P34021 · ECR_DROME
- ProteinEcdysone receptor
- GeneEcR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids878 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for ecdysone (PubMed:1913820, PubMed:30293839).
Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes (PubMed:1913820, PubMed:30293839).
Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes (PubMed:1913820, PubMed:30293839).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 264-336 | Nuclear receptor | ||||
Sequence: CLVCGDRASGYHYNALTCEGCKGFFRRSVTKSAVYCCKFGRACEMDMYMRRKCQECRLKKCLAVGMRPECVVP |
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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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEcdysone receptor
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP34021
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown blocks ecdysone-dependent fat body cell migration into the pupal head.
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000053524 | 1-878 | Ecdysone receptor | |||
Sequence: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISSGRDDLSPSSSLNGYSANESCDAKKSKKGPAPRVQEELCLVCGDRASGYHYNALTCEGCKGFFRRSVTKSAVYCCKFGRACEMDMYMRRKCQECRLKKCLAVGMRPECVVPENQCAMKRREKKAQKEKDKMTTSPSSQHGGNGSLASGGGQDFVKKEILDLMTCEPPQHATIPLLPDEILAKCQARNIPSLTYNQLAVIYKLIWYQDGYEQPSEEDLRRIMSQPDENESQTDVSFRHITEITILTVQLIVEFAKGLPAFTKIPQEDQITLLKACSSEVMMLRMARRYDHSSDSIFFANNRSYTRDSYKMAGMADNIEDLLHFCRQMFSMKVDNVEYALLTAIVIFSDRPGLEKAQLVEAIQSYYIDTLRIYILNRHCGDSMSLVFYAKLLSILTELRTLGNQNAEMCFSLKLKNRKLPKFLEEIWDVHAIPPSVQSHLQITQEENERLERAERMRASVGGAITAGIDCDSASTSAAAAAAQHQPQPQPQPQPSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQPQIQPQPQLLPVSAPVPASVTAPGSLSAVSTSSEYMGGSAAIGPITPATTSSITAAVTASSTTSAVPMGNGVGVGVGVGGNVSMYANAQTAMALMGVALHSHQEQLIGGVAVKSEHSTTA |
Proteomic databases
Expression
Tissue specificity
Isoform B1 predominates over isoform A in larval tissues, imaginal histoblast nests and midgut islands. Isoform A predominates over B1 in imaginal disks, and the larval prothoracic gland.
Developmental stage
In the salivary glands of mid instar larvae levels increase during puff stage 1 at 86-94 hours of development then remain relatively constant until the premetamorphic pulse of ecdysone in late larvae. Levels diminish dramatically from puff stage 7 onwards. Levels increase in the prepupal period during puff stage 13-14, the level remains stable until stage 21. A decrease in levels at puff stage 7 is also seen in the Malpighian tubules and less dramatically in the fat body and gut. In the wing disk the relatively low level remains unchanged.
Gene expression databases
Interaction
Subunit
Heterodimer of USP and ECR (PubMed:8247157).
Only the heterodimer is capable of high-affinity binding to ecdysone (PubMed:8247157).
Interacts with trr in an ecdysone-dependent manner (PubMed:14603321).
Upon ecdysone stimulation, interacts with Nup98 (PubMed:28366641).
Only the heterodimer is capable of high-affinity binding to ecdysone (PubMed:8247157).
Interacts with trr in an ecdysone-dependent manner (PubMed:14603321).
Upon ecdysone stimulation, interacts with Nup98 (PubMed:28366641).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-27 | Disordered | ||||
Sequence: MKRRWSNNGGFMRLPEESSSEVTSSSN | ||||||
Region | 1-263 | Modulating | ||||
Sequence: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISSGRDDLSPSSSLNGYSANESCDAKKSKKGPAPRVQEEL | ||||||
Compositional bias | 12-27 | Polar residues | ||||
Sequence: MRLPEESSSEVTSSSN | ||||||
Region | 209-254 | Disordered | ||||
Sequence: GLGMQHTPRSDSVNSISSGRDDLSPSSSLNGYSANESCDAKKSKKG | ||||||
Compositional bias | 215-245 | Polar residues | ||||
Sequence: TPRSDSVNSISSGRDDLSPSSSLNGYSANES | ||||||
Zinc finger | 264-284 | NR C4-type | ||||
Sequence: CLVCGDRASGYHYNALTCEGC | ||||||
Zinc finger | 300-324 | NR C4-type | ||||
Sequence: CKFGRACEMDMYMRRKCQECRLKKC | ||||||
Compositional bias | 344-358 | Basic and acidic residues | ||||
Sequence: RREKKAQKEKDKMTT | ||||||
Region | 344-374 | Disordered | ||||
Sequence: RREKKAQKEKDKMTTSPSSQHGGNGSLASGG | ||||||
Domain | 419-654 | NR LBD | ||||
Sequence: NQLAVIYKLIWYQDGYEQPSEEDLRRIMSQPDENESQTDVSFRHITEITILTVQLIVEFAKGLPAFTKIPQEDQITLLKACSSEVMMLRMARRYDHSSDSIFFANNRSYTRDSYKMAGMADNIEDLLHFCRQMFSMKVDNVEYALLTAIVIFSDRPGLEKAQLVEAIQSYYIDTLRIYILNRHCGDSMSLVFYAKLLSILTELRTLGNQNAEMCFSLKLKNRKLPKFLEEIWDVHA | ||||||
Region | 698-759 | Disordered | ||||
Sequence: TSAAAAAAQHQPQPQPQPQPSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQP | ||||||
Compositional bias | 717-759 | Polar residues | ||||
Sequence: PSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQP |
Sequence similarities
Belongs to the nuclear hormone receptor family. NR1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P34021-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameECR-B1
- SynonymsB
- Length878
- Mass (Da)93,853
- Last updated1994-02-01 v1
- ChecksumB48D610D722F014F
P34021-2
- NameECR-A
- SynonymsA, D
- Differences from canonical
- 1-226: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS → MLTTSGQQQSKQKLSTLPSHILLQQQLAASAGPSSSVSLSPSSSAALTLHVASANGGARETTSAAAVKDKLRPTPTAIKIEPMPDVISVGTVAGGSSVATVVAPAATTTSNKPNSTAAPSTSAAAANGHLVLVPNKRPRLDVTEDWMSTPSPGSVPSSAPPLSPSPGSQNHSYNMSNGYASPMSAGSYDPYSPTGKT
P34021-3
- NameECR-B2
- SynonymsC
- Differences from canonical
- 1-226: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS → MDTCGLVAELAHYIDAY
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_003661 | 1-226 | in isoform ECR-A | |||
Sequence: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS → MLTTSGQQQSKQKLSTLPSHILLQQQLAASAGPSSSVSLSPSSSAALTLHVASANGGARETTSAAAVKDKLRPTPTAIKIEPMPDVISVGTVAGGSSVATVVAPAATTTSNKPNSTAAPSTSAAAANGHLVLVPNKRPRLDVTEDWMSTPSPGSVPSSAPPLSPSPGSQNHSYNMSNGYASPMSAGSYDPYSPTGKT | ||||||
Alternative sequence | VSP_003662 | 1-226 | in isoform ECR-B2 | |||
Sequence: MKRRWSNNGGFMRLPEESSSEVTSSSNGLVLPSGVNMSPSSLDSHDYCDQDLWLCGNESGSFGGSNGHGLSQQQQSVITLAMHGCSSTLPAQTTIIPINGNANGNGGSTNGQYVPGATNLGALANGMLNGGFNGMQQQIQNGHGLINSTTPSTPTTPLHLQQNLGGAGGGGIGGMGILHHANGTPNGLIGVVGGGGGVGLGVGGGGVGGLGMQHTPRSDSVNSISS → MDTCGLVAELAHYIDAY | ||||||
Compositional bias | 12-27 | Polar residues | ||||
Sequence: MRLPEESSSEVTSSSN | ||||||
Compositional bias | 215-245 | Polar residues | ||||
Sequence: TPRSDSVNSISSGRDDLSPSSSLNGYSANES | ||||||
Compositional bias | 344-358 | Basic and acidic residues | ||||
Sequence: RREKKAQKEKDKMTT | ||||||
Compositional bias | 717-759 | Polar residues | ||||
Sequence: PSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQP | ||||||
Sequence conflict | 867-878 | in Ref. 4; AAL68274 | ||||
Sequence: GVAVKSEHSTTA → EWRLSRSTRRLHSRRRVSSTNITTTTSTSCWSRKRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74078 EMBL· GenBank· DDBJ | AAA28498.1 EMBL· GenBank· DDBJ | mRNA | ||
S63761 EMBL· GenBank· DDBJ | AAB27496.2 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57278.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57280.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68347.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY075461 EMBL· GenBank· DDBJ | AAL68274.1 EMBL· GenBank· DDBJ | mRNA | ||
AY058575 EMBL· GenBank· DDBJ | AAL13804.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BT012469 EMBL· GenBank· DDBJ | AAS93740.1 EMBL· GenBank· DDBJ | mRNA | ||
BT015234 EMBL· GenBank· DDBJ | AAT94463.1 EMBL· GenBank· DDBJ | mRNA |