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Protein

Frataxin homolog, mitochondrial

Gene

fh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
OMAiYERVCSD.
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

        10         20         30         40         50
MFAGRLMVRS IVGRACLATM GRWSKPQAHA SQVILPSTPA IAAVAIQCEE
60 70 80 90 100
FTANRRLFSS QIETESTLDG ATYERVCSDT LDALCDYFEE LTENASELQG
110 120 130 140 150
TDVAYSDGVL TVNLGGQHGT YVINRQTPNK QIWLSSPTSG PKRYDFVGTV
160 170 180 190
AAGRWIYKHS GQSLHELLQQ EIPGILKSQS VDFLRLPYCS
Length:190
Mass (Da):20,922
Last modified:May 1, 2000 - v1
Checksum:i8C48332C239F3036
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi58300. 2 interactions.
IntActiQ9W385. 1 interaction.

Proteomic databases

PaxDbiQ9W385.
PRIDEiQ9W385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2271.
FlyBaseiFBgn0030092. fh.

Phylogenomic databases

eggNOGiCOG1965.
GeneTreeiENSGT00390000005811.
InParanoidiQ9W385.
OMAiYERVCSD.
OrthoDBiEOG7HHWVD.
PhylomeDBiQ9W385.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii31845.
NextBioi775622.
PROiQ9W385.

Gene expression databases

BgeeiQ9W385.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.