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D3ZYW7

- FRDA_RAT

UniProt

D3ZYW7 - FRDA_RAT

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Protein

Frataxin, mitochondrial

Gene

Fxn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. enzyme binding Source: RGD
  2. ferric iron binding Source: InterPro
  3. ferroxidase activity Source: UniProtKB-EC
  4. metallochaperone activity Source: RGD

GO - Biological processi

  1. cellular iron ion homeostasis Source: RGD
  2. heme biosynthetic process Source: UniProtKB-KW
  3. ion transport Source: UniProtKB-KW
  4. iron-sulfur cluster assembly Source: InterPro
  5. positive regulation of axon extension Source: RGD
  6. response to drug Source: RGD
  7. response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Heme biosynthesis, Ion transport, Iron storage, Iron transport, Transport

Keywords - Ligandi

Iron

Names & Taxonomyi

Protein namesi
Recommended name:
Frataxin, mitochondrial (EC:1.16.3.1)
Short name:
Fxn
Cleaved into the following 2 chains:
Gene namesi
Name:Fxn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1565754. Fxn.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040MitochondrionBy similarityAdd
BLAST
Chaini41 – 208168Frataxin intermediate formPRO_0000399465Add
BLAST
Chaini79 – 208130Frataxin mature formBy similarityPRO_0000399391Add
BLAST

Post-translational modificationi

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).By similarity

Proteomic databases

PRIDEiD3ZYW7.

Interactioni

Subunit structurei

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.By similarity1 Publication

Family & Domainsi

Sequence similaritiesi

Belongs to the frataxin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiD3ZYW7.
PhylomeDBiD3ZYW7.
TreeFamiTF318958.

Family and domain databases

Gene3Di3.30.920.10. 1 hit.
InterProiIPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
[Graphical view]
PANTHERiPTHR16821. PTHR16821. 1 hit.
PfamiPF01491. Frataxin_Cyay. 1 hit.
[Graphical view]
PRINTSiPR00904. FRATAXIN.
SUPFAMiSSF55387. SSF55387. 1 hit.
TIGRFAMsiTIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEiPS50810. FRATAXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D3ZYW7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWTFGRRAAA GLLPRTASRA SAWVRNPRGR ERIGTCGRRG LHVTANADAI
60 70 80 90 100
RHSHLNLHYL GQILNIKKQS VCVVHLRNSG TLGNPSSLDE TAYERLAEET
110 120 130 140 150
LDALAEFFED LADKPYTLKD YDVSFGDGVL TIKLGGDLGT YVINKQTPLL
160 170 180 190 200
YLWFSGPCSG PKRYDWTGKN WVYSHDGVSL HELLARELTE ALNTKLDLSS

LAYSGKGT
Length:208
Mass (Da):23,066
Last modified:April 20, 2010 - v1
Checksum:i401B8210F5CEDD35
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03005338 Genomic DNA. No translation available.
AABR03006217 Genomic DNA. No translation available.
AABR03009513 Genomic DNA. No translation available.
UniGeneiRn.13133.

Genome annotation databases

UCSCiRGD:1565754. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03005338 Genomic DNA. No translation available.
AABR03006217 Genomic DNA. No translation available.
AABR03009513 Genomic DNA. No translation available.
UniGenei Rn.13133.

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi D3ZYW7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1565754. rat.

Organism-specific databases

RGDi 1565754. Fxn.

Phylogenomic databases

InParanoidi D3ZYW7.
PhylomeDBi D3ZYW7.
TreeFami TF318958.

Family and domain databases

Gene3Di 3.30.920.10. 1 hit.
InterProi IPR017789. Frataxin.
IPR002908. Frataxin/CyaY.
[Graphical view ]
PANTHERi PTHR16821. PTHR16821. 1 hit.
Pfami PF01491. Frataxin_Cyay. 1 hit.
[Graphical view ]
PRINTSi PR00904. FRATAXIN.
SUPFAMi SSF55387. SSF55387. 1 hit.
TIGRFAMsi TIGR03421. FeS_CyaY. 1 hit.
TIGR03422. mito_frataxin. 1 hit.
PROSITEi PS50810. FRATAXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFRDA_RAT
AccessioniPrimary (citable) accession number: D3ZYW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 20, 2010
Last modified: November 26, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3