O35943 (FRDA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 98. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||207 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.6
4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
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. Interacts with ACO2; the interaction is dependent on citrate By similarity. Ref.2
Heart, liver, skeletal muscle, kidney, spleen and thymus. Weakly expressed in the brain and lung. Ref.1
Expression in the ventricular zone which corresponds to dividing neuronal precursors begins at day 12.5, increases during embryonic development and persists at postnatal day 7 (P7) in the ependymal layer, which is the remenant of the ventricular zone. Weak expression seen in the spinal cord and medulla oblongata, starting at embryonic day 14.5 (E14.5) and expression also observed in dorsal root ganglia, starting at E14.5. At P14, expression in the dorsal root ganglia is restricted to the cortical region where the sensory neuron cell bodies are located. In non-neural tissues strong expression seen in the developing liver from E10.5. Expression detected in the heart and in the cortex of the developing kidney at E12.5 and later. Very high expression observed in the brown adipose tissue. Expression seen in small islands around the neck and back at E14.5, then in large masses at E16.5 and E18.5 and at P14 is absent in brown adipose tissue. Expression also seen in the thymus and developing gut at E14.5 and until postnatal life. At P14, expression in thymus is restricted to the proliferating cells in the cortical zone and is also prominent in the spleen. Found in the lung at E14.5. Ref.1
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.
Loss of cell division and lethal in fibroblasts. Ref.5
Belongs to the frataxin family.
Sequence annotation (Features)
|||"Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin."|
Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O., Koenig M.
Nat. Genet. 16:345-351(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
|||"Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia."|
Cavadini P., O'Neill H.A., Benada O., Isaya G.
Hum. Mol. Genet. 11:217-227(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
|||"Frataxin is essential for extramitochondrial Fe-S cluster proteins in mammalian tissues."|
Martelli A., Wattenhofer-Donze M., Schmucker S., Bouvet S., Reutenauer L., Puccio H.
Hum. Mol. Genet. 16:2651-2658(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
|||"The in vivo mitochondrial two-step maturation of human frataxin."|
Schmucker S., Argentini M., Carelle-Calmels N., Martelli A., Puccio H.
Hum. Mol. Genet. 17:3521-3531(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
|||"The first cellular models based on frataxin missense mutations that reproduce spontaneously the defects associated with Friedreich ataxia."|
Calmels N., Schmucker S., Wattenhofer-Donze M., Martelli A., Vaucamps N., Reutenauer L., Messaddeq N., Bouton C., Koenig M., Puccio H.
PLoS ONE 4:E6379-E6379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
|||"Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant."|
Huang M.L., Becker E.M., Whitnall M., Rahmanto Y.S., Ponka P., Richardson D.R.
Proc. Natl. Acad. Sci. U.S.A. 106:16381-16386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|+||Additional computationally mapped references.|
|U95736 mRNA. Translation: AAB67778.1.|
|RefSeq||NP_032070.1. NM_008044.2. |
3D structure databases
|SMR||O35943. Positions 86-205. |
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000081333; ENSMUSP00000080081; ENSMUSG00000059363. |
|MGI||MGI:1096879. Fxn. |
Gene expression databases
|GermOnline||ENSMUSG00000059363. Mus musculus. |
Family and domain databases
|Gene3D||3.30.920.10. 1 hit. |
|InterPro||IPR017789. Frataxin. |
|PANTHER||PTHR16821. PTHR16821. 1 hit. |
|Pfam||PF01491. Frataxin_Cyay. 1 hit. |
|PRINTS||PR00904. FRATAXIN. |
|SUPFAM||SSF55387. Frataxin_like. 1 hit. |
|TIGRFAMs||TIGR03421. FeS_CyaY. 1 hit. |
TIGR03422. mito_frataxin. 1 hit.
|PROSITE||PS01344. FRATAXIN_1. 1 hit. |
PS50810. FRATAXIN_2. 1 hit.
|Accession||Primary (citable) accession number: O35943|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|