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Q9W385

- FRDA_DROME

UniProt

Q9W385 - FRDA_DROME

Protein

Frataxin homolog, mitochondrial

Gene

fh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe2+ to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe2+ to Fe3+. May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization.1 Publication

    Catalytic activityi

    4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. ferroxidase activity Source: UniProtKB-EC
    3. iron chaperone activity Source: FlyBase

    GO - Biological processi

    1. axon transport of mitochondrion Source: FlyBase
    2. cellular iron ion homeostasis Source: UniProtKB-KW
    3. heme biosynthetic process Source: UniProtKB-KW
    4. ion transport Source: UniProtKB-KW
    5. iron-sulfur cluster assembly Source: InterPro
    6. positive regulation of heart contraction Source: FlyBase
    7. regulation of mitochondrial membrane potential Source: FlyBase
    8. response to hydrogen peroxide Source: FlyBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Heme biosynthesis, Ion transport, Iron storage, Iron transport, Transport

    Keywords - Ligandi

    Iron

    Enzyme and pathway databases

    ReactomeiREACT_180798. Mitochondrial iron-sulfur cluster biogenesis.
    REACT_180813. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Frataxin homolog, mitochondrial (EC:1.16.3.1)
    Short name:
    Dfh
    Gene namesi
    Name:fh
    ORF Names:CG8971
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0030092. fh.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: FlyBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 190Frataxin homolog, mitochondrialPRO_0000010133
    Transit peptidei1 – ?Mitochondrion

    Proteomic databases

    PaxDbiQ9W385.
    PRIDEiQ9W385.

    Expressioni

    Developmental stagei

    Expressed throughout development, levels are high during embryogenesis but low in following stages.1 Publication

    Gene expression databases

    BgeeiQ9W385.

    Interactioni

    Subunit structurei

    Monomer (probable predominant form). Oligomer By similarity.By similarity

    Protein-protein interaction databases

    BioGridi58300. 2 interactions.
    IntActiQ9W385. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9W385.
    SMRiQ9W385. Positions 67-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the frataxin family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1965.
    GeneTreeiENSGT00390000005811.
    InParanoidiQ9W385.
    OMAiDALCDYF.
    OrthoDBiEOG7HHWVD.
    PhylomeDBiQ9W385.

    Family and domain databases

    Gene3Di3.30.920.10. 1 hit.
    InterProiIPR017789. Frataxin.
    IPR002908. Frataxin/CyaY.
    IPR020895. Frataxin_CS.
    [Graphical view]
    PANTHERiPTHR16821. PTHR16821. 1 hit.
    PfamiPF01491. Frataxin_Cyay. 1 hit.
    [Graphical view]
    PRINTSiPR00904. FRATAXIN.
    SUPFAMiSSF55387. SSF55387. 1 hit.
    TIGRFAMsiTIGR03421. FeS_CyaY. 1 hit.
    TIGR03422. mito_frataxin. 1 hit.
    PROSITEiPS01344. FRATAXIN_1. 1 hit.
    PS50810. FRATAXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9W385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFAGRLMVRS IVGRACLATM GRWSKPQAHA SQVILPSTPA IAAVAIQCEE    50
    FTANRRLFSS QIETESTLDG ATYERVCSDT LDALCDYFEE LTENASELQG 100
    TDVAYSDGVL TVNLGGQHGT YVINRQTPNK QIWLSSPTSG PKRYDFVGTV 150
    AAGRWIYKHS GQSLHELLQQ EIPGILKSQS VDFLRLPYCS 190
    Length:190
    Mass (Da):20,922
    Last modified:May 1, 2000 - v1
    Checksum:i8C48332C239F3036
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002208 mRNA. Translation: CAC20098.1.
    AF208491 mRNA. Translation: AAG35732.1.
    AF208492 Genomic DNA. Translation: AAG35733.1.
    AE014298 Genomic DNA. Translation: AAF46449.1.
    AY094649 mRNA. Translation: AAM11002.1.
    RefSeqiNP_511094.1. NM_078539.3.
    UniGeneiDm.2903.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071348; FBpp0071283; FBgn0030092.
    GeneIDi31845.
    KEGGidme:Dmel_CG8971.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002208 mRNA. Translation: CAC20098.1 .
    AF208491 mRNA. Translation: AAG35732.1 .
    AF208492 Genomic DNA. Translation: AAG35733.1 .
    AE014298 Genomic DNA. Translation: AAF46449.1 .
    AY094649 mRNA. Translation: AAM11002.1 .
    RefSeqi NP_511094.1. NM_078539.3.
    UniGenei Dm.2903.

    3D structure databases

    ProteinModelPortali Q9W385.
    SMRi Q9W385. Positions 67-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58300. 2 interactions.
    IntActi Q9W385. 1 interaction.

    Proteomic databases

    PaxDbi Q9W385.
    PRIDEi Q9W385.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071348 ; FBpp0071283 ; FBgn0030092 .
    GeneIDi 31845.
    KEGGi dme:Dmel_CG8971.

    Organism-specific databases

    CTDi 2271.
    FlyBasei FBgn0030092. fh.

    Phylogenomic databases

    eggNOGi COG1965.
    GeneTreei ENSGT00390000005811.
    InParanoidi Q9W385.
    OMAi DALCDYF.
    OrthoDBi EOG7HHWVD.
    PhylomeDBi Q9W385.

    Enzyme and pathway databases

    Reactomei REACT_180798. Mitochondrial iron-sulfur cluster biogenesis.
    REACT_180813. Mitochondrial protein import.

    Miscellaneous databases

    GenomeRNAii 31845.
    NextBioi 775622.
    PROi Q9W385.

    Gene expression databases

    Bgeei Q9W385.

    Family and domain databases

    Gene3Di 3.30.920.10. 1 hit.
    InterProi IPR017789. Frataxin.
    IPR002908. Frataxin/CyaY.
    IPR020895. Frataxin_CS.
    [Graphical view ]
    PANTHERi PTHR16821. PTHR16821. 1 hit.
    Pfami PF01491. Frataxin_Cyay. 1 hit.
    [Graphical view ]
    PRINTSi PR00904. FRATAXIN.
    SUPFAMi SSF55387. SSF55387. 1 hit.
    TIGRFAMsi TIGR03421. FeS_CyaY. 1 hit.
    TIGR03422. mito_frataxin. 1 hit.
    PROSITEi PS01344. FRATAXIN_1. 1 hit.
    PS50810. FRATAXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Testis.
    5. "Drosophila frataxin: an iron chaperone during cellular Fe-S cluster bioassembly."
      Kondapalli K.C., Kok N.M., Dancis A., Stemmler T.L.
      Biochemistry 47:6917-6927(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiFRDA_DROME
    AccessioniPrimary (citable) accession number: Q9W385
    Secondary accession number(s): Q9GQQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3