Frataxin homolog, mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• 4 Fe²⁺

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  • See the description of this molecule in ChEBI.

  + 4 H⁺

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  + O₂

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  = 4 Fe³⁺

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  + 2 H₂O

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.12

    "Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity."
    Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., Isaya G.
    Hum. Mol. Genet. 15:467-479(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-79; ASP-82; GLU-93; ASP-97 AND GLU-103.
  EC:1.16.3.1
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  • See the description of this EC number in ENZYME.
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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.12

    "Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity."
    Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., Isaya G.
    Hum. Mol. Genet. 15:467-479(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-79; ASP-82; GLU-93; ASP-97 AND GLU-103.
  Source: Rhea

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  4

  Fe²⁺

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  zoom

  +

  4

  H⁺

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  +

  O₂

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  =

  4

  Fe³⁺

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  zoom

  +

  2

  H₂O

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  • See the description of this molecule in ChEBI.

  

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• 2 iron, 2 sulfur cluster binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ferric iron binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ferrous iron binding Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia."
    Adamec J., Rusnak F., Owen W.G., Naylor S., Benson L.M., Gacy A.M., Isaya G.
    Am J Hum Genet 67:549-562(2000) [PubMed] [Europe PMC] [Abstract]
  • "Monomeric yeast frataxin is an iron-binding protein."
    Cook J.D., Bencze K.Z., Jankovic A.D., Crater A.K., Busch C.N., Bradley P.B., Stemmler A.J., Spaller M.R., Stemmler T.L.
    Biochemistry 45:7767-7777(2006) [PubMed] [Europe PMC] [Abstract]
• ferroxidase activity Source: SGDInferred from direct assayⁱ
  • "The ferroxidase activity of yeast frataxin."
    Park S., Gakh O., Mooney S.M., Isaya G.
    J Biol Chem 277:38589-38595(2002) [PubMed] [Europe PMC] [Abstract]
  • "Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation."
    Park S., Gakh O., O'Neill H.A., Mangravita A., Nichol H., Ferreira G.C., Isaya G.
    J Biol Chem 278:31340-31351(2003) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.15

    "The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron."
    Karlberg T., Schagerlof U., Gakh O., Park S., Ryde U., Lindahl M., Leath K., Garman E., Isaya G., Al-Karadaghi S.
    Structure 14:1535-1546(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 52-174 ALONE AND IN COMPLEX WITH IRON, ELECTRON MICROSCOPY OF MUTANT ALA-73, FUNCTION, SUBUNIT.
• iron chaperone activity Source: SGDInferred from direct assayⁱ
  • "Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation."
    Park S., Gakh O., O'Neill H.A., Mangravita A., Nichol H., Ferreira G.C., Isaya G.
    J Biol Chem 278:31340-31351(2003) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cellular iron ion homeostasis Source: SGDInferred from direct assayⁱ
  • Ref.4

    "Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin."
    Babcock M., de Silva D., Oaks R., Davis-Kaplan S., Jiralerspong S., Montermini L., Pandolfo M., Kaplan J.
    Science 276:1709-1712(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• glutathione metabolic process Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia."
    Auchere F., Santos R., Planamente S., Lesuisse E., Camadro J.M.
    Hum Mol Genet 17:2790-2802(2008) [PubMed] [Europe PMC] [Abstract]
• heme biosynthetic process Source: UniProtKB-KW
• ion transport Source: UniProtKB-KW
• iron incorporation into metallo-sulfur cluster Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• iron-sulfur cluster assembly Source: SGDInferred from direct assayⁱ
  • Ref.9

    "An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1."
    Gerber J., Muhlenhoff U., Lill R.
    EMBO Rep. 4:906-911(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH ISU1.
• mitochondrial electron transport, succinate to ubiquinone Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Frataxin interacts functionally with mitochondrial electron transport chain proteins."
    Gonzalez-Cabo P., Vazquez-Manrique R.P., Garcia-Gimeno M.A., Sanz P., Palau F.
    Hum. Mol. Genet. 14:2091-2098(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH YHB1; SDH1; SDH2; AIM45 AND CIR1.
• response to iron(II) ion Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.12

    "Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity."
    Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., Isaya G.
    Hum. Mol. Genet. 15:467-479(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-79; ASP-82; GLU-93; ASP-97 AND GLU-103.
• response to oxidative stress Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.12

    "Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity."
    Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., Isaya G.
    Hum. Mol. Genet. 15:467-479(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-79; ASP-82; GLU-93; ASP-97 AND GLU-103.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.15

    "The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron."
    Karlberg T., Schagerlof U., Gakh O., Park S., Ryde U., Lindahl M., Leath K., Garman E., Isaya G., Al-Karadaghi S.
    Structure 14:1535-1546(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 52-174 ALONE AND IN COMPLEX WITH IRON, ELECTRON MICROSCOPY OF MUTANT ALA-73, FUNCTION, SUBUNIT.

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MIKRSLASLV RVSSVMGRRY MIAAAGGERA RFCPAVTNKK NHTVNTFQKR 
        60         70         80         90        100
FVESSTDGQV VPQEVLNLPL EKYHEEADDY LDHLLDSLEE LSEAHPDCIP 
       110        120        130        140        150
DVELSHGVMT LEIPAFGTYV INKQPPNKQI WLASPLSGPN RFDLLNGEWV 
       160        170 
SLRNGTKLTD ILTEEVEKAI SKSQ                             

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome IV
   Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families