Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UKP4

- ATS7_HUMAN

UniProt

Q9UKP4 - ATS7_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 7

Gene

ADAMTS7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Metalloprotease that may play a role in the degradation of COMP.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    pH dependencei

    Optimum pH is between 7.5 and 9.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi204 – 2041Zinc; in inhibited formBy similarity
    Metal bindingi388 – 3881Zinc; catalyticBy similarity
    Active sitei389 – 3891PROSITE-ProRule annotation
    Metal bindingi392 – 3921Zinc; catalyticBy similarity
    Metal bindingi398 – 3981Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: BHF-UCL
    2. metallopeptidase activity Source: ProtInc
    3. protein binding Source: BHF-UCL
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to BMP stimulus Source: BHF-UCL
    2. cellular response to interleukin-1 Source: BHF-UCL
    3. cellular response to tumor necrosis factor Source: BHF-UCL
    4. negative regulation of chondrocyte differentiation Source: BHF-UCL
    5. proteolysis involved in cellular protein catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.231.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 7 (EC:3.4.24.-)
    Short name:
    ADAM-TS 7
    Short name:
    ADAM-TS7
    Short name:
    ADAMTS-7
    Alternative name(s):
    COMPase
    Gene namesi
    Name:ADAMTS7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:223. ADAMTS7.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix By similarity
    Note: Also found associated with the external cell surface.By similarity

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24551.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 2362091 PublicationPRO_0000029176Add
    BLAST
    Chaini237 – 16861450A disintegrin and metalloproteinase with thrombospondin motifs 7PRO_0000029177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi318 ↔ 372By similarity
    Disulfide bondi347 ↔ 354By similarity
    Disulfide bondi366 ↔ 447By similarity
    Disulfide bondi405 ↔ 431By similarity
    Disulfide bondi474 ↔ 497By similarity
    Disulfide bondi485 ↔ 503By similarity
    Disulfide bondi492 ↔ 522By similarity
    Disulfide bondi516 ↔ 527By similarity
    Disulfide bondi550 ↔ 587By similarity
    Disulfide bondi554 ↔ 592By similarity
    Disulfide bondi565 ↔ 577By similarity
    Glycosylationi693 – 6931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi778 – 7781N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs. N- and C-glycosylations can also facilitate secretion. O-glycosylated proteoglycan. Contains chondroitin sulfate.1 Publication
    May be cleaved by a furin endopeptidase By similarity. The precursor is sequentially processed.By similarity1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Proteoglycan, Zymogen

    Proteomic databases

    PaxDbiQ9UKP4.
    PRIDEiQ9UKP4.

    PTM databases

    PhosphoSiteiQ9UKP4.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments.2 Publications

    Inductioni

    Up-regulated in articular cartilage and synovium from arthritis patients.1 Publication

    Gene expression databases

    BgeeiQ9UKP4.
    CleanExiHS_ADAMTS7.
    GenevestigatoriQ9UKP4.

    Organism-specific databases

    HPAiHPA034581.

    Interactioni

    Subunit structurei

    Interacts with COMP.1 Publication

    Protein-protein interaction databases

    IntActiQ9UKP4. 3 interactions.
    STRINGi9606.ENSP00000373472.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKP4.
    SMRiQ9UKP4. Positions 239-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini242 – 452211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini462 – 53776DisintegrinAdd
    BLAST
    Domaini538 – 59356TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini821 – 88060TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini881 – 94060TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini942 – 99554TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1411 – 145949TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1462 – 152261TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1523 – 156745TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1569 – 162961TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1632 – 167241PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni698 – 809112SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi202 – 2098Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi595 – 697103Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 PLAC domain.PROSITE-ProRule annotation
    Contains 8 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237764.
    HOGENOMiHOG000015092.
    HOVERGENiHBG050620.
    KOiK08622.
    OMAiKGKYCVG.
    OrthoDBiEOG7V765X.
    PhylomeDBiQ9UKP4.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 7 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 8 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 8 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 7 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UKP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGGPSPRSP APLLRPLLLL LCALAPGAPG PAPGRATEGR AALDIVHPVR     50
    VDAGGSFLSY ELWPRALRKR DVSVRRDAPA FYELQYRGRE LRFNLTANQH 100
    LLAPGFVSET RRRGGLGRAH IRAHTPACHL LGEVQDPELE GGLAAISACD 150
    GLKGVFQLSN EDYFIEPLDS APARPGHAQP HVVYKRQAPE RLAQRGDSSA 200
    PSTCGVQVYP ELESRRERWE QRQQWRRPRL RRLHQRSVSK EKWVETLVVA 250
    DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE 300
    EEDLKITHHA DNTLKSFCKW QKSINMKGDA HPLHHDTAIL LTRKDLCAAM 350
    NRPCETLGLS HVAGMCQPHR SCSINEDTGL PLAFTVAHEL GHSFGIQHDG 400
    SGNDCEPVGK RPFIMSPQLL YDAAPLTWSR CSRQYITRFL DRGWGLCLDD 450
    PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA YSAFCEDMDN VCHTLWCSVG 500
    TTCHSKLDAA VDGTRCGENK WCLSGECVPV GFRPEAVDGG WSGWSAWSIC 550
    SRSCGMGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR 600
    HVQCSHFDAM LYKGQLHTWV PVVNDVNPCE LHCRPANEYF AEKLRDAVVD 650
    GTPCYQVRAS RDLCINGICK NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV 700
    SGTFEEAEGL GYVDVGLIPA GAREIRIQEV AEAANFLALR SEDPEKYFLN 750
    GGWTIQWNGD YQVAGTTFTY ARRGNWENLT SPGPTKEPVW IQLLFQESNP 800
    GVHYEYTIHR EAGGHDEVPP PVFSWHYGPW TKCTVTCGRG VQRQNVYCLE 850
    RQAGPVDEEH CDPLGRPDDQ QRKCSEQPCP ARWWAGEWQL CSSSCGPGGL 900
    SRRAVLCIRS VGLDEQSALE PPACEHLPRP PTETPCNRHV PCPATWAVGN 950
    WSQCSVTCGE GTQRRNVLCT NDTGVPCDEA QQPASEVTCS LPLCRWPLGT 1000
    LGPEGSGSGS SSHELFNEAD FIPHHLAPRP SPASSPKPGT MGNAIEEEAP 1050
    ELDLPGPVFV DDFYYDYNFI NFHEDLSYGP SEEPDLDLAG TGDRTPPPHS 1100
    HPAAPSTGSP VPATEPPAAK EEGVLGPWSP SPWPSQAGRS PPPPSEQTPG 1150
    NPLINFLPEE DTPIGAPDLG LPSLSWPRVS TDGLQTPATP ESQNDFPVGK 1200
    DSQSQLPPPW RDRTNEVFKD DEEPKGRGAP HLPPRPSSTL PPLSPVGSTH 1250
    SSPSPDVAEL WTGGTVAWEP ALEGGLGPVD SELWPTVGVA SLLPPPIAPL 1300
    PEMKVRDSSL EPGTPSFPTP GPGSWDLQTV AVWGTFLPTT LTGLGHMPEP 1350
    ALNPGPKGQP ESLSPEVPLS SRLLSTPAWD SPANSHRVPE TQPLAPSLAE 1400
    AGPPADPLVV RNAGWQAGNW SECSTTCGLG AVWRPVRCSS GRDEDCAPAG 1450
    RPQPARRCHL RPCATWHSGN WSKCSRSCGG GSSVRDVQCV DTRDLRPLRP 1500
    FHCQPGPAKP PAHRPCGAQP CLSWYTSSWR ECSEACGGGE QQRLVTCPEP 1550
    GLCEEALRPN TTRPCNTHPC TQWVVGPWGQ CSGPCGGGVQ RRLVKCVNTQ 1600
    TGLPEEDSDQ CGHEAWPESS RPCGTEDCEP VEPPRCERDR LSFGFCETLR 1650
    LLGRCQLPTI RTQCCRSCSP PSHGAPSRGH QRVARR 1686
    Length:1,686
    Mass (Da):184,095
    Last modified:September 2, 2008 - v2
    Checksum:iAB38264B8E8DB740
    GO

    Sequence cautioni

    The sequence AAD56358.1 differs from that shown. Reason: Probable cloning artifact.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti642 – 6421E → K in AAD56358. (PubMed:16585064)Curated
    Sequence conflicti1101 – 11011H → R in AAQ94616. (PubMed:15489334)Curated
    Sequence conflicti1364 – 13641S → T in AAQ94616. (PubMed:15489334)Curated
    Sequence conflicti1479 – 14791G → D in AAQ94616. (PubMed:15489334)Curated
    Sequence conflicti1511 – 15111P → H in AAQ94616. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141S → P.
    Corresponds to variant rs3825807 [ dbSNP | Ensembl ].
    VAR_046112
    Natural varianti307 – 3071T → M.1 Publication
    Corresponds to variant rs2127898 [ dbSNP | Ensembl ].
    VAR_046113
    Natural varianti1319 – 13191T → A.1 Publication
    Corresponds to variant rs11630236 [ dbSNP | Ensembl ].
    VAR_046114
    Natural varianti1414 – 14141G → S.1 Publication
    Corresponds to variant rs2929155 [ dbSNP | Ensembl ].
    VAR_046115
    Natural varianti1583 – 15831G → A.1 Publication
    Corresponds to variant rs7495616 [ dbSNP | Ensembl ].
    VAR_046116

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY327122 mRNA. Translation: AAQ94616.1.
    BC061631 mRNA. Translation: AAH61631.1.
    AF140675 mRNA. Translation: AAD56358.1. Sequence problems.
    CCDSiCCDS32303.1.
    RefSeqiNP_055087.2. NM_014272.3.
    UniGeneiHs.16441.

    Genome annotation databases

    EnsembliENST00000388820; ENSP00000373472; ENSG00000136378.
    GeneIDi11173.
    KEGGihsa:11173.
    UCSCiuc002bej.4. human.

    Polymorphism databases

    DMDMi205371741.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY327122 mRNA. Translation: AAQ94616.1 .
    BC061631 mRNA. Translation: AAH61631.1 .
    AF140675 mRNA. Translation: AAD56358.1 . Sequence problems.
    CCDSi CCDS32303.1.
    RefSeqi NP_055087.2. NM_014272.3.
    UniGenei Hs.16441.

    3D structure databases

    ProteinModelPortali Q9UKP4.
    SMRi Q9UKP4. Positions 239-713.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9UKP4. 3 interactions.
    STRINGi 9606.ENSP00000373472.

    Protein family/group databases

    MEROPSi M12.231.

    PTM databases

    PhosphoSitei Q9UKP4.

    Polymorphism databases

    DMDMi 205371741.

    Proteomic databases

    PaxDbi Q9UKP4.
    PRIDEi Q9UKP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000388820 ; ENSP00000373472 ; ENSG00000136378 .
    GeneIDi 11173.
    KEGGi hsa:11173.
    UCSCi uc002bej.4. human.

    Organism-specific databases

    CTDi 11173.
    GeneCardsi GC15M079051.
    H-InvDB HIX0012467.
    HGNCi HGNC:223. ADAMTS7.
    HPAi HPA034581.
    MIMi 605009. gene.
    neXtProti NX_Q9UKP4.
    PharmGKBi PA24551.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237764.
    HOGENOMi HOG000015092.
    HOVERGENi HBG050620.
    KOi K08622.
    OMAi KGKYCVG.
    OrthoDBi EOG7V765X.
    PhylomeDBi Q9UKP4.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GenomeRNAii 11173.
    NextBioi 42517.
    PROi Q9UKP4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UKP4.
    CleanExi HS_ADAMTS7.
    Genevestigatori Q9UKP4.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 7 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 8 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 8 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 7 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein."
      Liu C.-J., Kong W., Ilalov K., Yu S., Xu K., Prazak L., Fajardo M., Sehgal B., Di Cesare P.E.
      FASEB J. 20:988-990(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, PH DEPENDENCE, INTERACTION WITH COMP, INDUCTION, TISSUE SPECIFICITY, VARIANTS ALA-1319; SER-1414 AND ALA-1583.
    2. "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], VARIANT MET-307.
      Tissue: Ovary.
    3. "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
      Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
      J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    4. "ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain."
      Somerville R.P.T., Longpre J.-M., Apel E.D., Lewis R.M., Wang L.W., Sanes J.R., Leduc R., Apte S.S.
      J. Biol. Chem. 279:35159-35175(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 237-243, IDENTIFICATION, GLYCOSYLATION, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiATS7_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKP4
    Secondary accession number(s): Q14F51, Q6P7J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3