Rora
entrez
19883
canonical
uniprot
P51448
canonical
ensembl
ENSMUSG00000032238
resolver
ensp
ENSMUSP00000034766
resolver
ensp
ENSMUSP00000109254
resolver
ensp
ENSMUSP00000275388
resolver
ensp
ENSMUSP00000275391
resolver
genesymbol
Rora
resolver
genesymbol_syn
Nr1f1
resolver
genesymbol_syn
Rzra
resolver
uniprot
P70283
resolver
uniprot
P97741
resolver
uniprot
P97773
resolver
uniprot
Q3U1P4
resolver
uniprot
Q8C3F5
resolver
uniprot
Q923G1
resolver
uniprot_entry
Q3U1P4_MOUSE
resolver
uniprot_entry
Q8C3F5_MOUSE
resolver
uniprot_entry
RORA_MOUSE
resolver
uniprot_sec
P70283
resolver
uniprot_sec
P97741
resolver
uniprot_sec
P97773
resolver
uniprot_sec
Q923G1
resolver
amino_acid_sequence
MESAPAAPDPAASEPGSSGSEAAAGSRETPLTQDTGRKSEAPGAGRRQSYASSSRGISVTKKTHTSQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNATYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRMQQQQRDHQQQPGEAEPLTPTYNISANGLTELHDDLSTYMDGHTPEGSKADSAVSSFYLDIQPSPDQSGLDINGIKPEPICDYTPASGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHLETCQYLREELQQITWQTFLQEEIENYQNKQREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFIRMCRAFDSQNNTVYFDGKYASPDVFKSLGCEDFISFVFEFGKSLCSMHLTEDEIALFSAFVLMSADRSWLQEKVKIEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCGRHTEKLMAFKAIYPDIVRLHFPPLYKELFTSEFEPAMQIDG
uniprot
proteins
disease_involvement
DISEASE: Note=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. {ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:19014374, ECO:0000269|PubMed:9226375}.
uniprot
proteins
function
FUNCTION: 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, BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as 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 G6PC1 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. {ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:14687547, ECO:0000269|PubMed:15821743, ECO:0000269|PubMed:17666523, ECO:0000269|PubMed:18055760, ECO:0000269|PubMed:18164222, ECO:0000269|PubMed:18441015, ECO:0000269|PubMed:19014374, ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23172836, ECO:0000269|PubMed:23723244}.
uniprot
proteins
mass_dalton
58845
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by conventional PKCs in neurons inhibits transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in vitro. {ECO:0000250|UniProtKB:P35398}.; PTM: Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P35398}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Proteasomal degradation is required for efficient transcriptional activity and is prevented by HR. {ECO:0000250|UniProtKB:P35398}.; PTM: [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. {ECO:0000250|UniProtKB:P35398}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
11053433
uniprot
proteins
pubmed
14687547
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15821743
uniprot
proteins
pubmed
17476214
uniprot
proteins
pubmed
17666523
uniprot
proteins
pubmed
18055760
uniprot
proteins
pubmed
18164222
uniprot
proteins
pubmed
18441015
uniprot
proteins
pubmed
18535165
uniprot
proteins
pubmed
19014374
uniprot
proteins
pubmed
19039140
uniprot
proteins
pubmed
19324970
uniprot
proteins
pubmed
19381306
uniprot
proteins
pubmed
19965867
uniprot
proteins
pubmed
20159955
uniprot
proteins
pubmed
20300063
uniprot
proteins
pubmed
21499262
uniprot
proteins
pubmed
21628546
uniprot
proteins
pubmed
22170608
uniprot
proteins
pubmed
22753030
uniprot
proteins
pubmed
22789990
uniprot
proteins
pubmed
23172836
uniprot
proteins
pubmed
23723244
uniprot
proteins
pubmed
7935491
uniprot
proteins
pubmed
8602221
uniprot
proteins
pubmed
8750880
uniprot
proteins
pubmed
9226375
uniprot
proteins
sequence_length
523
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:22753030, ECO:0000269|PubMed:23723244}.
uniprot
proteins