FXN

Frataxin, mitochondrial

210 amino acids

Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) 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 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. Modulates the RNA-binding activity of ACO1.

Belongs to the frataxin family.

23.135 kDa

MWTLGRRAVAGLLASPSPAQAQTLTRVPRPAELAPLCGRRGLRTDIDATCTPRRASSNQRGLNQIWNVKKQSVYLMNLRKSGTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA

FXN

Frataxin, mitochondrial

210 amino acids

Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) 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 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. Modulates the RNA-binding activity of ACO1 (By similarity).

Belongs to the frataxin family.

23.133 kDa

MWTFGRRAVAGLLASPSPAQAQTLTRAPRLAELAQLCSRRGLRTGINATRTTHHTSSNLRGLNQIRNVKRQSVYLMNLRKSGTLGHPGSLDDTTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDRTGKNWVYSHDGVSLHELLGAELTKALKTKLDLSSLAYSGKDA

Fxn

Frataxin, mitochondrial

208 amino acids

Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) 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 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. Modulates the RNA-binding activity of ACO1 (By similarity).

Belongs to the frataxin family.

23.066 kDa

MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT

Fxn

Frataxin, mitochondrial

207 amino acids

Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) 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 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. Modulates the RNA-binding activity of ACO1 (By similarity).

Belongs to the frataxin family.

22.924 kDa

MWAFGGRAAVGLLPRTASRASAWVGNPRWREPIVTCGRRGLHVTVNAGATRHAHLNLHYLQILNIKKQSVCVVHLRNLGTLDNPSSLDETAYERLAEETLDSLAEFFEDLADKPYTLEDYDVSFGDGVLTIKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLARELTKALNTKLDLSSLAYSGKGT

fxn

Frataxin, mitochondrial

193 amino acids

Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) 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 Fe(2+) to Fe(3+). May be able to store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization (By similarity).

Belongs to the frataxin family.

22.206 kDa

MIFNFLNKASNKTHTKLLLFSSIRNRILINNISSTSKWSSINNNNKQSSVSKTNIFIITTHNKQQQQLSKSFSTINNNTKPISDVNLFHDIVDEEFELFVDRLEILSEANTCEGFEVEGNDGVLTIIVGNKGTYVINKQTPNRQIWWSSPLSGPKRFDYDSVEKRWVDNRDGTPLRQLLNSEINTLCKYDMEI