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Q9WVH4

- FOXO3_MOUSE

UniProt

Q9WVH4 - FOXO3_MOUSE

Protein

Forkhead box protein O3

Gene

Foxo3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Transcriptional activator which triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. Recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3'. Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi156 – 25095Fork-headPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin DNA binding Source: UniProtKB
    2. core promoter binding Source: UniProtKB
    3. DNA binding Source: MGI
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding Source: MGI
    6. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. antral ovarian follicle growth Source: MGI
    2. cellular response to oxidative stress Source: UniProtKB
    3. DNA damage response, signal transduction by p53 class mediator Source: MGI
    4. extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
    5. glucose homeostasis Source: MGI
    6. initiation of primordial ovarian follicle growth Source: MGI
    7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. oocyte maturation Source: MGI
    9. ovulation from ovarian follicle Source: MGI
    10. positive regulation of erythrocyte differentiation Source: Ensembl
    11. positive regulation of neuron apoptotic process Source: Ensembl
    12. positive regulation of transcription, DNA-templated Source: MGI
    13. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    14. regulation of transcription, DNA-templated Source: MGI
    15. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. regulation of translation Source: UniProtKB
    17. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_218211. AKT phosphorylates targets in the nucleus.
    REACT_220645. Signaling by NODAL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Forkhead box protein O3
    Gene namesi
    Name:Foxo3
    Synonyms:Fkhr2, Foxo3a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1890081. Foxo3.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Nucleus PROSITE-ProRule annotation
    Note: Translocates to the nucleus upon oxidative stress and in the absence of survival factors.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB-SubCell
    3. membrane Source: MGI
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 672672Forkhead box protein O3PRO_0000415334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphothreonine; by PKB/AKT1By similarity
    Modified residuei46 – 461N6-methyllysineBy similarity
    Modified residuei148 – 1481N6-methyllysineBy similarity
    Modified residuei178 – 1781Phosphothreonine; by AMPKBy similarity
    Modified residuei208 – 2081Phosphoserine; by STK4/MST1By similarity
    Modified residuei214 – 2141Phosphoserine; by MAPKAPK5By similarity
    Modified residuei229 – 2291N6-methyllysineBy similarity
    Modified residuei241 – 2411N6-acetyllysine2 Publications
    Modified residuei252 – 2521Phosphoserine; by PKB/AKT1 and MAPKAPK5By similarity
    Modified residuei261 – 2611N6-methyllysineBy similarity
    Modified residuei270 – 2701N6-methyllysineBy similarity
    Modified residuei279 – 2791PhosphoserineBy similarity
    Modified residuei283 – 2831PhosphoserineBy similarity
    Modified residuei289 – 2891N6-methyllysineBy similarity
    Modified residuei314 – 3141Phosphoserine; by SGK1By similarity
    Modified residuei398 – 3981Phosphoserine; by AMPKBy similarity
    Modified residuei412 – 4121Phosphoserine; by AMPKBy similarity
    Modified residuei418 – 4181N6-methyllysineBy similarity
    Modified residuei420 – 4201PhosphoserineBy similarity
    Modified residuei550 – 5501Phosphoserine; by MAPKAPK5By similarity
    Modified residuei554 – 5541Phosphoserine; by AMPK and MAPKAPK5By similarity
    Modified residuei587 – 5871Phosphoserine; by AMPKBy similarity
    Modified residuei625 – 6251Phosphoserine; by AMPKBy similarity

    Post-translational modificationi

    Deacetylation by SIRT1 or SIRT2 stimulates interaction of FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3 ubiquitination and proteasomal degradation By similarity. Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional activity in response to oxidative stress.By similarity
    In the presence of survival factors such as IGF-1, phosphorylated on Thr-32 and Ser-252 by AKT1/PKB. This phosphorylated form then interacts with 14-3-3 proteins and is retained in the cytoplasm. Survival factor withdrawal induces dephosphorylation and promotes translocation to the nucleus where the dephosphorylated protein induces transcription of target genes and triggers apoptosis. Although AKT1/PKB doesn't appear to phosphorylate Ser-314 directly, it may activate other kinases that trigger phosphorylation at this residue. Phosphorylated by STK4/MST1 on Ser-208 upon oxidative stress, which leads to dissociation from YWHAB/14-3-3-beta and nuclear translocation. Phosphorylated by PIM1. Phosphorylation by AMPK leads to the activation of transcriptional activity without affecting subcellular localization. Phosphorylation by MAPKAPK5 promotes nuclear localization and DNA-binding, leading to induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation By similarity.By similarity
    Heavyly methylated by SET9 which decreases stability, while moderately increasing transcriptional activity. The main methylation site is Lys-270. Methylation doesn't affect subcellular location By similarity.By similarity
    Polyubiquitinated. Ubiquitinated by a SCF complex containing SKP2, leading to proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9WVH4.

    PTM databases

    PhosphoSiteiQ9WVH4.

    Expressioni

    Tissue specificityi

    Expressed in white and brown adipose tissues (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9WVH4.
    BgeeiQ9WVH4.
    GenevestigatoriQ9WVH4.

    Interactioni

    Subunit structurei

    Interacts with YWHAB/14-3-3-beta and YWHAZ/14-3-3-zeta, which are required for cytosolic sequestration. Upon oxidative stress, interacts with STK4/MST1, which disrupts interaction with YWHAB/14-3-3-beta and leads to nuclear translocation. Interacts with PIM1. Interacts with DDIT3/CHOP. Interacts (deacetylated form) with SKP2 By similarity. Interacts with SIRT2; the interaction occurs independently of SIRT2 deacetylase activity.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FcorP0DJI62EBI-6127038,EBI-6126630
    SETD7Q8WTS65EBI-6127038,EBI-1268586From a different organism.

    Protein-protein interaction databases

    IntActiQ9WVH4. 2 interactions.
    STRINGi10090.ENSMUSP00000101141.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WVH4.
    SMRiQ9WVH4. Positions 157-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi241 – 25818Nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi546 – 59550Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5025.
    GeneTreeiENSGT00390000000589.
    HOGENOMiHOG000251635.
    HOVERGENiHBG078744.
    InParanoidiQ9WVH4.
    KOiK09408.
    OMAiNLPVMGH.
    OrthoDBiEOG7R2BJD.
    PhylomeDBiQ9WVH4.
    TreeFamiTF315583.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00250. Fork_head. 1 hit.
    [Graphical view]
    PRINTSiPR00053. FORKHEAD.
    SMARTiSM00339. FH. 1 hit.
    [Graphical view]
    PROSITEiPS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WVH4-1 [UniParc]FASTAAdd to Basket

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    MAEAPASPVP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE    50
    TAADSMIPEE DDDEDDEDGG GRASSAMVIG GGVSSTLGSG LLLEDSAMLL 100
    APGGQDLGSG PASAAGALSG GTPTQLQPQQ PLPQPQPGAA GGSGQPRKCS 150
    SRRNAWGNLS YADLITRAIE SSPDKRLTLS QIYEWMVRCV PYFKDKGDSN 200
    SSAGWKNSIR HNLSLHSRFM RVQNEGTGKS SWWIINPDGG KSGKAPRRRA 250
    VSMDNSNKYT KSRGRAAKKK AALQAAPESA DDSPSQLSKW PGSPTSRSSD 300
    ELDAWTDFRS RTNSNASTVS GRLSPILAST ELDDVQDDDG PLSPMLYSSS 350
    ASLSPSVSKP CTVELPRLTD MAGTMNLNDG LAENLMDDLL DNIALPPSQP 400
    SPPGGLMQRG SSFPYTAKSS GLGSPTGSFN STVFGPSSLN SLRQSPMQTI 450
    QENRPATFSS VSHYGNQTLQ DLLASDSLSH SDVMMTQSDP LMSQASTAVS 500
    AQNARRNVML RNDPMMSFAA QPTQGSLVNQ NLLHHQHQTQ GALGGSRALS 550
    NSVSNMGLSD SSSLGSAKHQ QQSPASQSMQ TLSDSLSGSS LYSASANLPV 600
    MGHDKFPSDL DLDMFNGSLE CDMESIIRSE LMDADGLDFN FDSLISTQNV 650
    VGLNVGNFTG AKQASSQSWV PG 672
    Length:672
    Mass (Da):71,064
    Last modified:November 1, 1999 - v1
    Checksum:iEC218D9BA0C1DAC5
    GO

    Sequence cautioni

    The sequence AAH19532.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114259 mRNA. Translation: AAD42107.1.
    AK047413 mRNA. Translation: BAC33049.1.
    AC116179 Genomic DNA. No translation available.
    AC140402 Genomic DNA. No translation available.
    CH466540 Genomic DNA. Translation: EDL04998.1.
    BC019532 mRNA. Translation: AAH19532.1. Sequence problems.
    CCDSiCCDS23810.1.
    RefSeqiNP_062714.1. NM_019740.2.
    XP_006512869.1. XM_006512806.1.
    UniGeneiMm.338613.
    Mm.391700.
    Mm.417859.
    Mm.466459.

    Genome annotation databases

    EnsembliENSMUST00000056974; ENSMUSP00000050683; ENSMUSG00000048756.
    ENSMUST00000105502; ENSMUSP00000101141; ENSMUSG00000048756.
    ENSMUST00000175881; ENSMUSP00000135380; ENSMUSG00000048756.
    GeneIDi56484.
    KEGGimmu:56484.
    UCSCiuc007eyl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114259 mRNA. Translation: AAD42107.1 .
    AK047413 mRNA. Translation: BAC33049.1 .
    AC116179 Genomic DNA. No translation available.
    AC140402 Genomic DNA. No translation available.
    CH466540 Genomic DNA. Translation: EDL04998.1 .
    BC019532 mRNA. Translation: AAH19532.1 . Sequence problems.
    CCDSi CCDS23810.1.
    RefSeqi NP_062714.1. NM_019740.2.
    XP_006512869.1. XM_006512806.1.
    UniGenei Mm.338613.
    Mm.391700.
    Mm.417859.
    Mm.466459.

    3D structure databases

    ProteinModelPortali Q9WVH4.
    SMRi Q9WVH4. Positions 157-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WVH4. 2 interactions.
    STRINGi 10090.ENSMUSP00000101141.

    PTM databases

    PhosphoSitei Q9WVH4.

    Proteomic databases

    PRIDEi Q9WVH4.

    Protocols and materials databases

    DNASUi 56484.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056974 ; ENSMUSP00000050683 ; ENSMUSG00000048756 .
    ENSMUST00000105502 ; ENSMUSP00000101141 ; ENSMUSG00000048756 .
    ENSMUST00000175881 ; ENSMUSP00000135380 ; ENSMUSG00000048756 .
    GeneIDi 56484.
    KEGGi mmu:56484.
    UCSCi uc007eyl.1. mouse.

    Organism-specific databases

    CTDi 2309.
    MGIi MGI:1890081. Foxo3.

    Phylogenomic databases

    eggNOGi COG5025.
    GeneTreei ENSGT00390000000589.
    HOGENOMi HOG000251635.
    HOVERGENi HBG078744.
    InParanoidi Q9WVH4.
    KOi K09408.
    OMAi NLPVMGH.
    OrthoDBi EOG7R2BJD.
    PhylomeDBi Q9WVH4.
    TreeFami TF315583.

    Enzyme and pathway databases

    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_218211. AKT phosphorylates targets in the nucleus.
    REACT_220645. Signaling by NODAL.

    Miscellaneous databases

    ChiTaRSi FOXO3. mouse.
    NextBioi 312750.
    PROi Q9WVH4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WVH4.
    Bgeei Q9WVH4.
    Genevestigatori Q9WVH4.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00250. Fork_head. 1 hit.
    [Graphical view ]
    PRINTSi PR00053. FORKHEAD.
    SMARTi SM00339. FH. 1 hit.
    [Graphical view ]
    PROSITEi PS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of members of the FKHR (FOX O) subclass of winged-helix transcription factors in the mouse."
      Biggs W.H. III, Cavenee W.K., Arden K.C.
      Mamm. Genome 12:416-425(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-255.
    6. "SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction."
      Wang F., Nguyen M., Qin F.X., Tong Q.
      Aging Cell 6:505-514(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH SIRT2.
    7. "Novel repressor regulates insulin sensitivity through interaction with Foxo1."
      Nakae J., Cao Y., Hakuno F., Takemori H., Kawano Y., Sekioka R., Abe T., Kiyonari H., Tanaka T., Sakai J., Takahashi S., Itoh H.
      EMBO J. 31:2275-2295(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiFOXO3_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVH4
    Secondary accession number(s): D3Z6Y6, Q05CZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3