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FOXO_DROAN
ID   FOXO_DROAN              Reviewed;         600 AA.
AC   B3LYS5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Forkhead box protein O {ECO:0000250|UniProtKB:Q95V55};
GN   Name=foxo {ECO:0000250|UniProtKB:Q95V55}; ORFNames=GF16233;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1] {ECO:0000312|EMBL:EDV44041.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV44041.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Transcription factor involved in the regulation of the
CC       insulin signaling pathway. Consistently activates both the downstream
CC       target Thor\d4EBP and the feedback control target InR. Involved in
CC       negative regulation of the cell cycle, modulating cell growth and
CC       proliferation. In response to cellular stresses, such as nutrient
CC       deprivation or increased levels of reactive oxygen species, foxo is
CC       activated and inhibits growth through the action of target genes such
CC       as Thor. Foxo activated in the adult fat body can regulate lifespan in
CC       adults; an insulin peptide itself may function as one secondary
CC       messenger of insulin-regulated aging. Also regulates Lip4, homolog of
CC       human acid lipases, thereby acting as a key modulator of lipid
CC       metabolism by insulin signaling and integrates insulin responses to
CC       glucose and lipid homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with melt. {ECO:0000250|UniProtKB:Q95V55}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q95V55}. Nucleus
CC       {ECO:0000250|UniProtKB:Q95V55, ECO:0000255|PROSITE-ProRule:PRU00089}.
CC       Note=When phosphorylated, translocated from nucleus to cytoplasm.
CC       Dephosphorylation triggers nuclear translocation (By similarity).
CC       {ECO:0000250|UniProtKB:Q95V55}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDV44041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH902617; EDV44041.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001955480.2; XM_001955444.2.
DR   AlphaFoldDB; B3LYS5; -.
DR   SMR; B3LYS5; -.
DR   STRING; 7217.FBpp0119425; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   InParanoid; B3LYS5; -.
DR   ChiTaRS; foxo; fly.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   3: Inferred from homology;
KW   Activator; Cell cycle; Cytoplasm; Developmental protein; Differentiation;
KW   DNA-binding; Growth regulation; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..600
FT                   /note="Forkhead box protein O"
FT                   /id="PRO_0000396504"
FT   DNA_BIND        100..206
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          187..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphothreonine; by PKB/AKT1"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         195
FT                   /note="Phosphoserine; by PKB/AKT1"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         264
FT                   /note="Phosphoserine; by PKB/AKT1"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q95V55"
SQ   SEQUENCE   600 AA;  65699 MW;  013622ABE1CC0C31 CRC64;
     MMDGFAQDWP TLTHTDNGLA MDQLGVGVGV GDLPIDAGFE PQTRARSNTW PCPRPDNFVE
     PVDELDSTKA SNQQLAPGDS QQAIQNANAA KKNSSRRNAW GNLSYADLIT HAIGSATDKR
     LTLSQIYEWM VQNVPYFKDK GDSNSSAGWK NSIRHNLSLH NRFMRVQNEG TGKSSWWMLN
     PEAKPGKSVR RRAASMETSR YEKRRGRAKK RVEALRQAGV VGLNDATPSP SSSVSEGLDH
     FPESPLHSGG GFQLSPDFRQ RASSNASSCG RLSPIRAQDL EPDWGFPGVD YQNTTMTQAL
     EELTGSMADE LTLCTQQQQQ GFSAASGLPT QPPPPPYQPP QPQQQQQQGQ QPSPYALNGP
     TPGYNTLQPQ SQCLLHRSLN CSCLHNARDG LSPNSVTTTM SPAYPNSEPS SDSLNTYSNV
     VLDGPADTAA LLVQQQQQLA TNLEGQCLEV LNSEAQPIDE FNLENFPVGN LECNVEELLQ
     QEMSYGGLLD INIPLASVNT NLVNSGAPIS NITTSTGTSL NLNQLQAQLH QQQQQQQQLQ
     QQQQQQQHQQ HQQQQLLLNN NNNTSSSSLE LATQTPSTNL NARVQYSQPS VVTSPPSWVH
 
 
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