IED Industry Enzyme Database

Detail Information for IndEnz0005001152
IED ID IndEnz0005001152
Enzyme Type ID lipase001152
Protein Name Forkhead box protein O
dFOXO
Protein FKHR
Gene Name foxo Afx CG3143
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MMDGYAQEWPRLTHTDNGLAMDQLGGDLPLDVGFEPQTRARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSSRRNAWGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTGTMADELTLCNQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQQQQSPYALNGPASGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQLSASLEGQCLEVLNNEAQPIDEFNLENFPVGNLECNVEELLQQEMSYGGLLDINIPLATVNTNLVNSSSGPLSISNISNLSNISSNSGSSLSLNQLQAQLQQQQQQQQAQQQQQAQQQQQQHQQHQQQLLLNNNNNSSSSLELATQTATTNLNARVQYSQPSVVTSPPSWVH
Enzyme Length 613
Uniprot Accession Number Q95V55
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 95..201; /note=Fork-head; /evidence=ECO:0000255|PROSITE-ProRule:PRU00089
EC Number
Enzyme 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. {ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:12908874, ECO:0000269|PubMed:15175753, ECO:0000269|PubMed:16054033, ECO:0000269|PubMed:18234213}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (5); Chain (1); Compositional bias (5); DNA binding (1); Erroneous initiation (1); Modified residue (7); Mutagenesis (3); Region (4)
Keywords Activator;Alternative splicing;Cell cycle;Cytoplasm;DNA-binding;Developmental protein;Differentiation;Growth regulation;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation
Interact With Q8I9J6
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. {ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:15175753}.
Modified Residue MOD_RES 44; /note=Phosphothreonine; by PKB/AKT1; /evidence=ECO:0000269|PubMed:12893776; MOD_RES 75; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 190; /note=Phosphoserine; by PKB/AKT1; /evidence=ECO:0000269|PubMed:12893776; MOD_RES 259; /note=Phosphoserine; by PKB/AKT1; /evidence=ECO:0000269|PubMed:12893776; MOD_RES 262; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 263; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 268; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12844367; 14563554; 14597569; 14605208; 14745961; 14764878; 15192154; 15545659; 15565107; 15589139; 15691653; 15704171; 15710747; 15714554; 15734678; 15734679; 15734681; 15820683; 15843412; 15851659; 15935772; 15963974; 15998720; 16055649; 16086608; 16103212; 16163709; 16179433; 16230533; 16243018; 16254176; 16271526; 16332201; 16520939; 16564014; 16774996; 16783380; 16785324; 16890541; 16938867; 17041904; 17055976; 17090700; 17113379; 17139322; 17167488; 17183370; 17208179; 17215387; 17234883; 17289913; 17363962; 17369395; 17369827; 17462592; 17462750; 17465980; 17603113; 17686972; 17705839; 17765686; 17895391; 18068153; 18177722; 18221413; 18241326; 18245346; 18245854; 18246068; 18299344; 18344986; 18396138; 18460334; 18562277; 18632097; 18650956; 18665908; 18687152; 18690062; 18815370; 18827008; 19005568; 19018274; 19043547; 19128792; 19141596; 19211682; 19214224; 19237508; 19317915; 19378453; 19378454; 19390610; 19406101; 19470468; 19477978; 19494035; 19543366; 19553463; 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22706186; 22724070; 22751499; 22786647; 22843669; 22851689; 22858408; 22876196; 22911822; 22913798; 22935001; 22949833; 22956542; 22997544; 23063786; 23071443; 23072462; 23121290; 23129806; 23132240; 23190075; 23220476; 23228366; 23236133; 23240086; 23246004; 23251396; 23255216; 23307869; 23332152; 23355844; 23388617; 23499946; 23508807; 23519314; 23587490; 23593018; 23608455; 23624434; 23649823; 23732470; 23818862; 23836429; 23853709; 23874700; 23878722; 23885240; 23895933; 23934892; 23936253; 23977298; 24035390; 24038488; 24038661; 24062693; 24069139; 24086064; 24092876; 24133012; 24133450; 24137131; 24149429; 24191061; 24244197; 24255094; 24335260; 24348428; 24353210; 24357229; 24380076; 24430872; 24439372; 24508462; 24508822; 24509725; 24513978; 24558258; 24603715; 24609035; 24685228; 24690889; 24705759; 24746817; 24755363; 24768030; 24778227; 24819984; 24821805; 24832605; 24842780; 24847072; 24883306; 24902837; 24916379; 24949430; 24981286; 24983497; 24993942; 25007267; 25043021; 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33826881; 33914989; 33918672; 33946849; 33980491; 33990202; 33990225; 34012959; 34074704; 34078667; 34082046; 34101322; 34108216; 34146686; 34177563; 34267679; 34290618; 34349099; 34376687; 34381963; 34383711; 34385929; 34495320; 34545253; 34595369; 34944088;
Motif
Gene Encoded By
Mass 67,413
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda