D3ZYW7
uniprot
D3ZYW7
canonical
amino_acid_sequence
MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT
uniprot
proteins
ec_number
1.16.3.1
uniprot
proteins
function
FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); 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; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems (By similarity). May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation (PubMed:15247478). May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity). {ECO:0000250|UniProtKB:Q16595, ECO:0000250|UniProtKB:Q9H1K1, ECO:0000269|PubMed:15247478}.; FUNCTION: [Extramitochondrial frataxin]: Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival. {ECO:0000250|UniProtKB:Q16595}.
uniprot
proteins
mass_dalton
23066
uniprot
proteins
post_translational_modification
PTM: [Frataxin mature form]: 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 (frataxin(81-210)) which is the predominant form. The additional forms, frataxin(56-210) and frataxin(78-210), seem to be produced when the normal maturation process is impaired; their physiological relevance is unsure. {ECO:0000250|UniProtKB:Q16595}.
uniprot
proteins
protein_family
Frataxin family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15247478
uniprot
proteins
sequence_length
208
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.; SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}.
uniprot
proteins