Q9W385 (FRDA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Frataxin homolog, mitochondrial
Short name=Dfh
EC=1.16.3.1

Gene names

Name:	fh
ORF Names:	CG8971

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. Ref.5
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	Monomer (probable predominant form). Oligomer By similarity.
Subcellular location	Mitochondrion By similarity.
Developmental stage	Expressed throughout development, levels are high during embryogenesis but low in following stages. Ref.1
Sequence similarities	Belongs to the frataxin family.

Ontologies

Keywords
Biological process	Heme biosynthesis Ion transport Iron storage Iron transport Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon transport of mitochondrion Inferred from direct assay PubMed 20739558. Source: FlyBase cellular iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW iron-sulfur cluster assembly Inferred from electronic annotation. Source: InterPro regulation of mitochondrial membrane potential Inferred from direct assay PubMed 20739558. Source: FlyBase response to hydrogen peroxide Inferred from mutant phenotype PubMed 18184803. Source: FlyBase
Cellular_component	mitochondrion Inferred from mutant phenotype PubMed 17167074. Source: FlyBase
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC iron chaperone activity Inferred from direct assay Ref.5. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 190		Frataxin homolog, mitochondrial		PRO_0000010133

Sequences

	Sequence		Length	Mass (Da)
	Q9W385 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8C48332C239F3036	FASTA	190	20,922
	10 20 30 40 50 60 MFAGRLMVRS IVGRACLATM GRWSKPQAHA SQVILPSTPA IAAVAIQCEE FTANRRLFSS 70 80 90 100 110 120 QIETESTLDG ATYERVCSDT LDALCDYFEE LTENASELQG TDVAYSDGVL TVNLGGQHGT 130 140 150 160 170 180 YVINRQTPNK QIWLSSPTSG PKRYDFVGTV AAGRWIYKHS GQSLHELLQQ EIPGILKSQS 190 VDFLRLPYCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"dfh is a Drosophila homolog of the Friedreich's ataxia disease gene." Canizares-Sales J., Blanca-Postigo J.M., Navarro J.A., Monros E., Palau-Martinez F., Molto-Ruiz M.D. Gene 256:35-42(2000) [PubMed] [Europe PMC] [Abstract] 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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_511094.1. NM_078539.3.
UniGene	Dm.2903.
3D structure databases
ProteinModelPortal	Q9W385.
SMR	Q9W385. Positions 67-188.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9W385. 1 interaction.
Proteomic databases
PaxDb	Q9W385.
PRIDE	Q9W385.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071348; FBpp0071283; FBgn0030092.
GeneID	31845.
KEGG	dme:Dmel_CG8971.
Organism-specific databases
CTD	2271.
FlyBase	FBgn0030092. fh.
Phylogenomic databases
eggNOG	COG1965.
GeneTree	ENSGT00390000005811.
InParanoid	Q9W385.
OMA	DALCDYF.
OrthoDB	EOG4FN316.
PhylomeDB	Q9W385.
Gene expression databases
Bgee	Q9W385.
GermOnline	CG8971. Drosophila melanogaster.
Family and domain databases
Gene3D	3.30.920.10. 1 hit.
InterPro	IPR017789. Frataxin. IPR002908. Frataxin/CyaY. IPR020895. Frataxin_CS. [Graphical view]
PANTHER	PTHR16821. PTHR16821. 1 hit.
Pfam	PF01491. Frataxin_Cyay. 1 hit. [Graphical view]
PRINTS	PR00904. FRATAXIN.
SUPFAM	SSF55387. Frataxin_like. 1 hit.
TIGRFAMs	TIGR03421. FeS_CyaY. 1 hit. TIGR03422. mito_frataxin. 1 hit.
PROSITE	PS01344. FRATAXIN_1. 1 hit. PS50810. FRATAXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	31845.
NextBio	775622.

Entry information

Entry name

FRDA_DROME

Accession

Primary (citable) accession number: Q9W385
Secondary accession number(s): Q9GQQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project