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Protein

Frataxin, mitochondrial

Gene

FH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (PubMed:17092311). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe2+ to Fe3+ (PubMed:17092311). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization (PubMed:17092311). Binds to the mitochondrial cysteine desulfurase NIFS1 and increases its activity (PubMed:22511606).2 Publications

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • aerobic respiration Source: TAIR
  • cellular iron ion homeostasis Source: UniProtKB-KW
  • heme biosynthetic process Source: UniProtKB-KW
  • ion transport Source: UniProtKB-KW
  • iron-sulfur cluster assembly Source: InterPro
  • response to hydrogen peroxide Source: TAIR
  • response to oxidative stress Source: TAIR
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

BioCyciARA:AT4G03240-MONOMER.
ReactomeiREACT_325365. Mitochondrial iron-sulfur cluster biogenesis.
REACT_332819. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Frataxin, mitochondrial (EC:1.16.3.1)
Short name:
Fxn
Gene namesi
Name:FH
Ordered Locus Names:At4g03240
ORF Names:F4C21.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G03240.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 187Frataxin, mitochondrialPRO_0000193926
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PaxDbiQ9ZR07.
PRIDEiQ9ZR07.

Interactioni

Subunit structurei

Monomer. Oligomer (By similarity). Interacts with NIFS1 (PubMed:22511606).By similarity1 Publication

Protein-protein interaction databases

BioGridi13304. 1 interaction.
STRINGi3702.AT4G03240.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ZR07.
SMRiQ9ZR07. Positions 76-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the frataxin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1965.
HOGENOMiHOG000190729.
InParanoidiQ9ZR07.
KOiK19054.
OMAiANATIHD.
PhylomeDBiQ9ZR07.

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]
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.

Q9ZR07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATASRFLLR KLPRFLKLSP TLLRSNGVRV SSNLIQDSIE PLDSFWRIGS
60 70 80 90 100
RIRHDSLTTR SFSSQGPASV DYSSVLQEEE FHKLANFTIN HLLEKIEDYG
110 120 130 140 150
DNVQIDGFDI DYGNEVLTLK LGSLGTYVLN KQTPNRQIWM SSPVSGPSRF
160 170 180
DWDRDANAWI YRRTEAKLHK LLEEELENLC GEPIQLS
Length:187
Mass (Da):21,430
Last modified:December 6, 2005 - v2
Checksum:iFAFA6A8AF7FD7534
GO

Sequence cautioni

The sequence AAD14452.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB77809.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB85041.
RefSeqiNP_192233.2. NM_116562.3.
UniGeneiAt.50317.

Genome annotation databases

EnsemblPlantsiAT4G03240.1; AT4G03240.1; AT4G03240.
GeneIDi828013.
KEGGiath:AT4G03240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB85041.
RefSeqiNP_192233.2. NM_116562.3.
UniGeneiAt.50317.

3D structure databases

ProteinModelPortaliQ9ZR07.
SMRiQ9ZR07. Positions 76-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13304. 1 interaction.
STRINGi3702.AT4G03240.1.

Proteomic databases

PaxDbiQ9ZR07.
PRIDEiQ9ZR07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G03240.1; AT4G03240.1; AT4G03240.
GeneIDi828013.
KEGGiath:AT4G03240.

Organism-specific databases

TAIRiAT4G03240.

Phylogenomic databases

eggNOGiCOG1965.
HOGENOMiHOG000190729.
InParanoidiQ9ZR07.
KOiK19054.
OMAiANATIHD.
PhylomeDBiQ9ZR07.

Enzyme and pathway databases

BioCyciARA:AT4G03240-MONOMER.
ReactomeiREACT_325365. Mitochondrial iron-sulfur cluster biogenesis.
REACT_332819. Mitochondrial protein import.

Miscellaneous databases

PROiQ9ZR07.

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]
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. "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.
  7. "Structural and functional studies of the mitochondrial cysteine desulfurase from Arabidopsis thaliana."
    Turowski V.R., Busi M.V., Gomez-Casati D.F.
    Mol. Plant 5:1001-1010(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NIFS1.

Entry informationi

Entry nameiFRDA_ARATH
AccessioniPrimary (citable) accession number: Q9ZR07
Secondary accession number(s): Q6GKV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 6, 2005
Last modified: July 22, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.