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D3ZYW7 (FRDA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Cleaved into the following 2 chains:

  1. Frataxin intermediate form
  2. Frataxin mature form
Gene names
Name:Fxn
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes the biosynthesis of heme and 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+; the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activity of ACO1 By similarity. Ref.2

Catalytic activity

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

Subunit structure

Monomer (probable predominant form). Oligomer. Interacts with LYRM4 AND HSPA9. Interacts with ACO1. Interacts with ISCU. Interacts with FECH; one iron-bound FXN monomer seems to interact with a FECH homodimer. Interacts with SDHA and SDHB By similarity. Interacts with ACO2; the interaction is dependent on citrate. Ref.2

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity.

Post-translational modification

Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form By similarity.

Sequence similarities

Belongs to the frataxin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 208168Frataxin intermediate form
PRO_0000399465
Chain79 – 208130Frataxin mature form By similarity
PRO_0000399391

Sequences

Sequence LengthMass (Da)Tools
D3ZYW7 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: 401B8210F5CEDD35

FASTA20823,066
        10         20         30         40         50         60 
MWTFGRRAAA GLLPRTASRA SAWVRNPRGR ERIGTCGRRG LHVTANADAI RHSHLNLHYL 

        70         80         90        100        110        120 
GQILNIKKQS VCVVHLRNSG TLGNPSSLDE TAYERLAEET LDALAEFFED LADKPYTLKD 

       130        140        150        160        170        180 
YDVSFGDGVL TIKLGGDLGT YVINKQTPLL YLWFSGPCSG PKRYDWTGKN WVYSHDGVSL 

       190        200 
HELLARELTE ALNTKLDLSS LAYSGKGT 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity."
Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., Szweda L.I.
Science 305:242-245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS IRON CHAPERONE, INTERACTION WITH ACO2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03005338 Genomic DNA. No translation available.
AABR03006217 Genomic DNA. No translation available.
AABR03009513 Genomic DNA. No translation available.
UniGeneRn.13133.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDED3ZYW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1565754. rat.

Organism-specific databases

RGD1565754. Fxn.

Phylogenomic databases

PhylomeDBD3ZYW7.
TreeFamTF318958.

Family and domain databases

Gene3D3.30.920.10. 1 hit.
InterProIPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
[Graphical view]
PANTHERPTHR16821. PTHR16821. 1 hit.
PfamPF01491. Frataxin_Cyay. 1 hit.
[Graphical view]
PRINTSPR00904. FRATAXIN.
SUPFAMSSF55387. SSF55387. 1 hit.
TIGRFAMsTIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEPS50810. FRATAXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRDA_RAT
AccessionPrimary (citable) accession number: D3ZYW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families