UniProtKB - Q05343 (RXRA_RAT)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Retinoic acid receptor RXR-alpha
Gene
Rxra
Organism
Rattus norvegicus (Rat)
Status
Functioni
Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (By similarity). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.By similarity1 Publication
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 140 – 205 | Nuclear receptorPROSITE-ProRule annotationAdd BLAST | 66 | |
Zinc fingeri | 140 – 160 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 176 – 200 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
GO - Molecular functioni
- 9-cis retinoic acid receptor activity Source: RGD
- chromatin DNA binding Source: RGD
- DBD domain binding Source: RGD
- DNA binding Source: RGD
- DNA binding transcription factor activity Source: RGD
- double-stranded DNA binding Source: RGD
- enzyme binding Source: RGD
- LBD domain binding Source: RGD
- ligand-dependent nuclear receptor binding Source: RGD
- nuclear receptor activity Source: RGD
- peptide binding Source: RGD
- protein complex binding Source: RGD
- protein domain specific binding Source: RGD
- protein heterodimerization activity Source: RGD
- retinoic acid binding Source: RGD
- retinoic acid receptor binding Source: RGD
- retinoic acid-responsive element binding Source: RGD
- RNA polymerase II regulatory region sequence-specific DNA binding Source: RGD
- sequence-specific DNA binding Source: RGD
- steroid hormone receptor activity Source: RGD
- transcription factor binding Source: RGD
- vitamin D receptor binding Source: RGD
- zinc ion binding Source: RGD
GO - Biological processi
- aging Source: RGD
- axon regeneration Source: RGD
- camera-type eye development Source: RGD
- cardiac muscle cell proliferation Source: RGD
- cellular response to insulin stimulus Source: RGD
- embryo implantation Source: RGD
- female pregnancy Source: RGD
- heart development Source: RGD
- inflammatory response Source: RGD
- in utero embryonic development Source: RGD
- liver development Source: RGD
- maternal placenta development Source: RGD
- midgut development Source: RGD
- modulation by virus of host morphology or physiology Source: RGD
- negative regulation of cell proliferation Source: RGD
- negative regulation of transcription by RNA polymerase II Source: RGD
- peroxisome proliferator activated receptor signaling pathway Source: RGD
- placenta development Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of transcription, DNA-templated Source: RGD
- positive regulation of transcription by RNA polymerase II Source: RGD
- positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: RGD
- positive regulation of translational initiation by iron Source: RGD
- protein homotetramerization Source: RGD
- regulation of branching involved in prostate gland morphogenesis Source: RGD
- regulation of myelination Source: RGD
- regulation of transcription, DNA-templated Source: RGD
- regulation of transcription by RNA polymerase II Source: RGD
- response to ethanol Source: RGD
- response to glucocorticoid Source: RGD
- response to nutrient Source: RGD
- response to organic cyclic compound Source: RGD
- response to retinoic acid Source: RGD
- response to selenium ion Source: RGD
- response to vitamin A Source: RGD
- response to vitamin D Source: RGD
- retinoic acid receptor signaling pathway Source: RGD
- secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: RGD
- transcription, DNA-templated Source: UniProtKB-KW
- ventricular cardiac muscle cell differentiation Source: RGD
- ventricular cardiac muscle tissue morphogenesis Source: RGD
Keywordsi
Molecular function | DNA-binding, Receptor |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: Retinoic acid receptor RXR-alphaAlternative name(s): Nuclear receptor subfamily 2 group B member 1 Retinoid X receptor alpha |
Gene namesi | Name:Rxra Synonyms:Nr2b1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3610. Rxra. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000053568 | 1 – 467 | Retinoic acid receptor RXR-alphaAdd BLAST | 467 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 4 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 22 | PhosphoserineBy similarity | 1 | |
Modified residuei | 28 | PhosphoserineBy similarity | 1 | |
Modified residuei | 61 | Phosphoserine; by MAPK8 and MAPK9By similarity | 1 | |
Modified residuei | 75 | Phosphoserine; by MAPK8 and MAPK9By similarity | 1 | |
Modified residuei | 87 | Phosphothreonine; by MAPK8 and MAPK9By similarity | 1 | |
Cross-linki | 113 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity | ||
Modified residuei | 134 | PhosphoserineBy similarity | 1 | |
Modified residuei | 264 | PhosphoserineBy similarity | 1 | |
Modified residuei | 265 | Phosphoserine; by MAPK8 and MAPK9By similarity | 1 |
Post-translational modificationi
Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser-22 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265. Phosphorylated on Ser-28, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity).By similarity
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity).By similarity
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q05343. |
PRIDEi | Q05343. |
PTM databases
iPTMneti | Q05343. |
PhosphoSitePlusi | Q05343. |
Interactioni
Subunit structurei
Homodimer (By similarity). Heterodimer with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity (By similarity). Interacts with NCOA3 and NCOA6 coactivators. Interacts with FAM120B. Interacts with PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Heterodimerizes with PPARG (By similarity). Interacts with PRMT2 (By similarity). Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity. Interacts with ASXL1. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, MED1, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 and NCOA1 (By similarity). Interacts with VDR (By similarity).By similarity
GO - Molecular functioni
- DBD domain binding Source: RGD
- enzyme binding Source: RGD
- LBD domain binding Source: RGD
- ligand-dependent nuclear receptor binding Source: RGD
- protein complex binding Source: RGD
- protein domain specific binding Source: RGD
- protein heterodimerization activity Source: RGD
- retinoic acid receptor binding Source: RGD
- transcription factor binding Source: RGD
- vitamin D receptor binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000012892. |
Chemistry databases
BindingDBi | Q05343. |
Structurei
3D structure databases
ProteinModelPortali | Q05343. |
SMRi | Q05343. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 232 – 463 | NR LBDPROSITE-ProRule annotationAdd BLAST | 232 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 139 | ModulatingBy similarityAdd BLAST | 139 | |
Regioni | 206 – 229 | HingeBy similarityAdd BLAST | 24 |
Domaini
Composed of three domains: a modulating N-terminal or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or AF2 domain.
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 140 – 160 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 21 | |
Zinc fingeri | 176 – 200 | NR C4-typePROSITE-ProRule annotationAdd BLAST | 25 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG3575. Eukaryota. ENOG410XRZC. LUCA. |
HOGENOMi | HOG000260821. |
HOVERGENi | HBG005606. |
InParanoidi | Q05343. |
PhylomeDBi | Q05343. |
Family and domain databases
Gene3Di | 3.30.50.10. 1 hit. |
InterProi | View protein in InterPro IPR035500. NHR_like_dom_sf. IPR021780. Nuc_recep-AF1. IPR000536. Nucl_hrmn_rcpt_lig-bd. IPR001723. Nuclear_hrmn_rcpt. IPR000003. Retinoid-X_rcpt/HNF4. IPR001628. Znf_hrmn_rcpt. IPR013088. Znf_NHR/GATA. |
Pfami | View protein in Pfam PF00104. Hormone_recep. 1 hit. PF11825. Nuc_recep-AF1. 1 hit. PF00105. zf-C4. 1 hit. |
PRINTSi | PR00545. RETINOIDXR. PR00398. STRDHORMONER. PR00047. STROIDFINGER. |
SMARTi | View protein in SMART SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. |
SUPFAMi | SSF48508. SSF48508. 1 hit. |
PROSITEi | View protein in PROSITE PS51843. NR_LBD. 1 hit. PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q05343-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDTKHFLPLD FSTQVNSSSL SSPTGRGSMA APSLHPSLGP GLGSPLGSPG
60 70 80 90 100
QLHSPISTLS SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFETGSPQLN
110 120 130 140 150
SPMNPVSSSE DIKPPLGLNG VLKVPAHPSG NMSSFTKHIC AICGDRSSGK
160 170 180 190 200
HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK DCLIDKRQRN RCQYCRYQKC
210 220 230 240 250
LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI LEAELAVEPK
260 270 280 290 300
TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD
310 320 330 340 350
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI
360 370 380 390 400
FDRVLTELVS KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK
410 420 430 440 450
VYASLEAYCK HKYPEQPGRF AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT
460
PIDTFLMEML EAPHQTT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L06482 mRNA. Translation: AAA42093.1. |
PIRi | A47278. I67427. |
UniGenei | Rn.108206. |
Genome annotation databases
UCSCi | RGD:3610. rat. |
Similar proteinsi
Entry informationi
Entry namei | RXRA_RAT | |
Accessioni | Q05343Primary (citable) accession number: Q05343 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | February 1, 1994 | |
Last modified: | March 28, 2018 | |
This is version 152 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |