by disturbance of Purkinje cell development and immune system functioning. This phenotype exhibits lower body weight, reduced adiposity, decreased plasma cholesterol, triglyceride and apolipoprotein CIII levels, and is resistant to diet-induced obesity. Also has abnormal circadian rhythms.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Nuclear receptor ROR-alphaPRO_0000053513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-methyllysineBy similarity
Modified residuei183 – 1831Phosphothreonine; by MAPK1By similarity
Cross-linki240 – 240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Phosphorylation by conventional PKCs in neurons inhibits transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in vitro.By similarity
Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity. Desumoylated by SENP1.By similarity
Ubiquitinated, leading to its degradation by the proteasome. Proteasomal degradation is required for efficient transcriptional activity and is prevented by HR.By similarity
Isoform 1: monomethylated at Lys-38 by EZH2, this creates a degron recognized by a DCX (DDB1-DCAF1/VPRBP-CUL4A-RBX1) E3 ubiquitin ligase complex.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP51448.

PTM databases

PhosphoSiteiP51448.

Expressioni

Tissue specificityi

Expressed in cerebellum, heart, liver, lung, kidney, retina and brown and white adipose tissues. Expressed in the subset of mature Th17 cells.4 Publications

Developmental stagei

In cerebellum, expression begins at E12.5. In the developing retina, first expressed at E17 in the ganglion cell layer. At P3, expressed in the inner border of the neuroblasitic border (presumptive amacrine cells). By P6, levels increase in developing cones. Expression found in the presumptive bipolar cells by P9. During adipocyte differentiation, expression gradually increases.3 Publications

Inductioni

In T(H) cells, induced upon antigen receptor ligation in the presence of IL6 and TGB1 (via STAT3). Oscillates diurnally in central nervous system. In liver, Isoform 1 oscillates diurnally but not isoform 4.4 Publications

Gene expression databases

BgeeiP51448.
CleanExiMM_RORA.
ExpressionAtlasiP51448. baseline and differential.
GenevestigatoriP51448.

Interactioni

Subunit structurei

Monomer. Interacts (via the DNA-binding domain) with HIF1A; the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interacts with CEBPB; the interaction disrupts the interaction CEBPB:EP300. Interacts with the coactivators NCOA2, PPARGC1A (via LXXLL motif), EP300 and MED1. Interacts with the corepressor NCOR1. Interacts with MAGED1 and CTNNB1. Interacts with CRY1 and PER2. Interacts (via AF-2 motif) with PROX1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Atxn1P542543EBI-1169722,EBI-1169713
Maged1Q9QYH65EBI-1169722,EBI-1801274

Protein-protein interaction databases

BioGridi202956. 1 interaction.
DIPiDIP-35351N.
IntActiP51448. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP51448.
SMRiP51448. Positions 73-170, 271-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 271133HingeAdd
BLAST
Regioni272 – 523252Ligand-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi506 – 5116AF-2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 17575Gln-richAdd
BLAST

Domaini

The AF-2 (activation function-2) motif is required for recruiting coregulators containing LXXLL motifs.By similarity

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri73 – 9321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri109 – 13325NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG324222.
GeneTreeiENSGT00760000119049.
HOGENOMiHOG000010200.
HOVERGENiHBG106848.
InParanoidiP51448.
KOiK08532.
OMAiGHCLTGQ.
OrthoDBiEOG79PJNW.
PhylomeDBiP51448.
TreeFamiTF319910.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003079. ROR_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01293. RORNUCRECPTR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: P51448-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESAPAAPDP AASEPGSSGS EAAAGSRETP LTQDTGRKSE APGAGRRQSY
60 70 80 90 100
ASSSRGISVT KKTHTSQIEI IPCKICGDKS SGIHYGVITC EGCKGFFRRS
110 120 130 140 150
QQSNATYSCP RQKNCLIDRT SRNRCQHCRL QKCLAVGMSR DAVKFGRMSK
160 170 180 190 200
KQRDSLYAEV QKHRMQQQQR DHQQQPGEAE PLTPTYNISA NGLTELHDDL
210 220 230 240 250
STYMDGHTPE GSKADSAVSS FYLDIQPSPD QSGLDINGIK PEPICDYTPA
260 270 280 290 300
SGFFPYCSFT NGETSPTVSM AELEHLAQNI SKSHLETCQY LREELQQITW
310 320 330 340 350
QTFLQEEIEN YQNKQREVMW QLCAIKITEA IQYVVEFAKR IDGFMELCQN
360 370 380 390 400
DQIVLLKAGS LEVVFIRMCR AFDSQNNTVY FDGKYASPDV FKSLGCEDFI
410 420 430 440 450
SFVFEFGKSL CSMHLTEDEI ALFSAFVLMS ADRSWLQEKV KIEKLQQKIQ
460 470 480 490 500
LALQHVLQKN HREDGILTKL ICKVSTLRAL CGRHTEKLMA FKAIYPDIVR
510 520
LHFPPLYKEL FTSEFEPAMQ IDG
Length:523
Mass (Da):58,845
Last modified:October 1, 1996 - v1
Checksum:iA194E02E4D9D177E
GO
Isoform 2 (identifier: P51448-3)

Also known as: Alpha-2

Sequence is not available
Length:
Mass (Da):
Isoform 3 (identifier: P51448-4)

Also known as: Alpha-3

Sequence is not available
Length:
Mass (Da):
Isoform 4 (identifier: P51448-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha-4

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MESAPAAPDP...ISVTKKTHTS → MYFVIAAMKA

Show »
Length:467
Mass (Da):53,414
Checksum:i5621E275EC282A54
GO

Sequence cautioni

The sequence AAH03757.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA69930.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631H → R in CAA69930. (PubMed:7935491)Curated
Sequence conflicti180 – 1812EP → T in CAA69930. (PubMed:7935491)Curated
Sequence conflicti182 – 1821L → I in AAB46801. (PubMed:8750880)Curated
Sequence conflicti182 – 1821L → I in BAA22970. (PubMed:8750880)Curated
Sequence conflicti193 – 1942LT → SA in CAA69930. (PubMed:7935491)Curated
Sequence conflicti304 – 3041L → W in CAA69930. (PubMed:7935491)Curated
Sequence conflicti315 – 3151Missing in AAB46801. (PubMed:8750880)Curated
Sequence conflicti315 – 3151Missing in BAA22970. (PubMed:8750880)Curated
Sequence conflicti362 – 3621E → G in CAA69930. (PubMed:7935491)Curated
Sequence conflicti433 – 4331R → P in CAA69930. (PubMed:7935491)Curated
Sequence conflicti450 – 4512QL → HM in CAA69930. (PubMed:7935491)Curated
Sequence conflicti487 – 4871K → N in AAB46801. (PubMed:8750880)Curated
Sequence conflicti487 – 4871K → N in BAA22970. (PubMed:8750880)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti275 – 31440Missing in SG; disturbance of Purkinje cell and muscle development, lipid metabolism, circadian behavior and immune system functioning. 1 Publication
Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666MESAP…KTHTS → MYFVIAAMKA in isoform 4. 4 PublicationsVSP_003658Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53228 mRNA. Translation: AAC52513.1.
Y08640 mRNA. Translation: CAA69930.1. Different initiation.
Z82994 mRNA. Translation: CAB05396.1.
S82720 mRNA. Translation: AAB46801.2.
D45910 mRNA. Translation: BAA22970.1.
BC003757 mRNA. Translation: AAH03757.2. Different initiation.
CCDSiCCDS23314.1. [P51448-1]
CCDS72268.1. [P51448-2]
PIRiS68517.
RefSeqiNP_001276845.1. NM_001289916.1. [P51448-2]
NP_038674.1. NM_013646.2. [P51448-1]
UniGeneiMm.378450.
Mm.391890.
Mm.427266.
Mm.445802.
Mm.491288.

Genome annotation databases

EnsembliENSMUST00000034766; ENSMUSP00000034766; ENSMUSG00000032238. [P51448-1]
ENSMUST00000113624; ENSMUSP00000109254; ENSMUSG00000032238. [P51448-2]
GeneIDi19883.
KEGGimmu:19883.
UCSCiuc009qmx.1. mouse. [P51448-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53228 mRNA. Translation: AAC52513.1 .
Y08640 mRNA. Translation: CAA69930.1 . Different initiation.
Z82994 mRNA. Translation: CAB05396.1 .
S82720 mRNA. Translation: AAB46801.2 .
D45910 mRNA. Translation: BAA22970.1 .
BC003757 mRNA. Translation: AAH03757.2 . Different initiation.
CCDSi CCDS23314.1. [P51448-1 ]
CCDS72268.1. [P51448-2 ]
PIRi S68517.
RefSeqi NP_001276845.1. NM_001289916.1. [P51448-2 ]
NP_038674.1. NM_013646.2. [P51448-1 ]
UniGenei Mm.378450.
Mm.391890.
Mm.427266.
Mm.445802.
Mm.491288.

3D structure databases

ProteinModelPortali P51448.
SMRi P51448. Positions 73-170, 271-511.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202956. 1 interaction.
DIPi DIP-35351N.
IntActi P51448. 2 interactions.

PTM databases

PhosphoSitei P51448.

Proteomic databases

PRIDEi P51448.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034766 ; ENSMUSP00000034766 ; ENSMUSG00000032238 . [P51448-1 ]
ENSMUST00000113624 ; ENSMUSP00000109254 ; ENSMUSG00000032238 . [P51448-2 ]
GeneIDi 19883.
KEGGi mmu:19883.
UCSCi uc009qmx.1. mouse. [P51448-1 ]

Organism-specific databases

CTDi 6095.
MGIi MGI:104661. Rora.

Phylogenomic databases

eggNOGi NOG324222.
GeneTreei ENSGT00760000119049.
HOGENOMi HOG000010200.
HOVERGENi HBG106848.
InParanoidi P51448.
KOi K08532.
OMAi GHCLTGQ.
OrthoDBi EOG79PJNW.
PhylomeDBi P51448.
TreeFami TF319910.

Enzyme and pathway databases

Reactomei REACT_118837. Rora activates circadian gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_24972. Circadian Clock.

Miscellaneous databases

ChiTaRSi RORA. mouse.
NextBioi 297388.
PROi P51448.
SOURCEi Search...

Gene expression databases

Bgeei P51448.
CleanExi MM_RORA.
ExpressionAtlasi P51448. baseline and differential.
Genevestigatori P51448.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003079. ROR_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01293. RORNUCRECPTR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. "RZRs, a new family of retinoid-related orphan receptors that function as both monomers and homodimers."
    Carlberg C., Hooft van Huijsduijnen R., Staple J.K., Delamarter J.F., Becker-Andre M.
    Mol. Endocrinol. 8:757-770(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Strain: C57BL/6.
    Tissue: Skin.
  3. "The structural integrity of ROR alpha isoforms is mutated in staggerer mice: cerebellar coexpression of ROR alpha1 and ROR alpha4."
    Matysiak-Scholze U., Nehls M.C.
    Genomics 43:78-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT SG 275-HIS--LYS-314 DEL.
    Strain: C57BL/6.
    Tissue: Cerebellum.
  4. "An orphan nuclear receptor, mROR alpha, and its spatial expression in adult mouse brain."
    Matsui T., Sashihara S., Oh Y., Waxman S.G.
    Brain Res. Mol. Brain Res. 33:217-226(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Brain.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Strain: FVB/N.
    Tissue: Mammary gland.
  6. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 39-61, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  7. "Transcriptional regulation of apolipoprotein C-III gene expression by the orphan nuclear receptor RORalpha."
    Raspe E., Duez H., Gervois P., Fievet C., Fruchart J.C., Besnard S., Mariani J., Tedgui A., Staels B.
    J. Biol. Chem. 276:2865-2871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRIGLYCERIDE METABOLISM, DNA-BINDING, CHARACTERIZATION OF VARIANT SG PHENOTYPE.
  8. "RORalpha coordinates reciprocal signaling in cerebellar development through sonic hedgehog and calcium-dependent pathways."
    Gold D.A., Baek S.H., Schork N.J., Rose D.W., Larsen D.D., Sachs B.D., Rosenfeld M.G., Hamilton B.A.
    Neuron 40:1119-1131(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CEREBELLAR DEVELOPMENT, DEVELOPMENTAL STAGE, INTERACTION WITH CTNNB1, CHARACTERIZATION OF VARIANT SG PHENOTYPE.
  9. "The orphan nuclear receptor RORalpha regulates circadian transcription of the mammalian core-clock Bmal1."
    Akashi M., Takumi T.
    Nat. Struct. Mol. Biol. 12:441-448(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, CHARACTERIZATION OF VARIANT SG PHENOTYPE.
  10. "Transcriptional coactivator PGC-1alpha integrates the mammalian clock and energy metabolism."
    Liu C., Li S., Liu T., Borjigin J., Lin J.D.
    Nature 447:477-481(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPARGC1A.
  11. "Gene expression profiling reveals a regulatory role for ROR alpha and ROR gamma in phase I and phase II metabolism."
    Kang H.S., Angers M., Beak J.Y., Wu X., Gimble J.M., Wada T., Xie W., Collins J.B., Grissom S.F., Jetten A.M.
    Physiol. Genomics 31:281-294(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN METABOLISM REGULATION, CHARACTERIZATION OF VARIANT SG PHENOTYPE, TISSUE SPECIFICITY.
  12. "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, CHARACTERIZATION OF VARIANT SG PHENOTYPE, DNA-BINDING.
  13. "The emerging role of nuclear receptor RORalpha and its crosstalk with LXR in xeno- and endobiotic gene regulation."
    Wada T., Kang H.S., Jetten A.M., Xie W.
    Exp. Biol. Med. 233:1191-1201(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW OF FUNCTION IN METABOLISM REGULATION.
  14. "T helper 17 lineage differentiation is programmed by orphan nuclear receptors ROR alpha and ROR gamma."
    Yang X.O., Pappu B.P., Nurieva R., Akimzhanov A., Kang H.S., Chung Y., Ma L., Shah B., Panopoulos A.D., Schluns K.S., Watowich S.S., Tian Q., Jetten A.M., Dong C.
    Immunity 28:29-39(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T(H)17 CELLS DIFFERENTIATION, INDUCTION BY IL6 AND TGFB1, TISSUE SPECIFICITY.
  15. "The orphan nuclear receptor, RORalpha, regulates gene expression that controls lipid metabolism: staggerer (SG/SG) mice are resistant to diet-induced obesity."
    Lau P., Fitzsimmons R.L., Raichur S., Wang S.C., Lechtken A., Muscat G.E.
    J. Biol. Chem. 283:18411-18421(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIPID METABOLISM REGULATION, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT SG PHENOTYPE.
  16. "Absence of the SRC-2 coactivator results in a glycogenopathy resembling Von Gierke's disease."
    Chopra A.R., Louet J.F., Saha P., An J., Demayo F., Xu J., York B., Karpen S., Finegold M., Moore D., Chan L., Newgard C.B., O'Malley B.W.
    Science 322:1395-1399(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA2.
  17. "Retinoic acid receptor-related orphan receptor alpha regulates a subset of cone genes during mouse retinal development."
    Fujieda H., Bremner R., Mears A.J., Sasaki H.
    J. Neurochem. 108:91-101(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, CHARACTERIZATION OF VARIANT SG.
  18. "The orphan nuclear receptor RORalpha restrains adipocyte differentiation through a reduction of C/EBPbeta activity and perilipin gene expression."
    Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.
    Mol. Endocrinol. 23:759-771(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOGENESIS, INTERACTION WITH CEBPB, DEVELOPMENTAL STAGE.
  19. "Retinoid-related orphan receptors (RORs): critical roles in development, immunity, circadian rhythm, and cellular metabolism."
    Jetten A.M.
    Nucl. Recept. Signal. 7:3-35(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  20. "Interaction of MAGED1 with nuclear receptors affects circadian clock function."
    Wang X., Tang J., Xing L., Shi G., Ruan H., Gu X., Liu Z., Wu X., Gao X., Xu Y.
    EMBO J. 29:1389-1400(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGED1.
  21. "The mammalian clock component PERIOD2 coordinates circadian output by interaction with nuclear receptors."
    Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.
    Genes Dev. 24:345-357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PER2.
  22. "Modulation of retinoic acid receptor-related orphan receptor alpha and gamma activity by 7-oxygenated sterol ligands."
    Wang Y., Kumar N., Solt L.A., Richardson T.I., Helvering L.M., Crumbley C., Garcia-Ordonez R.D., Stayrook K.R., Zhang X., Novick S., Chalmers M.J., Griffin P.R., Burris T.P.
    J. Biol. Chem. 285:5013-5025(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLUCOSE METABOLISM REGULATION, IDENTIFICTION OF LIGANDS.
  23. Cited for: FUNCTION IN T(H)17 CELLS DIFFERENTIATION, INDUCTION BY IL6 AND TGFB1, INTERACTION WITH NCOR1 AND NCOA2, IDENTIFICATION OF LIGANDS.
  24. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
    Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
    Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1.
  25. "RORgamma directly regulates the circadian expression of clock genes and downstream targets in vivo."
    Takeda Y., Jothi R., Birault V., Jetten A.M.
    Nucleic Acids Res. 40:8519-8535(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DNA-BINDING, INDUCTION.
  26. "Action of RORs and their ligands in (patho)physiology."
    Solt L.A., Burris T.P.
    Trends Endocrinol. Metab. 23:619-627(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION AND LIGANDS.
  27. "Pivotal role of Rho-associated kinase 2 in generating the intrinsic circadian rhythm of vascular contractility."
    Saito T., Hirano M., Ide T., Ichiki T., Koibuchi N., Sunagawa K., Hirano K.
    Circulation 127:104-114(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  28. "Prospero-related homeobox 1 (Prox1) functions as a novel modulator of retinoic acid-related orphan receptors alpha- and gamma-mediated transactivation."
    Takeda Y., Jetten A.M.
    Nucleic Acids Res. 41:6992-7008(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PROX1.

Entry informationi

Entry nameiRORA_MOUSE
AccessioniPrimary (citable) accession number: P51448
Secondary accession number(s): P70283
, P97741, P97773, Q923G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3