Q95V55 · FOXO_DROME
- ProteinForkhead box protein O
- Genefoxo
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids613 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor involved in the regulation of the insulin signaling pathway. Consistently activates both the downstream target Thor\d4EBP and the feedback control target InR. Involved in negative regulation of the cell cycle, modulating cell growth and proliferation. In response to cellular stresses, such as nutrient deprivation or increased levels of reactive oxygen species, foxo is activated and inhibits growth through the action of target genes such as Thor. Foxo activated in the adult fat body can regulate lifespan in adults; an insulin peptide itself may function as one secondary messenger of insulin-regulated aging. Also regulates Lip4, homolog of human acid lipases, thereby acting as a key modulator of lipid metabolism by insulin signaling and integrates insulin responses to glucose and lipid homeostasis.
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 95-201 | Fork-head | ||||
Sequence: WGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRG |
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
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameForkhead box protein O
- Short namesdFOXO
- 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 accessionQ95V55
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Mutant foxo lacking Akt1 phosphorylation sites no longer responds to insulin inhibition, remains in the nucleus, and is constitutively active, inducing cell arrest.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 44 | Abolishes phosphorylation; when associated with A-190 and A-259. | ||||
Sequence: T → A | ||||||
Mutagenesis | 190 | Abolishes phosphorylation; when associated with A-44 and A-259. | ||||
Sequence: S → A | ||||||
Mutagenesis | 259 | Abolishes phosphorylation; when associated with A-44 and A-190. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000371436 | 1-613 | Forkhead box protein O | |||
Sequence: MMDGYAQEWPRLTHTDNGLAMDQLGGDLPLDVGFEPQTRARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSSRRNAWGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLEGQCLEVLNNEAQPIDEFNLENFPVGNLECNVEELLQQEMSYGGLLDINIPLATVNTNLVNSSSGPLSISNISNLSNISSNSGSSLSLNQLQAQLQQQQQQQQAQQQQQAQQQQQQHQQHQQQLLLNNNNNSSSSLELATQTATTNLNARVQYSQPSVVTSPPSWVH | ||||||
Modified residue | 44 | Phosphothreonine; by PKB/AKT1 | ||||
Sequence: T | ||||||
Modified residue | 75 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 190 | Phosphoserine; by PKB/AKT1 | ||||
Sequence: S | ||||||
Modified residue | 259 | Phosphoserine; by PKB/AKT1 | ||||
Sequence: S | ||||||
Modified residue | 262 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 268 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with melt.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q95V55 | HDAC4 Q8I9J6 | 3 | EBI-500849, EBI-4288282 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 39-90 | Disordered | ||||
Sequence: RARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSS | ||||||
Compositional bias | 59-90 | Polar residues | ||||
Sequence: ELDSTKASNQQLAPGDSQQAIQNANAAKKNSS | ||||||
Compositional bias | 182-198 | Basic and acidic residues | ||||
Sequence: KSVRRRAASMETSRYEK | ||||||
Region | 182-205 | Disordered | ||||
Sequence: KSVRRRAASMETSRYEKRRGRAKK | ||||||
Region | 217-269 | Disordered | ||||
Sequence: GLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSP | ||||||
Compositional bias | 219-233 | Polar residues | ||||
Sequence: NDATPSPSSSVSEGL | ||||||
Compositional bias | 252-267 | Polar residues | ||||
Sequence: DFRQRASSNASSCGRL | ||||||
Region | 317-360 | Disordered | ||||
Sequence: QGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASG | ||||||
Compositional bias | 339-360 | Polar residues | ||||
Sequence: HQQAQQQQQQQSPYALNGPASG |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q95V55-1
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.
- NameB
- SynonymsC
- Length613
- Mass (Da)67,413
- Last updated2001-12-01 v1
- ChecksumB472822ACA169BF9
Q95V55-2
- NameA
- Differences from canonical
- 146-243: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHS → SFAINALLSSDRFSFCLHRSIPPLAVIKDQRLLKNSLRWLRRNRRRLFHLIPETLFFADSALPANFSFFLRRLVVVRWFRGLADRWFGGSVARVFIIENSSSQSGDLAIEPVPKFYELSTNQSECKWQSGMAVDKTWIIGGDPVSATCRDSVSPISRSNGPMKYAYLIRDDSVSWGSNELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQVTINCDD
Q95V55-3
- NameD
- Differences from canonical
- 146-304: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGT → DLQILQFFYIQYISVFAKYIYLYVHICFSLVLVTELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQWRWLPIIARFPATRLIQCQFLRTPEPH
- 305-613: Missing
Q95V55-4
- NameE
- Differences from canonical
- 146-447: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLE → SFAINALLSSDRFSFCLHRSIPPLAVIKDQRLLKNSLRWLRRNRRRLFHLIPETLFFADSALPANFSFFLRRLVVVRWFRGLADRWFGGSVARVFIIENSSSQSGDLAIEPVPKFYELSTNQSECKWQSGMAVDKTWIIGGDPVSATCRDSVSPISRSNGPMKYAYLIRDDSVSWGSNELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQWRWLPIIARFPATRLIQCQFLRTPEPH
- 448-613: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4KGN1 | A0A0B4KGN1_DROME | foxo | 622 | ||
A0A126GUT4 | A0A126GUT4_DROME | foxo | 619 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 59-90 | Polar residues | ||||
Sequence: ELDSTKASNQQLAPGDSQQAIQNANAAKKNSS | ||||||
Alternative sequence | VSP_053041 | 146-243 | in isoform A | |||
Sequence: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHS → SFAINALLSSDRFSFCLHRSIPPLAVIKDQRLLKNSLRWLRRNRRRLFHLIPETLFFADSALPANFSFFLRRLVVVRWFRGLADRWFGGSVARVFIIENSSSQSGDLAIEPVPKFYELSTNQSECKWQSGMAVDKTWIIGGDPVSATCRDSVSPISRSNGPMKYAYLIRDDSVSWGSNELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQVTINCDD | ||||||
Alternative sequence | VSP_053040 | 146-304 | in isoform D | |||
Sequence: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGT → DLQILQFFYIQYISVFAKYIYLYVHICFSLVLVTELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQWRWLPIIARFPATRLIQCQFLRTPEPH | ||||||
Alternative sequence | VSP_053039 | 146-447 | in isoform E | |||
Sequence: NSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLE → SFAINALLSSDRFSFCLHRSIPPLAVIKDQRLLKNSLRWLRRNRRRLFHLIPETLFFADSALPANFSFFLRRLVVVRWFRGLADRWFGGSVARVFIIENSSSQSGDLAIEPVPKFYELSTNQSECKWQSGMAVDKTWIIGGDPVSATCRDSVSPISRSNGPMKYAYLIRDDSVSWGSNELHTSQSVAAQPLYEGPKRGHRQVILVDAQPGGQARQVCAPPCRFHGDVPVREAARQGQEAGGGTASGGRGGPQRCHALAQQQRQRGAGSLSRESAPQWRWLPIIARFPATRLIQCQFLRTPEPH | ||||||
Compositional bias | 182-198 | Basic and acidic residues | ||||
Sequence: KSVRRRAASMETSRYEK | ||||||
Compositional bias | 219-233 | Polar residues | ||||
Sequence: NDATPSPSSSVSEGL | ||||||
Compositional bias | 252-267 | Polar residues | ||||
Sequence: DFRQRASSNASSCGRL | ||||||
Alternative sequence | VSP_053042 | 305-613 | in isoform D | |||
Sequence: Missing | ||||||
Compositional bias | 339-360 | Polar residues | ||||
Sequence: HQQAQQQQQQQSPYALNGPASG | ||||||
Alternative sequence | VSP_053043 | 448-613 | in isoform E | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF426831 EMBL· GenBank· DDBJ | AAL28078.1 EMBL· GenBank· DDBJ | mRNA | ||
AF416728 EMBL· GenBank· DDBJ | AAL09043.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF55012.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAS65147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAS65148.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | ACL83512.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY058718 EMBL· GenBank· DDBJ | AAL13947.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY089542 EMBL· GenBank· DDBJ | AAL90280.1 EMBL· GenBank· DDBJ | mRNA |