| IED ID | IndEnz0002008123 |
| Enzyme Type ID | protease008123 |
| Protein Name |
Retinoic acid receptor RXR-alpha Nuclear receptor subfamily 2 group B member 1 Retinoid X receptor alpha |
| Gene Name | rxra nr2b1 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MSSAAMDTKHFLPLGGRTCADTLRCTTSWTAGYDFSSQVNSSSLSSSGLRGSMTAPLLHPSLGNSGLNNSLGSPTQLPSPLSSPINGMGPPFSVISPPLGPSMAIPSTPGLGYGTGSPQIHSPMNSVSSTEDIKPPPGINGILKVPMHPSGAMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDSKDCMIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKERNENEVESSNSANEDMPVEKILEAEHAVEPKTETYTEANMGLAPNSPSDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPLEVEALREKVYASLEAYCKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT |
| Enzyme Length | 488 |
| Uniprot Accession Number | P51128 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 342; /note=9-cis retinoic acid; /evidence=ECO:0000250|UniProtKB:P19793; BINDING 353; /note=9-cis retinoic acid; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P19793 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 158..233; /note=Nuclear receptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00407 |
| EC Number | |
| Enzyme 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. {ECO:0000250|UniProtKB:P19793}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Compositional bias (1); Cross-link (1); DNA binding (1); Domain (1); Metal binding (8); Region (6); Zinc finger (2) |
| Keywords | DNA-binding;Isopeptide bond;Metal-binding;Nucleus;Receptor;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. |
| Modified Residue | |
| Post Translational Modification | PTM: Sumoylated on Lys-134; which negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,469 |
| Kinetics | |
| Metal Binding | METAL 161; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P19793; METAL 164; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P19793; METAL 178; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P19793; METAL 181; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P19793; METAL 197; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P19793; METAL 203; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P19793; METAL 213; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P19793; METAL 216; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P19793 |
| Rhea ID | |
| Cross Reference Brenda |