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Q91Y44

- BRDT_MOUSE

UniProt

Q91Y44 - BRDT_MOUSE

Protein

Bromodomain testis-specific protein

Gene

Brdt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (28 Nov 2012)
      Previous versions | rss
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    Functioni

    Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids. Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei108 – 1081Histone H4K5ac
    Binding sitei108 – 1081JQ1 inhibitorBy similarity
    Binding sitei113 – 1131Histone H4K5ac

    GO - Molecular functioni

    1. histone binding Source: UniProtKB
    2. lysine-acetylated histone binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. chromatin remodeling Source: UniProtKB
    3. histone displacement Source: UniProtKB
    4. male meiosis Source: UniProtKB
    5. male meiosis I Source: UniProtKB
    6. mRNA processing Source: UniProtKB-KW
    7. positive regulation of transcription during meiosis Source: UniProtKB
    8. regulation of RNA splicing Source: UniProtKB
    9. RNA splicing Source: UniProtKB-KW
    10. spermatogenesis Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator

    Keywords - Biological processi

    Differentiation, Meiosis, mRNA processing, mRNA splicing, Spermatogenesis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bromodomain testis-specific protein
    Alternative name(s):
    Bromodomain-containing female sterile homeotic-like protein
    RING3-like protein
    Gene namesi
    Name:Brdt
    Synonyms:Fsrg3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1891374. Brdt.

    Subcellular locationi

    Nucleus 3 Publications
    Note: Detected on chromatin. Excluded from the chromocenter.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable but males are sterile, producing fewer and morphologically abnormal sperm. Aberrant morphogenesis are first detected in step 9 elongating spermatids, and those elongated spermatids that are formed lack the distinctive foci of heterochromatin at the peri-nuclear envelope. Spermatid nuclei show a fragmented chromocenter.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 512PF → AA: Abolishes interaction with histone H4 acetylated N-terminus; when associated with A-55.
    Mutagenesisi55 – 551V → A: Abolishes interaction with histone H4 acetylated N-terminus; when associated with 50-AA-51. 1 Publication
    Mutagenesisi293 – 2942PF → AA: Abolishes interaction with histone H4 acetylated N-terminus; when associated with A-298.
    Mutagenesisi298 – 2981V → A: Abolishes interaction with histone H4 acetylated N-terminus; when associated with 293-AA-294. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 956956Bromodomain testis-specific proteinPRO_0000239227Add
    BLAST

    Proteomic databases

    PaxDbiQ91Y44.
    PRIDEiQ91Y44.

    PTM databases

    PhosphoSiteiQ91Y44.

    Expressioni

    Tissue specificityi

    Testis-specific. Expressed in germinal cells from the early meiotic (pachytene) spermatocytes and during spermiogenesis in the round and elongating spermatids until the condensed late spermatids. No expression seen in spermatogonia.3 Publications

    Developmental stagei

    First detected when type B spermatogonia give rise to early meiotic cells (preleptotene, leptotene and zygotene) at 10-12 days post partum (dpp), producing a clearly detectable protein at 12 dpp (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ91Y44.
    BgeeiQ91Y44.
    CleanExiMM_BRDT.
    GenevestigatoriQ91Y44.

    Interactioni

    Subunit structurei

    Interacts with SMARCE1 By similarity. Interacts with mRNA splicing machinery proteins SRSF2, DDX5, HNRNPK and TARDBP. Interacts with the acetylated N-terminus of histone H1, H2, H3 and H4. Interacts with P-TEFb components CDK9 and CCNT1/cyclin-T1.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ccnt1Q9QWV92EBI-6260929,EBI-2655009
    Cdk9Q99J953EBI-6260929,EBI-2654963

    Protein-protein interaction databases

    BioGridi227777. 1 interaction.
    DIPiDIP-48975N.
    IntActiQ91Y44. 5 interactions.
    MINTiMINT-8409453.
    STRINGi10090.ENSMUSP00000108297.

    Structurei

    Secondary structure

    1
    956
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 368
    Helixi38 – 436
    Helixi46 – 516
    Turni57 – 615
    Helixi65 – 684
    Helixi75 – 839
    Helixi90 – 10718
    Helixi113 – 12917
    Helixi264 – 28219
    Helixi285 – 2873
    Helixi288 – 2914
    Helixi292 – 2943
    Helixi300 – 3034
    Helixi308 – 3114
    Helixi318 – 3269
    Helixi333 – 35018
    Helixi356 – 37217
    Beta strandi375 – 3773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WP1X-ray2.10A/B257-382[»]
    2WP2X-ray2.37A/B17-136[»]
    ProteinModelPortaliQ91Y44.
    SMRiQ91Y44. Positions 27-136, 259-381, 501-579.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91Y44.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 11573Bromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 35873Bromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini496 – 57883NETPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili417 – 44226Sequence AnalysisAdd
    BLAST
    Coiled coili844 – 94097Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi208 – 21912Nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi446 – 49651Lys-richAdd
    BLAST
    Compositional biasi625 – 63915Pro-richAdd
    BLAST
    Compositional biasi643 – 68947Ser-richAdd
    BLAST

    Domaini

    Bromo domains mediate interaction with histones that have acetylated lysine residues at specific positions. Bromo domain 1 mediates binding with histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) (PubMed:19794495).1 Publication

    Sequence similaritiesi

    Contains 2 bromo domains.PROSITE-ProRule annotation
    Contains 1 NET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5076.
    GeneTreeiENSGT00730000110626.
    HOGENOMiHOG000231200.
    HOVERGENiHBG004896.
    InParanoidiQ91Y44.
    KOiK11724.
    OMAiENQRDLG.
    OrthoDBiEOG7TTQ86.
    TreeFamiTF317345.

    Family and domain databases

    Gene3Di1.20.920.10. 2 hits.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR027353. NET_dom.
    [Graphical view]
    PfamiPF00439. Bromodomain. 2 hits.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 2 hits.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 2 hits.
    PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
    PS50014. BROMODOMAIN_2. 2 hits.
    PS51525. NET. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q91Y44-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSLPSRQTAI VNPPPPEYIN TKKSGRLTNQ LQFLQRVVLK ALWKHGFSWP    50
    FQQPVDAVKL KLPDYYTIIK TPMDLNTIKK RLENKYYEKA SECIEDFNTM 100
    FSNCYLYNKT GDDIVVMAQA LEKLFMQKLS QMPQEEQVVG GKERIKKDIQ 150
    QKIAVSSAKE QIPSKAAENV FKRQEIPSGL PDISLSPLNM AQEAPPICDS 200
    QSLVQITKGV KRRADTTTPT TSIAKASSES PPTLRETKPV NMPVKENTVK 250
    NVLPDSQQQH KVLKTVKVTE QLKHCSEILK EMLAKKHLPY AWPFYNPVDA 300
    DALGLHNYYD VVKNPMDLGT IKGKMDNQEY KDAYEFAADV RLMFMNCYKY 350
    NPPDHEVVAM ARTLQDVFEL HFAKIPDEPI ESMHACHLTT NSAQALSRES 400
    SSEASSGDAS SEDSEDERVQ HLAKLQEQLN AVHQQLQVLS QVPLRKLKKK 450
    NEKSKRAPKR KKVNNRDENP RKKPKQMKQK EKAKINQPKK KKPLLKSEEE 500
    DNAKPMNYDE KRQLSLDINK LPGDKLGRIV HIIQSREPSL RNSNPDEIEI 550
    DFETLKASTL RELEKYVLAC LRKRSLKPQA KKVVRSKEEL HSEKKLELER 600
    RLLDVNNQLN CRKRQTKRPA KVEKPPPPPP PPPPPPPPPE LASGSRLTDS 650
    SSSSGSGSGS SSSSSGSSSS SSSSGSASSS SDSSSSDSSD SEPEIFPKFT 700
    GVKQNDLPPK ENIKQIQSSV QDITSAEAPL AQQSTAPCGA PGKHSQQMLG 750
    CQVTQHLQAT ENTASVQTQP LSGDCKRVLL GPPVVHTSAE SLTVLEPECH 800
    APAQKDIKIK NADSWKSLGK PVKASSVLKS SDELFNQFRK AAIEKEVKAR 850
    TQEQMRKHLE HNAKDPKVSQ ENQREPGSGL TLESLSSKVQ DKSLEEDQSE 900
    QQPPSEAQDV SKLWLLKDRN LAREKEQERR RREAMAGTID MTLQSDIMTM 950
    FENNFD 956
    Length:956
    Mass (Da):107,255
    Last modified:November 28, 2012 - v3
    Checksum:iE727044706A67260
    GO
    Isoform 2 (identifier: Q91Y44-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         323-326: GKMD → VNTA
         327-956: Missing.

    Show »
    Length:326
    Mass (Da):36,914
    Checksum:i26432C1A10E68E1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081K → R in BAD91553. 1 PublicationCurated
    Sequence conflicti691 – 6911S → F in AAK50736. (PubMed:15261828)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei323 – 3264GKMD → VNTA in isoform 2. 1 PublicationVSP_019119
    Alternative sequencei327 – 956630Missing in isoform 2. 1 PublicationVSP_019120Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF358660 mRNA. Translation: AAK50736.1.
    AB208640 mRNA. Translation: BAD91553.1.
    AC126598 Genomic DNA. No translation available.
    CH466529 Genomic DNA. Translation: EDL20168.1.
    CCDSiCCDS19500.1. [Q91Y44-1]
    CCDS39197.1. [Q91Y44-2]
    RefSeqiNP_001073342.1. NM_001079873.1. [Q91Y44-2]
    NP_473395.2. NM_054054.2. [Q91Y44-1]
    UniGeneiMm.182836.

    Genome annotation databases

    EnsembliENSMUST00000031215; ENSMUSP00000031215; ENSMUSG00000029279. [Q91Y44-1]
    ENSMUST00000112677; ENSMUSP00000108297; ENSMUSG00000029279. [Q91Y44-2]
    GeneIDi114642.
    KEGGimmu:114642.
    UCSCiuc008ymb.1. mouse. [Q91Y44-2]
    uc008ymc.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Asking life to be patient - Issue 144 of November 2012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF358660 mRNA. Translation: AAK50736.1 .
    AB208640 mRNA. Translation: BAD91553.1 .
    AC126598 Genomic DNA. No translation available.
    CH466529 Genomic DNA. Translation: EDL20168.1 .
    CCDSi CCDS19500.1. [Q91Y44-1 ]
    CCDS39197.1. [Q91Y44-2 ]
    RefSeqi NP_001073342.1. NM_001079873.1. [Q91Y44-2 ]
    NP_473395.2. NM_054054.2. [Q91Y44-1 ]
    UniGenei Mm.182836.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WP1 X-ray 2.10 A/B 257-382 [» ]
    2WP2 X-ray 2.37 A/B 17-136 [» ]
    ProteinModelPortali Q91Y44.
    SMRi Q91Y44. Positions 27-136, 259-381, 501-579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 227777. 1 interaction.
    DIPi DIP-48975N.
    IntActi Q91Y44. 5 interactions.
    MINTi MINT-8409453.
    STRINGi 10090.ENSMUSP00000108297.

    PTM databases

    PhosphoSitei Q91Y44.

    Proteomic databases

    PaxDbi Q91Y44.
    PRIDEi Q91Y44.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031215 ; ENSMUSP00000031215 ; ENSMUSG00000029279 . [Q91Y44-1 ]
    ENSMUST00000112677 ; ENSMUSP00000108297 ; ENSMUSG00000029279 . [Q91Y44-2 ]
    GeneIDi 114642.
    KEGGi mmu:114642.
    UCSCi uc008ymb.1. mouse. [Q91Y44-2 ]
    uc008ymc.1. mouse.

    Organism-specific databases

    CTDi 676.
    MGIi MGI:1891374. Brdt.

    Phylogenomic databases

    eggNOGi COG5076.
    GeneTreei ENSGT00730000110626.
    HOGENOMi HOG000231200.
    HOVERGENi HBG004896.
    InParanoidi Q91Y44.
    KOi K11724.
    OMAi ENQRDLG.
    OrthoDBi EOG7TTQ86.
    TreeFami TF317345.

    Miscellaneous databases

    ChiTaRSi BRDT. mouse.
    EvolutionaryTracei Q91Y44.
    NextBioi 368594.
    PROi Q91Y44.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91Y44.
    Bgeei Q91Y44.
    CleanExi MM_BRDT.
    Genevestigatori Q91Y44.

    Family and domain databases

    Gene3Di 1.20.920.10. 2 hits.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR027353. NET_dom.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 2 hits.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 2 hits.
    PROSITEi PS00633. BROMODOMAIN_1. 2 hits.
    PS50014. BROMODOMAIN_2. 2 hits.
    PS51525. NET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of unique, differentiation stage-specific patterns of expression of the bromodomain-containing genes Brd2, Brd3, Brd4, and Brdt in the mouse testis."
      Shang E., Salazar G., Crowley T.E., Wang X., Lopez R.A., Wang X., Wolgemuth D.J.
      Gene Expr. Patterns 4:513-519(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "The Brd paralogous genes: testis-specific expression of the splicing variants."
      Taniguchi Y.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Testis.
    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. "Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein."
      Pivot-Pajot C., Caron C., Govin J., Vion A., Rousseaux S., Khochbin S.
      Mol. Cell. Biol. 23:5354-5365(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HISTONE H4, MUTAGENESIS OF 50-PRO-PHE-51; VAL-55; 293-PRO-PHE-294 AND VAL-298.
    6. "The first bromodomain of Brdt, a testis-specific member of the BET sub-family of double-bromodomain-containing proteins, is essential for male germ cell differentiation."
      Shang E., Nickerson H.D., Wen D., Wang X., Wolgemuth D.J.
      Development 134:3507-3515(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    7. "Bromodomain testis-specific protein is expressed in mouse oocyte and evolves faster than its ubiquitously expressed paralogs BRD2, -3, and -4."
      Paillisson A., Levasseur A., Gouret P., Callebaut I., Bontoux M., Pontarotti P., Monget P.
      Genomics 89:215-223(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "The first bromodomain of the testis-specific double bromodomain protein Brdt is required for chromocenter organization that is modulated by genetic background."
      Berkovits B.D., Wolgemuth D.J.
      Dev. Biol. 360:358-368(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    9. Cited for: FUNCTION.
    10. Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, INTERACTION WITH CDK9 AND CCNT1.
    11. "The testis-specific double bromodomain-containing protein BRDT forms a complex with multiple spliceosome components and is required for mRNA splicing and 3'-UTR truncation in round spermatids."
      Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.
      Nucleic Acids Res. 40:7162-7175(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRSF2; DDX5; HNRNPK AND TARDBP.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-136 AND 257-382 IN COMPLEX WITH HISTONE H4 PEPTIDE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiBRDT_MOUSE
    AccessioniPrimary (citable) accession number: Q91Y44
    Secondary accession number(s): G3X8Z8, Q59HJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Brdt is a promising target for male contraception. Inhibition by thienodiazepine inhibitor (+)-JQ1 that binds Asn-108, prevents recognition of acetylated histone H4. Treatment of mice with JQ1 reduces seminiferous tubule area, testis size and spermatozoa number and motility without affecting hormone levels. JQ1 causes a complete and reversible contraceptive effect in male mice (PubMed:22901802).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3