Q6P3U7 · Q6P3U7_HUMAN
- ProteinRetinoic acid receptor RXR
- GeneRXRA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids516 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Molecular Function | nuclear receptor activity | |
Molecular Function | nuclear steroid receptor 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
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6P3U7
Subcellular Location
PTM/Processing
Proteomic databases
Interaction
Subunit
Homodimer. Heterodimer; with a rar molecule.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-47 | Disordered | ||||
Sequence: ATFATTRRAAASARRRRHRSRRLPAARARAGRAGGRRARRPLPAPPA | ||||||
Compositional bias | 10-36 | Basic residues | ||||
Sequence: AASARRRRHRSRRLPAARARAGRAGGR | ||||||
Region | 71-161 | Disordered | ||||
Sequence: SSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDI | ||||||
Compositional bias | 100-117 | Polar residues | ||||
Sequence: QLHSPISTLSSPINGMGP | ||||||
Compositional bias | 125-157 | Polar residues | ||||
Sequence: PMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSS | ||||||
Domain | 186-261 | Nuclear receptor | ||||
Sequence: KHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQE | ||||||
Compositional bias | 260-276 | Basic and acidic residues | ||||
Sequence: QEERQRGKDRNENEVES | ||||||
Region | 260-282 | Disordered | ||||
Sequence: QEERQRGKDRNENEVESTSSANE | ||||||
Domain | 281-512 | NR LBD | ||||
Sequence: NEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAP |
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 statusFragment
- Length516
- Mass (Da)56,672
- Last updated2004-07-05 v1
- ChecksumC18FB97552E55929
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A | ||||||
Compositional bias | 10-36 | Basic residues | ||||
Sequence: AASARRRRHRSRRLPAARARAGRAGGR | ||||||
Compositional bias | 100-117 | Polar residues | ||||
Sequence: QLHSPISTLSSPINGMGP | ||||||
Compositional bias | 125-157 | Polar residues | ||||
Sequence: PMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSS | ||||||
Compositional bias | 260-276 | Basic and acidic residues | ||||
Sequence: QEERQRGKDRNENEVES |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC063827 EMBL· GenBank· DDBJ | AAH63827.1 EMBL· GenBank· DDBJ | mRNA |