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Q9EQQ0

- SUV92_MOUSE

UniProt

Q9EQQ0 - SUV92_MOUSE

Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

Suv39h2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.5 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi258 – 2581Zinc 1By similarity
    Metal bindingi258 – 2581Zinc 2By similarity
    Metal bindingi260 – 2601Zinc 1By similarity
    Metal bindingi263 – 2631Zinc 1By similarity
    Metal bindingi263 – 2631Zinc 3By similarity
    Metal bindingi268 – 2681Zinc 1By similarity
    Metal bindingi269 – 2691Zinc 1By similarity
    Metal bindingi269 – 2691Zinc 2By similarity
    Metal bindingi296 – 2961Zinc 2By similarity
    Metal bindingi296 – 2961Zinc 3By similarity
    Metal bindingi300 – 3001Zinc 2By similarity
    Metal bindingi302 – 3021Zinc 3By similarity
    Metal bindingi306 – 3061Zinc 3By similarity
    Binding sitei371 – 3711S-adenosyl-L-methioninePROSITE-ProRule annotation
    Metal bindingi400 – 4001Zinc 4By similarity
    Metal bindingi465 – 4651Zinc 4By similarity
    Metal bindingi467 – 4671Zinc 4By similarity
    Metal bindingi472 – 4721Zinc 4By similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone-lysine N-methyltransferase activity Source: UniProtKB
    3. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
    4. methyltransferase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein methyltransferase activity Source: MGI
    7. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. chromatin assembly or disassembly Source: UniProtKB
    3. chromatin remodeling Source: UniProtKB
    4. histone H3-K9 dimethylation Source: UniProtKB
    5. histone H3-K9 methylation Source: MGI
    6. histone H3-K9 trimethylation Source: UniProtKB
    7. histone lysine methylation Source: MGI
    8. male meiosis Source: UniProtKB
    9. negative regulation of circadian rhythm Source: UniProtKB
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. rhythmic process Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SUV39H2 (EC:2.1.1.43)
    Alternative name(s):
    Histone H3-K9 methyltransferase 2
    Short name:
    H3-K9-HMTase 2
    Suppressor of variegation 3-9 homolog 2
    Short name:
    Su(var)3-9 homolog 2
    Gene namesi
    Name:Suv39h2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1890396. Suv39h2.

    Subcellular locationi

    Nucleus. Chromosome. Chromosomecentromere
    Note: Associates with centromeric constitutive heterochromatin during most stages of spermato- and spermiogenesis. Predominantly accumulates at the sex chromosomes present at the XY body.

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. chromosome, centromeric region Source: UniProtKB-SubCell
    3. nuclear heterochromatin Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice lacking Suv39h1 and Suv39h2 display severely impaired viability and chromosomal instabilities that are associated with an increased tumor risk and perturbed chromosome interactions during male meiosis. They also show a higher level of histone H3 with phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and an increased portion of cells with aberrant nuclear morphologies.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 477477Histone-lysine N-methyltransferase SUV39H2PRO_0000186060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei448 – 4481PhosphoserineBy similarity
    Modified residuei451 – 4511PhosphoserineBy similarity
    Modified residuei455 – 4551PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9EQQ0.

    PTM databases

    PhosphoSiteiQ9EQQ0.

    Expressioni

    Tissue specificityi

    Testis specific; predominant expression in type B spermatogonia and preleptotene spermatocytes.

    Developmental stagei

    Strong expression in early embryos with a peak at E10.5. Expression is down-regulated at E17.5, and is nearly absent during postnatal development. In adult testes, prominent expression in late but not early spermatocytes.

    Gene expression databases

    ArrayExpressiQ9EQQ0.
    BgeeiQ9EQQ0.
    GenevestigatoriQ9EQQ0.

    Interactioni

    Subunit structurei

    Interacts with SMAD5. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.

    Protein-protein interaction databases

    BioGridi211103. 2 interactions.
    DIPiDIP-32586N.
    IntActiQ9EQQ0. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQQ0.
    SMRiQ9EQQ0. Positions 119-167, 191-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini118 – 17659ChromoPROSITE-ProRule annotationAdd
    BLAST
    Domaini256 – 31459Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini317 – 440124SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 47717Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni328 – 3303S-adenosyl-L-methionine bindingBy similarity
    Regioni397 – 3982S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin By similarity.By similarity
    In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 1 chromo domain.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00750000117355.
    HOGENOMiHOG000231244.
    HOVERGENiHBG055621.
    InParanoidiQ9EQQ0.
    KOiK11419.
    OrthoDBiEOG7RJPR0.
    PhylomeDBiQ9EQQ0.
    TreeFamiTF106452.

    Family and domain databases

    InterProiIPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR011381. Histone_H3-K9_MeTrfase.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00385. Chromo. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009343. SUV39_SET. 1 hit.
    SMARTiSM00298. CHROMO. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    PROSITEiPS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51579. SAM_MT43_SUVAR39_3. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9EQQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA    50
    GERRAGSQRA WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK 100
    EKLTCKSIGI TKRNLNNYEV EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE 150
    PLRNLRCPQL LRQFSDDKKT YLAQERKCKA VNSKSLQPAI AEYIVQKAKQ 200
    RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN EYRPAPGISI 250
    NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC 300
    RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE 350
    VITSEEAERR GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC 400
    DPNLQVFSVF IDNLDTRLPR IALFSTRTIN AGEELTFDYQ MKGSGEASSD 450
    SIDHSPAKKR VRTQCKCGAE TCRGYLN 477
    Length:477
    Mass (Da):54,098
    Last modified:March 1, 2001 - v1
    Checksum:i4008D46CF0F07006
    GO

    Sequence cautioni

    The sequence AAF73152.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31T → A in BAC38921. (PubMed:16141072)Curated
    Sequence conflicti131 – 1311Missing in AAF73152. (PubMed:11094092)Curated
    Sequence conflicti323 – 3231K → R in BAB29948. (PubMed:16141072)Curated
    Sequence conflicti323 – 3231K → R in BAC38921. (PubMed:16141072)Curated
    Sequence conflicti325 – 3251S → N in AAF73152. (PubMed:11094092)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149204 Genomic DNA. Translation: AAF73152.1. Sequence problems.
    AF149205 mRNA. Translation: AAG09134.1.
    AK015728 mRNA. Translation: BAB29948.1.
    AK083457 mRNA. Translation: BAC38921.1.
    AL732620 Genomic DNA. Translation: CAM16043.1.
    CCDSiCCDS15652.1.
    RefSeqiNP_073561.2. NM_022724.4.
    UniGeneiMm.128273.
    Mm.23483.

    Genome annotation databases

    EnsembliENSMUST00000027956; ENSMUSP00000027956; ENSMUSG00000026646.
    GeneIDi64707.
    KEGGimmu:64707.
    UCSCiuc008ied.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149204 Genomic DNA. Translation: AAF73152.1 . Sequence problems.
    AF149205 mRNA. Translation: AAG09134.1 .
    AK015728 mRNA. Translation: BAB29948.1 .
    AK083457 mRNA. Translation: BAC38921.1 .
    AL732620 Genomic DNA. Translation: CAM16043.1 .
    CCDSi CCDS15652.1.
    RefSeqi NP_073561.2. NM_022724.4.
    UniGenei Mm.128273.
    Mm.23483.

    3D structure databases

    ProteinModelPortali Q9EQQ0.
    SMRi Q9EQQ0. Positions 119-167, 191-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211103. 2 interactions.
    DIPi DIP-32586N.
    IntActi Q9EQQ0. 1 interaction.

    PTM databases

    PhosphoSitei Q9EQQ0.

    Proteomic databases

    PRIDEi Q9EQQ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027956 ; ENSMUSP00000027956 ; ENSMUSG00000026646 .
    GeneIDi 64707.
    KEGGi mmu:64707.
    UCSCi uc008ied.2. mouse.

    Organism-specific databases

    CTDi 79723.
    MGIi MGI:1890396. Suv39h2.

    Phylogenomic databases

    eggNOGi COG2940.
    GeneTreei ENSGT00750000117355.
    HOGENOMi HOG000231244.
    HOVERGENi HBG055621.
    InParanoidi Q9EQQ0.
    KOi K11419.
    OrthoDBi EOG7RJPR0.
    PhylomeDBi Q9EQQ0.
    TreeFami TF106452.

    Miscellaneous databases

    NextBioi 320183.
    PROi Q9EQQ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EQQ0.
    Bgeei Q9EQQ0.
    Genevestigatori Q9EQQ0.

    Family and domain databases

    InterProi IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    IPR011381. Histone_H3-K9_MeTrfase.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00385. Chromo. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009343. SUV39_SET. 1 hit.
    SMARTi SM00298. CHROMO. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    PROSITEi PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS51579. SAM_MT43_SUVAR39_3. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression."
      O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R., Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M., Sattler L., Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., Jenuwein T.
      Mol. Cell. Biol. 20:9423-9433(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION.
      Strain: C57BL/6J.
    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: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability."
      Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S., Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A., Opravil S., Doyle M., Sibilia M., Jenuwein T.
      Cell 107:323-337(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. Cited for: FUNCTION.
    6. "Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains."
      Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J., Hunt D.F., Shinkai Y., Allis C.D.
      Mol. Cell 12:1591-1598(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases."
      Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T., Blasco M.A.
      Nat. Genet. 36:94-99(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
      Duong H.A., Weitz C.J.
      Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFIACTION IN A LARGE PER COMPLEX.

    Entry informationi

    Entry nameiSUV92_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQQ0
    Secondary accession number(s): Q8BNK2, Q9CUK3, Q9JLP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 124 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