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Q92871

- PMM1_HUMAN

UniProt

Q92871 - PMM1_HUMAN

Protein

Phosphomannomutase 1

Gene

PMM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.1 Publication

    Catalytic activityi

    Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity.By similarity

    Kineticsi

    1. KM=54 µM for alpha-D-mannose 1-phosphate1 Publication
    2. KM=7.5 µM for alpha-D-glucose 1-phosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei19 – 191Nucleophile1 Publication
    Metal bindingi19 – 191Magnesium
    Active sitei21 – 211Proton donor/acceptorSequence Analysis
    Metal bindingi21 – 211Magnesium; via carbonyl oxygen
    Binding sitei28 – 281Substrate
    Binding sitei132 – 1321Substrate
    Binding sitei143 – 1431Substrate
    Binding sitei150 – 1501Substrate
    Binding sitei186 – 1861Substrate; via amide nitrogen
    Binding sitei188 – 1881Substrate
    Binding sitei190 – 1901Substrate
    Metal bindingi218 – 2181Magnesium

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphomannomutase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    3. GDP-mannose biosynthetic process Source: Reactome
    4. mannose biosynthetic process Source: InterPro
    5. mannose metabolic process Source: UniProtKB
    6. post-translational protein modification Source: Reactome
    7. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi5.4.2.8. 2681.
    ReactomeiREACT_22423. Synthesis of GDP-mannose.
    UniPathwayiUPA00126; UER00424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase 1 (EC:5.4.2.8)
    Short name:
    PMM 1
    Alternative name(s):
    PMMH-22
    Gene namesi
    Name:PMM1
    Synonyms:PMMH22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9114. PMM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33440.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 262261Phosphomannomutase 1PRO_0000199692Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ92871.
    PaxDbiQ92871.
    PRIDEiQ92871.

    PTM databases

    PhosphoSiteiQ92871.

    Expressioni

    Tissue specificityi

    Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.

    Gene expression databases

    ArrayExpressiQ92871.
    BgeeiQ92871.
    CleanExiHS_PMM1.
    GenevestigatoriQ92871.

    Organism-specific databases

    HPAiHPA030712.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111385. 4 interactions.
    IntActiQ92871. 4 interactions.
    MINTiMINT-1482037.
    STRINGi9606.ENSP00000216259.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218
    Turni22 – 243
    Helixi33 – 4210
    Turni43 – 453
    Beta strandi46 – 516
    Helixi56 – 638
    Turni66 – 683
    Helixi69 – 724
    Beta strandi74 – 785
    Helixi79 – 813
    Beta strandi83 – 864
    Beta strandi89 – 913
    Helixi96 – 1005
    Helixi102 – 11716
    Beta strandi128 – 1314
    Beta strandi136 – 1383
    Helixi147 – 16014
    Helixi162 – 17312
    Turni174 – 1763
    Beta strandi179 – 1824
    Beta strandi185 – 1873
    Beta strandi189 – 1935
    Helixi198 – 2014
    Helixi202 – 2054
    Turni206 – 2094
    Beta strandi211 – 2188
    Helixi227 – 2315
    Beta strandi235 – 2395
    Helixi243 – 25412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FUCX-ray2.10A1-262[»]
    2FUEX-ray1.75A1-262[»]
    ProteinModelPortaliQ92871.
    SMRiQ92871. Positions 13-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92871.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic PMM family.Curated

    Phylogenomic databases

    eggNOGiCOG0561.
    HOGENOMiHOG000181843.
    HOVERGENiHBG009971.
    InParanoidiQ92871.
    KOiK17497.
    OMAiNDYEIYD.
    OrthoDBiEOG773XH0.
    PhylomeDBiQ92871.
    TreeFamiTF300874.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view]
    PANTHERiPTHR10466. PTHR10466. 1 hit.
    PfamiPF03332. PMM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q92871-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV    50
    VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL 100
    GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER 150
    IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY 200
    CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC 250
    REIFFPETAH EA 262
    Length:262
    Mass (Da):29,747
    Last modified:November 1, 1997 - v2
    Checksum:i1FBA7BFC9C3BB0BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111K → R in AAC51117. (PubMed:9070917)Curated
    Sequence conflicti169 – 1691A → D in AAC51117. (PubMed:9070917)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62526 mRNA. Translation: AAC51117.1.
    D87810 mRNA. Translation: BAA13460.1.
    U86070 mRNA. Translation: AAC00023.1.
    CR456544 mRNA. Translation: CAG30430.1.
    AK289368 mRNA. Translation: BAF82057.1.
    AK316580 mRNA. Translation: BAG38168.1.
    AL023553 Genomic DNA. Translation: CAB46025.1.
    CH471095 Genomic DNA. Translation: EAW60443.1.
    BC010855 mRNA. Translation: AAH10855.1.
    BC016818 mRNA. Translation: AAH16818.1.
    CCDSiCCDS14020.1.
    RefSeqiNP_002667.2. NM_002676.2.
    UniGeneiHs.75835.

    Genome annotation databases

    EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
    GeneIDi5372.
    KEGGihsa:5372.
    UCSCiuc003bal.2. human.

    Polymorphism databases

    DMDMi2499519.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62526 mRNA. Translation: AAC51117.1 .
    D87810 mRNA. Translation: BAA13460.1 .
    U86070 mRNA. Translation: AAC00023.1 .
    CR456544 mRNA. Translation: CAG30430.1 .
    AK289368 mRNA. Translation: BAF82057.1 .
    AK316580 mRNA. Translation: BAG38168.1 .
    AL023553 Genomic DNA. Translation: CAB46025.1 .
    CH471095 Genomic DNA. Translation: EAW60443.1 .
    BC010855 mRNA. Translation: AAH10855.1 .
    BC016818 mRNA. Translation: AAH16818.1 .
    CCDSi CCDS14020.1.
    RefSeqi NP_002667.2. NM_002676.2.
    UniGenei Hs.75835.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FUC X-ray 2.10 A 1-262 [» ]
    2FUE X-ray 1.75 A 1-262 [» ]
    ProteinModelPortali Q92871.
    SMRi Q92871. Positions 13-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111385. 4 interactions.
    IntActi Q92871. 4 interactions.
    MINTi MINT-1482037.
    STRINGi 9606.ENSP00000216259.

    PTM databases

    PhosphoSitei Q92871.

    Polymorphism databases

    DMDMi 2499519.

    Proteomic databases

    MaxQBi Q92871.
    PaxDbi Q92871.
    PRIDEi Q92871.

    Protocols and materials databases

    DNASUi 5372.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216259 ; ENSP00000216259 ; ENSG00000100417 .
    GeneIDi 5372.
    KEGGi hsa:5372.
    UCSCi uc003bal.2. human.

    Organism-specific databases

    CTDi 5372.
    GeneCardsi GC22M041972.
    HGNCi HGNC:9114. PMM1.
    HPAi HPA030712.
    MIMi 601786. gene.
    neXtProti NX_Q92871.
    PharmGKBi PA33440.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0561.
    HOGENOMi HOG000181843.
    HOVERGENi HBG009971.
    InParanoidi Q92871.
    KOi K17497.
    OMAi NDYEIYD.
    OrthoDBi EOG773XH0.
    PhylomeDBi Q92871.
    TreeFami TF300874.

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00424 .
    BRENDAi 5.4.2.8. 2681.
    Reactomei REACT_22423. Synthesis of GDP-mannose.

    Miscellaneous databases

    EvolutionaryTracei Q92871.
    GeneWikii PMM1.
    GenomeRNAii 5372.
    NextBioi 20842.
    PROi Q92871.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92871.
    Bgeei Q92871.
    CleanExi HS_PMM1.
    Genevestigatori Q92871.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view ]
    PANTHERi PTHR10466. PTHR10466. 1 hit.
    Pfami PF03332. PMM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13."
      Matthijs G., Schollen E., Pirard M., Budarf M.L., van Schaftingen E., Cassiman J.-J.
      Genomics 40:41-47(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13."
      Wada Y., Sakamoto M.
      Genomics 39:416-417(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Hansen S.H., Frank S.R., Casanova J.E.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Brain and Pancreas.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a."
      Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N.
      J. Biol. Chem. 281:14918-14926(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND MANNOSE 1-PHOSPHATE, FUNCTION, ACTIVE SITE, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiPMM1_HUMAN
    AccessioniPrimary (citable) accession number: Q92871
    Secondary accession number(s): A8K003, Q92586
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 137 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3