P51128 · RXRA_XENLA
- ProteinRetinoic acid receptor RXR-alpha
- Generxra
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids488 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to 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 to regulate transcription. The high affinity ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the rar/rxr heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation.
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 158-233 | Nuclear receptor | ||||
Sequence: KHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDSKDCMIDKRQRNRCQYCRYQKCLAMGMKREAVQE | ||||||
Binding site | 161 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 178 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 197 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 203 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 213 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 216 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 342 | 9-cis-retinoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 342 | all-trans-retinoate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 353 | 9-cis-retinoate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 353 | all-trans-retinoate (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | nuclear receptor activity | |
Molecular Function | nuclear steroid receptor activity | |
Molecular Function | nuclear thyroid hormone receptor binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | retinoic acid-responsive element binding | |
Molecular Function | zinc ion binding | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | response to retinoic acid | |
Biological Process | retinoic acid receptor signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameRetinoic acid receptor RXR-alpha
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionP51128
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053569 | 1-488 | Retinoic acid receptor RXR-alpha | |||
Sequence: MSSAAMDTKHFLPLGGRTCADTLRCTTSWTAGYDFSSQVNSSSLSSSGLRGSMTAPLLHPSLGNSGLNNSLGSPTQLPSPLSSPINGMGPPFSVISPPLGPSMAIPSTPGLGYGTGSPQIHSPMNSVSSTEDIKPPPGINGILKVPMHPSGAMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDSKDCMIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKERNENEVESSNSANEDMPVEKILEAEHAVEPKTETYTEANMGLAPNSPSDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPLEVEALREKVYASLEAYCKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT | ||||||
Cross-link | 134 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K |
Post-translational modification
Sumoylated on Lys-134; which negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity).
Keywords
- PTM
Expression
Developmental stage
It is synthesized during oogenesis and persists during early cleavage, levels drop before gastrulation and remain low until the tailbud stage, and then increase in the later stages.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-160 | Modulating | ||||
Sequence: MSSAAMDTKHFLPLGGRTCADTLRCTTSWTAGYDFSSQVNSSSLSSSGLRGSMTAPLLHPSLGNSGLNNSLGSPTQLPSPLSSPINGMGPPFSVISPPLGPSMAIPSTPGLGYGTGSPQIHSPMNSVSSTEDIKPPPGINGILKVPMHPSGAMASFTKHI | ||||||
Zinc finger | 161-181 | NR C4-type | ||||
Sequence: CAICGDRSSGKHYGVYSCEGC | ||||||
Region | 186-191 | Nuclear localization signal | ||||
Sequence: KRTVRK | ||||||
Zinc finger | 197-216 | NR C4-type | ||||
Sequence: CRDSKDCMIDKRQRNRCQYC | ||||||
Region | 227-250 | Hinge | ||||
Sequence: KREAVQEERQRGKERNENEVESSN | ||||||
Compositional bias | 232-248 | Basic and acidic residues | ||||
Sequence: QEERQRGKERNENEVES | ||||||
Region | 232-256 | Disordered | ||||
Sequence: QEERQRGKERNENEVESSNSANEDM | ||||||
Domain | 253-484 | NR LBD | ||||
Sequence: NEDMPVEKILEAEHAVEPKTETYTEANMGLAPNSPSDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPLEVEALREKVYASLEAYCKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAP | ||||||
Region | 374-394 | Required for nuclear export | ||||
Sequence: RVLTELVSKMRDMQMDKTELG | ||||||
Region | 473-484 | AF-2 | ||||
Sequence: IDTFLMEMLEAP |
Domain
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Sequence similarities
Belongs to the nuclear hormone receptor family. NR2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length488
- Mass (Da)53,469
- Last updated1996-10-01 v1
- Checksum876FE43E901905D8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 232-248 | Basic and acidic residues | ||||
Sequence: QEERQRGKERNENEVES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L11446 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |