Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZR07 (FRDA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Frataxin, mitochondrial

Short name=Fxn
EC=1.16.3.1
Gene names
Name:FH
Ordered Locus Names:At4g03240
ORF Names:F4C21.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 187Frataxin, mitochondrialPRO_0000193926

Sequences

Sequence LengthMass (Da)Tools
Q9ZR07 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: FAFA6A8AF7FD7534

FASTA18721,430
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRB85041.
RefSeqNP_192233.2. NM_116562.3.
UniGeneAt.50317.

3D structure databases

ProteinModelPortalQ9ZR07.
SMRQ9ZR07. Positions 76-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13304. 1 interaction.

Proteomic databases

PaxDbQ9ZR07.
PRIDEQ9ZR07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G03240.1; AT4G03240.1; AT4G03240.
GeneID828013.
KEGGath:AT4G03240.

Organism-specific databases

TAIRAT4G03240.

Phylogenomic databases

eggNOGCOG1965.
HOGENOMHOG000190729.
InParanoidQ9ZR07.
OMAAWIYRRT.
PhylomeDBQ9ZR07.

Enzyme and pathway databases

BioCycARA:AT4G03240-MONOMER.

Gene expression databases

GenevestigatorQ9ZR07.

Family and domain databases

Gene3D3.30.920.10. 1 hit.
InterProIPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
IPR020895. Frataxin_CS.
[Graphical view]
PANTHERPTHR16821. PTHR16821. 1 hit.
PfamPF01491. Frataxin_Cyay. 1 hit.
[Graphical view]
SUPFAMSSF55387. SSF55387. 1 hit.
TIGRFAMsTIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEPS01344. FRATAXIN_1. 1 hit.
PS50810. FRATAXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9ZR07.

Entry information

Entry nameFRDA_ARATH
AccessionPrimary (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 14, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names