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P17719

- DYR_DROME

UniProt

P17719 - DYR_DROME

Protein

Dihydrofolate reductase

Gene

Dhfr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    By interacting with vestigial (vg), may control genes involved in DNA replication.
    Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.By similarity

    Catalytic activityi

    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei69 – 691SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 217NADPBy similarity
    Nucleotide bindingi53 – 553NADPBy similarity
    Nucleotide bindingi75 – 773NADPBy similarity
    Nucleotide bindingi113 – 1208NADPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: FlyBase
    2. NADP binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. glycine biosynthetic process Source: InterPro
    3. nucleotide biosynthetic process Source: InterPro
    4. one-carbon metabolic process Source: UniProtKB-KW
    5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication, One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:Dhfr
    ORF Names:CG14887
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0004087. Dhfr.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 182182Dihydrofolate reductasePRO_0000186370Add
    BLAST

    Proteomic databases

    PaxDbiP17719.

    Expressioni

    Gene expression databases

    BgeeiP17719.

    Interactioni

    Subunit structurei

    Monomer. Interacts with vg.1 Publication

    Protein-protein interaction databases

    BioGridi67048. 3 interactions.
    DIPiDIP-20310N.
    IntActiP17719. 1 interaction.
    MINTiMINT-323567.
    STRINGi7227.FBpp0082746.

    Structurei

    3D structure databases

    ProteinModelPortaliP17719.
    SMRiP17719. Positions 4-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 180178DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 346Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the dihydrofolate reductase family.Curated
    Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0262.
    GeneTreeiENSGT00390000010283.
    InParanoidiP17719.
    KOiK00287.
    OMAiLPWHPIR.
    OrthoDBiEOG7V1FS3.
    PhylomeDBiP17719.

    Family and domain databases

    Gene3Di3.40.430.10. 1 hit.
    InterProiIPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view]
    PfamiPF00186. DHFR_1. 1 hit.
    [Graphical view]
    PRINTSiPR00070. DHFR.
    SUPFAMiSSF53597. SSF53597. 1 hit.
    PROSITEiPS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17719-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRFNLIVAV CENFGIGIRG DLPWRIKSEL KYFSRTTKRT SDPTKQNAVV    50
    MGRKTYFGVP ESKRPLPDRL NIVLSTTLQE SDLPKGVLLC PNLETAMKIL 100
    EEQNEVENIW IVGGSGVYEE AMASPRCHRL YITKIMQKFD CDTFFPAIPD 150
    SFREVAPDSD MPLGVQEENG IKFEYKILEK HS 182
    Length:182
    Mass (Da):20,775
    Last modified:June 1, 2001 - v3
    Checksum:iD2C9198F1D2CE430
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → T AA sequence (PubMed:2116172)Curated
    Sequence conflicti11 – 111C → S AA sequence (PubMed:2116172)Curated
    Sequence conflicti134 – 1341K → Q in AAA19051. (PubMed:8195153)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U06861 Unassigned DNA. Translation: AAA19051.1.
    AE014297 Genomic DNA. Translation: AAF55324.1.
    AE014297 Genomic DNA. Translation: ABI31175.1.
    PIRiA53803.
    S10759. A33105.
    RefSeqiNP_001036720.1. NM_001043255.2.
    NP_732147.1. NM_169721.2.
    UniGeneiDm.8025.

    Genome annotation databases

    EnsemblMetazoaiFBtr0083295; FBpp0082746; FBgn0004087.
    FBtr0110910; FBpp0110210; FBgn0004087.
    GeneIDi42003.
    KEGGidme:Dmel_CG14887.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U06861 Unassigned DNA. Translation: AAA19051.1 .
    AE014297 Genomic DNA. Translation: AAF55324.1 .
    AE014297 Genomic DNA. Translation: ABI31175.1 .
    PIRi A53803.
    S10759. A33105.
    RefSeqi NP_001036720.1. NM_001043255.2.
    NP_732147.1. NM_169721.2.
    UniGenei Dm.8025.

    3D structure databases

    ProteinModelPortali P17719.
    SMRi P17719. Positions 4-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67048. 3 interactions.
    DIPi DIP-20310N.
    IntActi P17719. 1 interaction.
    MINTi MINT-323567.
    STRINGi 7227.FBpp0082746.

    Proteomic databases

    PaxDbi P17719.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0083295 ; FBpp0082746 ; FBgn0004087 .
    FBtr0110910 ; FBpp0110210 ; FBgn0004087 .
    GeneIDi 42003.
    KEGGi dme:Dmel_CG14887.

    Organism-specific databases

    CTDi 1719.
    FlyBasei FBgn0004087. Dhfr.

    Phylogenomic databases

    eggNOGi COG0262.
    GeneTreei ENSGT00390000010283.
    InParanoidi P17719.
    KOi K00287.
    OMAi LPWHPIR.
    OrthoDBi EOG7V1FS3.
    PhylomeDBi P17719.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Miscellaneous databases

    GenomeRNAii 42003.
    NextBioi 826685.
    PROi P17719.

    Gene expression databases

    Bgeei P17719.

    Family and domain databases

    Gene3Di 3.40.430.10. 1 hit.
    InterProi IPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view ]
    Pfami PF00186. DHFR_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00070. DHFR.
    SUPFAMi SSF53597. SSF53597. 1 hit.
    PROSITEi PS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dihydrofolate reductase of Drosophila. Cloning and expression of a gene with a rare transcript."
      Hao H., Tyshenko M.G., Walker V.K.
      J. Biol. Chem. 269:15179-15185(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 155-176.
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "The purification of dihydrofolate reductase from Drosophila melanogaster."
      Rancourt S.L., Walker V.K.
      Biochim. Biophys. Acta 1039:261-268(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-23.
      Strain: Canton-S.
    5. "The Drosophila wing differentiation factor vestigial-scalloped is required for cell proliferation and cell survival at the dorso-ventral boundary of the wing imaginal disc."
      Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A., Vaudin P., Becker J.L., Silber J.
      Cell Death Differ. 11:110-122(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VG, INVOLVEMENT IN DNA REPLICATION.

    Entry informationi

    Entry nameiDYR_DROME
    AccessioniPrimary (citable) accession number: P17719
    Secondary accession number(s): A4V302, Q9VEU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3