Q9ZR07 (FRDA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Frataxin, mitochondrial
Short name=Fxn
EC=1.16.3.1

Gene names

Name:	FH
Ordered Locus Names:	At4g03240
ORF Names:	F4C21.17

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	187 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.6
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	Monomer. Oligomer By similarity.
Subcellular location	Mitochondrion Ref.6.
Sequence similarities	Belongs to the frataxin family.
Sequence caution	The sequence AAD14452.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB77809.1 differs from that shown. Reason: Erroneous gene model prediction.

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	aerobic respiration Inferred from mutant phenotype Ref.1. Source: TAIR 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 response to hydrogen peroxide Inferred from mutant phenotype Ref.1. Source: TAIR
Cellular_component	mitochondrion Inferred from sequence or structural similarity Ref.1. Source: TAIR
Molecular_function	ferric iron binding Inferred from electronic annotation. Source: InterPro ferroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 187		Frataxin, mitochondrial		PRO_0000193926

Sequences

	Sequence		Length	Mass (Da)
	Q9ZR07 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: FAFA6A8AF7FD7534	FASTA	187	21,430
	10 20 30 40 50 60 MATASRFLLR KLPRFLKLSP TLLRSNGVRV SSNLIQDSIE PLDSFWRIGS RIRHDSLTTR 70 80 90 100 110 120 SFSSQGPASV DYSSVLQEEE FHKLANFTIN HLLEKIEDYG DNVQIDGFDI DYGNEVLTLK 130 140 150 160 170 180 LGSLGTYVLN KQTPNRQIWM SSPVSGPSRF DWDRDANAWI YRRTEAKLHK LLEEELENLC GEPIQLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana." Busi M.V., Zabaleta E.J., Araya A., Gomez-Casati D.F. FEBS Lett. 576:141-144(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress." Busi M.V., Maliandi M.V., Valdez H., Clemente M., Zabaleta E.J., Araya A., Gomez-Casati D.F. Plant J. 48:873-882(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY649366 mRNA. Translation: AAU11485.1. AC005275 Genomic DNA. Translation: AAD14452.1. Sequence problems. AL161496 Genomic DNA. Translation: CAB77809.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE82296.1. BT014964 mRNA. Translation: AAT47815.1. AK176448 mRNA. Translation: BAD44211.1. AK176831 mRNA. Translation: BAD44594.1.
IPI	IPI00527007.
PIR	B85041.
RefSeq	NP_192233.2. NM_116562.3.
UniGene	At.50317.
3D structure databases
ProteinModelPortal	Q9ZR07.
SMR	Q9ZR07. Positions 76-187.
ModBase	Search...
Proteomic databases
PaxDb	Q9ZR07.
PRIDE	Q9ZR07.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G03240.1; AT4G03240.1; AT4G03240.
GeneID	828013.
KEGG	ath:AT4G03240.
Organism-specific databases
TAIR	At4g03240.
Phylogenomic databases
eggNOG	COG1965.
HOGENOM	HOG000190729.
InParanoid	Q9ZR07.
OMA	QIDGFDI.
PhylomeDB	Q9ZR07.
ProtClustDB	CLSN2918569.
Gene expression databases
Genevestigator	Q9ZR07.
GermOnline	AT4G03240. Arabidopsis thaliana.
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]
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...

Entry information

Entry name

FRDA_ARATH

Accession

Primary (citable) accession number: Q9ZR07
Secondary accession number(s): Q6GKV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program