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Frataxin, mitochondrial (EC 1.16.3.1) (Friedreich ataxia protein) (Fxn) [Cleaved into: Frataxin intermediate form (i-FXN); Frataxin(56-210) (m56-FXN); Frataxin(78-210) (d-FXN) (m78-FXN); Frataxin mature form (Frataxin(81-210)) (m81-FXN)]

 FRDA_HUMAN              Reviewed;         210 AA.
Q16595; A8MXJ6; C9JJ89; O15545; O95656; Q15294; Q5VZ01;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
25-OCT-2017, entry version 183.
RecName: Full=Frataxin, mitochondrial;
EC=1.16.3.1;
AltName: Full=Friedreich ataxia protein;
Short=Fxn;
Contains:
RecName: Full=Frataxin intermediate form;
Short=i-FXN;
Contains:
RecName: Full=Frataxin(56-210);
AltName: Full=m56-FXN;
Contains:
RecName: Full=Frataxin(78-210);
AltName: Full=d-FXN;
AltName: Full=m78-FXN;
Contains:
RecName: Full=Frataxin mature form;
AltName: Full=Frataxin(81-210);
AltName: Full=m81-FXN;
Flags: Precursor;
Name=FXN; Synonyms=FRDA, X25;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2),
ALTERNATIVE SPLICING, AND VARIANT PHE-154.
PubMed=8596916; DOI=10.1126/science.271.5254.1423;
Campuzano V., Montermini L., Molto M.D., Pianese L., Cossee M.,
Cavalcanti F., Monros E., Rodius F., Duclos F., Monticelli A.,
Zara F., Canizares J., Koutnikova H., Bidichandani S., Gellera C.,
Brice A., Trouillas P., de Michele G., Filla A., de Frutos R.,
Palau F., Patel P.I., di Donato S., Mandel J.-L., Cocozza S.,
Koenig M., Pandolfo M.;
"Friedreich's ataxia: autosomal recessive disease caused by an
intronic GAA triplet repeat expansion.";
Science 271:1423-1427(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 81-90, PROTEOLYTIC PROCESSING, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 39-ARG-ARG-40; 53-ARG-ARG-54;
78-LEU-ARG-79 AND 79-ARG-LYS-80.
PubMed=18725397; DOI=10.1093/hmg/ddn244;
Schmucker S., Argentini M., Carelle-Calmels N., Martelli A.,
Puccio H.;
"The in vivo mitochondrial two-step maturation of human frataxin.";
Hum. Mol. Genet. 17:3521-3531(2008).
[5]
PROTEIN SEQUENCE OF 81-86, PROTEOLYTIC PROCESSING, MUTAGENESIS OF
53-ARG-ARG-54 AND 79-ARG-LYS-80, AND TISSUE SPECIFICITY.
PubMed=17468497; DOI=10.1093/hmg/ddm102;
Condo I., Ventura N., Malisan F., Rufini A., Tomassini B., Testi R.;
"In vivo maturation of human frataxin.";
Hum. Mol. Genet. 16:1534-1540(2007).
[6]
PROTEIN SEQUENCE OF 81-86, FUNCTION, INTERACTION WITH ACO1, AND
SUBCELLULAR LOCATION.
PubMed=20053667; DOI=10.1093/hmg/ddp592;
Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R.;
"Molecular control of the cytosolic aconitase/IRP1 switch by
extramitochondrial frataxin.";
Hum. Mol. Genet. 19:1221-1229(2010).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-128, AND VARIANT FRDA TYR-122.
Kostrzewa M.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-128, AND VARIANT FRDA TYR-122.
Doudney J.D., Pook M.A., Al-Mahdawi S., Carvajal J.J., Hillerman R.,
Chamberlain S.;
"A novel splice site mutation (384+1G-A) in the Friedreich's ataxia
gene.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-210.
Laccone F., Schloesser M.;
"Correct sequence in exon 5a of x25: human frataxin (FRDA),
F175(TTC)-->Y175(TAC) and W202(TGG)-->S202(TCC).";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[10]
SUBCELLULAR LOCATION.
PubMed=9302253; DOI=10.1093/hmg/6.11.1771;
Campuzano V., Montermini L., Lutz Y., Cova L., Hindelang C.,
Jiralerspong S., Trottier Y., Kish S.J., Faucheux B., Trouillas P.,
Authier F.J., Duerr A., Mandel J.-L., Vescovi A., Pandolfo M.,
Koenig M.;
"Frataxin is reduced in Friedreich ataxia patients and is associated
with mitochondrial membranes.";
Hum. Mol. Genet. 6:1771-1780(1997).
[11]
SUBCELLULAR LOCATION.
PubMed=9241270; DOI=10.1038/ng0897-345;
Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O.,
Koenig M.;
"Studies of human, mouse and yeast homologues indicate a mitochondrial
function for frataxin.";
Nat. Genet. 16:345-351(1997).
[12]
PROTEOLYTIC PROCESSING.
PubMed=10545606; DOI=10.1093/hmg/8.12.2255;
Gordon D.M., Shi Q., Dancis A., Pain D.;
"Maturation of frataxin within mammalian and yeast mitochondria: one-
step processing by matrix processing peptidase.";
Hum. Mol. Genet. 8:2255-2262(1999).
[13]
PROTEOLYTIC PROCESSING.
PubMed=10428860; DOI=10.1074/jbc.274.32.22763;
Branda S.S., Cavadini P., Adamec J., Kalousek F., Taroni F., Isaya G.;
"Yeast and human frataxin are processed to mature form in two
sequential steps by the mitochondrial processing peptidase.";
J. Biol. Chem. 274:22763-22769(1999).
[14]
PROTEOLYTIC PROCESSING.
PubMed=11020385; DOI=10.1074/jbc.M006539200;
Cavadini P., Adamec J., Taroni F., Gakh O., Isaya G.;
"Two-step processing of human frataxin by mitochondrial processing
peptidase. Precursor and intermediate forms are cleaved at different
rates.";
J. Biol. Chem. 275:41469-41475(2000).
[15]
POSSIBLE FUNCTION IN IRON STORAGE, AND SUBUNIT.
PubMed=11823441; DOI=10.1093/hmg/11.3.217;
Cavadini P., O'Neill H.A., Benada O., Isaya G.;
"Assembly and iron-binding properties of human frataxin, the protein
deficient in Friedreich ataxia.";
Hum. Mol. Genet. 11:217-227(2002).
[16]
POSSIBLE FUNCTION IN IRON STORAGE, AND SUBUNIT.
PubMed=12755598; DOI=10.1021/bi027021l;
Nichol H., Gakh O., O'Neill H.A., Pickering I.J., Isaya G.,
George G.N.;
"Structure of frataxin iron cores: an X-ray absorption spectroscopic
study.";
Biochemistry 42:5971-5976(2003).
[17]
FUNCTION IN IRON-SULFUR CLUSTER BIOSYNTHESIS, AND INTERACTION WITH
ISCU.
PubMed=12785837; DOI=10.1021/ja027967i;
Yoon T., Cowan J.A.;
"Iron-sulfur cluster biosynthesis. Characterization of frataxin as an
iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins.";
J. Am. Chem. Soc. 125:6078-6084(2003).
[18]
POSSIBLE FUNCTION IN HEME BIOSYNTHESIS, AND INTERACTION WITH FECH.
PubMed=15123683; DOI=10.1074/jbc.C400107200;
Yoon T., Cowan J.A.;
"Frataxin-mediated iron delivery to ferrochelatase in the final step
of heme biosynthesis.";
J. Biol. Chem. 279:25943-25946(2004).
[19]
FUNCTION.
PubMed=15247478; DOI=10.1126/science.1098991;
Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G.,
Szweda L.I.;
"Frataxin acts as an iron chaperone protein to modulate mitochondrial
aconitase activity.";
Science 305:242-245(2004).
[20]
FUNCTION IN OXIDATIVE STRESS, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=15641778; DOI=10.1021/bi048459j;
O'Neill H.A., Gakh O., Park S., Cui J., Mooney S.M., Sampson M.,
Ferreira G.C., Isaya G.;
"Assembly of human frataxin is a mechanism for detoxifying redox-
active iron.";
Biochemistry 44:537-545(2005).
[21]
INTERACTION WITH SDHA AND SDHB.
PubMed=15961414; DOI=10.1093/hmg/ddi214;
Gonzalez-Cabo P., Vazquez-Manrique R.P., Garcia-Gimeno M.A., Sanz P.,
Palau F.;
"Frataxin interacts functionally with mitochondrial electron transport
chain proteins.";
Hum. Mol. Genet. 14:2091-2098(2005).
[22]
FUNCTION, AND INVOLVEMENT IN HEME BIOSYNTHESIS.
PubMed=16239244; DOI=10.1093/hmg/ddi393;
Schoenfeld R.A., Napoli E., Wong A., Zhan S., Reutenauer L., Morin D.,
Buckpitt A.R., Taroni F., Lonnerdal B., Ristow M., Puccio H.,
Cortopassi G.A.;
"Frataxin deficiency alters heme pathway transcripts and decreases
mitochondrial heme metabolites in mammalian cells.";
Hum. Mol. Genet. 14:3787-3799(2005).
[23]
INTERACTION WITH ISCU, AND SUBCELLULAR LOCATION.
PubMed=16091420; DOI=10.1242/jcs.02516;
Acquaviva F., De Biase I., Nezi L., Ruggiero G., Tatangelo F.,
Pisano C., Monticelli A., Garbi C., Acquaviva A.M., Cocozza S.;
"Extra-mitochondrial localisation of frataxin and its association with
IscU1 during enterocyte-like differentiation of the human colon
adenocarcinoma cell line Caco-2.";
J. Cell Sci. 118:3917-3924(2005).
[24]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15581888; DOI=10.1016/j.jmb.2004.10.074;
O'Neill H.A., Gakh O., Isaya G.;
"Supramolecular assemblies of human frataxin are formed via subunit-
subunit interactions mediated by a non-conserved amino-terminal
region.";
J. Mol. Biol. 345:433-439(2005).
[25]
FUNCTION IN CELL SURVIVAL, AND SUBCELLULAR LOCATION.
PubMed=16608849; DOI=10.1074/jbc.M511960200;
Condo I., Ventura N., Malisan F., Tomassini B., Testi R.;
"A pool of extramitochondrial frataxin that promotes cell survival.";
J. Biol. Chem. 281:16750-16756(2006).
[26]
INTERACTION WITH LYRM4 AND HSPA9, AND CHARACTERIZATION OF VARIANTS
PHE-154 AND ARG-155.
PubMed=17331979; DOI=10.1093/hmg/ddm038;
Shan Y., Napoli E., Cortopassi G.;
"Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex
and multiple mitochondrial chaperones.";
Hum. Mol. Genet. 16:929-941(2007).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 88-210.
PubMed=10900192; DOI=10.1074/jbc.C000407200;
Dhe-Paganon S., Shigeta R., Chi Y.-I., Ristow M., Shoelson S.E.;
"Crystal structure of human frataxin.";
J. Biol. Chem. 275:30753-30756(2000).
[30]
STRUCTURE BY NMR OF 91-210.
PubMed=10903947; DOI=10.1016/S0969-2126(00)00158-1;
Musco G., Stier G., Kolmerer B., Adinolfi S., Martin S., Frenkiel T.,
Gibson T., Pastore A.;
"Towards a structural understanding of Friedreich's ataxia: the
solution structure of frataxin.";
Structure 8:695-707(2000).
[31]
VARIANTS FRDA VAL-130 AND PHE-154.
PubMed=9150176;
Bidichandani S.I., Ashizawa T., Patel P.I.;
"Atypical Friedreich ataxia caused by compound heterozygosity for a
novel missense mutation and the GAA triplet-repeat expansion.";
Am. J. Hum. Genet. 60:1251-1256(1997).
[32]
VARIANT FRDA SER-106.
PubMed=9779809;
DOI=10.1002/(SICI)1096-8628(19981012)79:5<396::AID-AJMG13>3.0.CO;2-M;
Bartolo C., Mendell J.R., Prior T.W.;
"Identification of a missense mutation in a Friedreich's ataxia
patient: implications for diagnosis and carrier studies.";
Am. J. Med. Genet. 79:396-399(1998).
[33]
VARIANTS FRDA VAL-130; CYS-165 AND PHE-182.
PubMed=10732799; DOI=10.1007/s100480050037;
Forrest S.M., Knight M., Delatycki M.B., Paris D., Williamson R.,
King J., Yeung L., Nassif N., Nicholson G.A.;
"The correlation of clinical phenotype in Friedreich ataxia with the
site of point mutations in the FRDA gene.";
Neurogenetics 1:253-257(1998).
[34]
VARIANTS FRDA TYR-122 AND VAL-130.
PubMed=9989622;
DOI=10.1002/1531-8249(199902)45:2<200::AID-ANA10>3.0.CO;2-U;
Cossee M., Duerr A., Schmitt M., Dahl N., Trouillas P., Allinson P.,
Kostrzewa M., Nivelon-Chevallier A., Gustavson K.-H.,
Kohlschuetter A., Mueller U., Mandel J.-L., Brice A., Koenig M.,
Cavalcanti F., Tammaro A., de Michele G., Filla A., Cocozza S.,
Labuda M., Montermini L., Poirier J., Pandolfo M.;
"Friedreich's ataxia: point mutations and clinical presentation of
compound heterozygotes.";
Ann. Neurol. 45:200-206(1999).
[35]
VARIANT FRDA ARG-155.
Labuda M., Poirier J., Pandolfo M.;
"A missense mutation (W155R) in an American patient with Friedreich's
ataxia.";
Hum. Mutat. 13:506-506(1999).
[36]
VARIANT FRDA ARG-198.
PubMed=10874325;
DOI=10.1002/1098-1004(200007)16:1<95::AID-HUMU29>3.0.CO;2-E;
Al-Mahdawi S., Pook M., Chamberlain S.;
"A novel missense mutation (L198R) in the Friedreich's ataxia gene.";
Hum. Mutat. 16:95-95(2000).
[37]
CHARACTERIZATION OF VARIANT FRDA PHE-154.
PubMed=19629184; DOI=10.1371/journal.pone.0006379;
Calmels N., Schmucker S., Wattenhofer-Donze M., Martelli A.,
Vaucamps N., Reutenauer L., Messaddeq N., Bouton C., Koenig M.,
Puccio H.;
"The first cellular models based on frataxin missense mutations that
reproduce spontaneously the defects associated with Friedreich
ataxia.";
PLoS ONE 4:E6379-E6379(2009).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:12785837, ECO:0000269|PubMed:15247478,
ECO:0000269|PubMed:15641778, ECO:0000269|PubMed:16239244,
ECO:0000269|PubMed:16608849, ECO:0000269|PubMed:20053667}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
{ECO:0000269|PubMed:15641778}.
-!- SUBUNIT: Monomer (probable predominant form). Oligomer. Monomers
and polymeric aggregates of >1 MDa have been isolated from
mitochondria. A small fraction of heterologous overexpressed
recombinant frataxin forms high-molecular wight aggregates that
incoroprate iron. Interacts with LYRM4 AND HSPA9. Interacts with
ACO1. Interacts with ISCU isoform 1 and isoform 2. 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).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15581888,
ECO:0000269|PubMed:16091420, ECO:0000269|PubMed:16608849,
ECO:0000269|PubMed:18725397, ECO:0000269|PubMed:20053667,
ECO:0000269|PubMed:9241270, ECO:0000269|PubMed:9302253}.
Cytoplasm, cytosol {ECO:0000269|PubMed:16091420,
ECO:0000269|PubMed:16608849, ECO:0000269|PubMed:20053667}.
Note=PubMed:18725397 reports localization exclusively in
mitochondria. {ECO:0000305|PubMed:18725397}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16595-1; Sequence=Displayed;
Name=2;
IsoId=Q16595-2; Sequence=VSP_001576;
Note=Not highly expressed and may be artifactual.;
Name=3;
IsoId=Q16595-3; Sequence=VSP_047282;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in the heart, peripheral blood
lymphocytes and dermal fibroblasts. {ECO:0000269|PubMed:17468497}.
-!- PTM: 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:0000269|PubMed:10428860,
ECO:0000269|PubMed:10545606, ECO:0000269|PubMed:11020385,
ECO:0000269|PubMed:17468497, ECO:0000269|PubMed:18725397}.
-!- DISEASE: Friedreich ataxia (FRDA) [MIM:229300]: Autosomal
recessive, progressive degenerative disease characterized by
neurodegeneration and cardiomyopathy it is the most common
inherited ataxia. The disorder is usually manifest before
adolescence and is generally characterized by incoordination of
limb movements, dysarthria, nystagmus, diminished or absent tendon
reflexes, Babinski sign, impairment of position and vibratory
senses, scoliosis, pes cavus, and hammer toe. In most patients,
FRDA is due to GAA triplet repeat expansions in the first intron
of the frataxin gene. But in some cases the disease is due to
mutations in the coding region. {ECO:0000269|PubMed:10732799,
ECO:0000269|PubMed:10874325, ECO:0000269|PubMed:19629184,
ECO:0000269|PubMed:9150176, ECO:0000269|PubMed:9779809,
ECO:0000269|PubMed:9989622, ECO:0000269|Ref.35, ECO:0000269|Ref.7,
ECO:0000269|Ref.8}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: The unusual migration profile of mature frataxin on
SDS-PAGE due to its acidic N-terminus most likely contributed to
conflicting reports for the N-terminus of the mature protein.
Unlike prokaryotic and yeast frataxin homologs, which self-
assemble at high iron concentrations, oligomerization of human
frataxin is not induced by iron. The existence of a specialized
mitochondrial ferritin in mammalia (FTMT) is suggesting that iron
storage would be redundant function, at least in mammalian
mitochondria.
-!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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EMBL; U43747; AAA98510.1; -; mRNA.
EMBL; U43752; AAA98508.1; -; Genomic_DNA.
EMBL; U43748; AAA98508.1; JOINED; Genomic_DNA.
EMBL; U43749; AAA98508.1; JOINED; Genomic_DNA.
EMBL; U43750; AAA98508.1; JOINED; Genomic_DNA.
EMBL; U43751; AAA98508.1; JOINED; Genomic_DNA.
EMBL; U43753; AAA98509.1; -; Genomic_DNA.
EMBL; U43748; AAA98509.1; JOINED; Genomic_DNA.
EMBL; U43749; AAA98509.1; JOINED; Genomic_DNA.
EMBL; U43750; AAA98509.1; JOINED; Genomic_DNA.
EMBL; U43751; AAA98509.1; JOINED; Genomic_DNA.
EMBL; AL162730; CAH71829.1; -; Genomic_DNA.
EMBL; BC023633; AAH23633.1; -; mRNA.
EMBL; BC048097; AAH48097.1; -; mRNA.
EMBL; Y13751; CAA74077.1; -; Genomic_DNA.
EMBL; AF028240; AAB84047.1; -; Genomic_DNA.
EMBL; U93173; AAD00734.1; -; Genomic_DNA.
CCDS; CCDS43834.1; -. [Q16595-3]
CCDS; CCDS55313.1; -. [Q16595-2]
CCDS; CCDS6626.1; -. [Q16595-1]
RefSeq; NP_000135.2; NM_000144.4. [Q16595-1]
RefSeq; NP_001155178.1; NM_001161706.1. [Q16595-2]
RefSeq; NP_852090.1; NM_181425.2. [Q16595-3]
UniGene; Hs.20685; -.
PDB; 1EKG; X-ray; 1.80 A; A=86-210.
PDB; 1LY7; NMR; -; A=91-210.
PDB; 3S4M; X-ray; 1.30 A; A=82-210.
PDB; 3S5D; X-ray; 1.50 A; A=82-210.
PDB; 3S5E; X-ray; 1.31 A; A=82-210.
PDB; 3S5F; X-ray; 1.50 A; A/B=82-210.
PDB; 3T3J; X-ray; 1.70 A; A=82-210.
PDB; 3T3K; X-ray; 1.24 A; A=82-210.
PDB; 3T3L; X-ray; 1.15 A; A=82-210.
PDB; 3T3T; X-ray; 1.38 A; A/B/C/D=82-210.
PDB; 3T3X; X-ray; 1.57 A; A/B=82-210.
PDB; 5KZ5; EM; 14.30 A; A/B/C/D/E/F/G/H/I/J/K/L=42-210.
PDBsum; 1EKG; -.
PDBsum; 1LY7; -.
PDBsum; 3S4M; -.
PDBsum; 3S5D; -.
PDBsum; 3S5E; -.
PDBsum; 3S5F; -.
PDBsum; 3T3J; -.
PDBsum; 3T3K; -.
PDBsum; 3T3L; -.
PDBsum; 3T3T; -.
PDBsum; 3T3X; -.
PDBsum; 5KZ5; -.
DisProt; DP00607; -.
ProteinModelPortal; Q16595; -.
SMR; Q16595; -.
BioGrid; 108677; 5.
CORUM; Q16595; -.
IntAct; Q16595; 6.
MINT; MINT-2856590; -.
STRING; 9606.ENSP00000366482; -.
ChEMBL; CHEMBL2321640; -.
TCDB; 9.B.21.1.1; the frataxin (frataxin) family.
iPTMnet; Q16595; -.
PhosphoSitePlus; Q16595; -.
BioMuta; FXN; -.
OGP; Q16595; -.
EPD; Q16595; -.
MaxQB; Q16595; -.
PaxDb; Q16595; -.
PeptideAtlas; Q16595; -.
PRIDE; Q16595; -.
TopDownProteomics; Q16595-1; -. [Q16595-1]
TopDownProteomics; Q16595-2; -. [Q16595-2]
DNASU; 2395; -.
Ensembl; ENST00000377270; ENSP00000366482; ENSG00000165060. [Q16595-1]
Ensembl; ENST00000396364; ENSP00000379650; ENSG00000165060. [Q16595-2]
Ensembl; ENST00000396366; ENSP00000379652; ENSG00000165060. [Q16595-3]
GeneID; 2395; -.
KEGG; hsa:2395; -.
UCSC; uc004agz.3; human. [Q16595-1]
CTD; 2395; -.
DisGeNET; 2395; -.
EuPathDB; HostDB:ENSG00000165060.11; -.
GeneCards; FXN; -.
GeneReviews; FXN; -.
HGNC; HGNC:3951; FXN.
HPA; CAB022164; -.
HPA; HPA068304; -.
MalaCards; FXN; -.
MIM; 229300; phenotype.
MIM; 606829; gene.
neXtProt; NX_Q16595; -.
OpenTargets; ENSG00000165060; -.
Orphanet; 95; Friedreich ataxia.
PharmGKB; PA28369; -.
eggNOG; KOG3413; Eukaryota.
eggNOG; COG1965; LUCA.
GeneTree; ENSGT00390000005811; -.
HOGENOM; HOG000190729; -.
HOVERGEN; HBG005745; -.
InParanoid; Q16595; -.
KO; K19054; -.
OMA; QSVYLMN; -.
OrthoDB; EOG091G0UR5; -.
PhylomeDB; Q16595; -.
TreeFam; TF318958; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
ChiTaRS; FXN; human.
EvolutionaryTrace; Q16595; -.
GeneWiki; Frataxin; -.
GenomeRNAi; 2395; -.
PRO; PR:Q16595; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165060; -.
CleanEx; HS_FXN; -.
ExpressionAtlas; Q16595; baseline and differential.
Genevisible; Q16595; HS.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005759; C:mitochondrial matrix; ISS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:BHF-UCL.
GO; GO:0008199; F:ferric iron binding; IDA:BHF-UCL.
GO; GO:0008198; F:ferrous iron binding; IDA:BHF-UCL.
GO; GO:0004322; F:ferroxidase activity; IDA:UniProtKB.
GO; GO:0034986; F:iron chaperone activity; IDA:BHF-UCL.
GO; GO:0051536; F:iron-sulfur cluster binding; IDA:BHF-UCL.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Ensembl.
GO; GO:0006783; P:heme biosynthetic process; NAS:BHF-UCL.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IDA:BHF-UCL.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0006119; P:oxidative phosphorylation; IEA:Ensembl.
GO; GO:1904234; P:positive regulation of aconitate hydratase activity; IMP:BHF-UCL.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0051349; P:positive regulation of lyase activity; IDA:UniProtKB.
GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IMP:BHF-UCL.
GO; GO:0019230; P:proprioception; IEA:Ensembl.
GO; GO:0016540; P:protein autoprocessing; IDA:BHF-UCL.
GO; GO:0010722; P:regulation of ferrochelatase activity; IDA:BHF-UCL.
GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
Gene3D; 3.30.920.10; -; 1.
InterPro; IPR017789; Frataxin.
InterPro; IPR002908; Frataxin/CyaY.
InterPro; IPR036524; Frataxin/CyaY_sf.
InterPro; IPR020895; Frataxin_CS.
PANTHER; PTHR16821; PTHR16821; 1.
Pfam; PF01491; Frataxin_Cyay; 1.
PRINTS; PR00904; FRATAXIN.
SMART; SM01219; Frataxin_Cyay; 1.
SUPFAM; SSF55387; SSF55387; 1.
TIGRFAMs; TIGR03421; FeS_CyaY; 1.
TIGRFAMs; TIGR03422; mito_frataxin; 1.
PROSITE; PS01344; FRATAXIN_1; 1.
PROSITE; PS50810; FRATAXIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Heme biosynthesis;
Ion transport; Iron; Iron storage; Iron transport; Metal-binding;
Mitochondrion; Oxidoreductase; Polymorphism; Reference proteome;
Transit peptide; Transport; Triplet repeat expansion.
TRANSIT 1 41 Mitochondrion.
CHAIN 42 210 Frataxin intermediate form.
/FTId=PRO_0000010129.
CHAIN 56 210 Frataxin(56-210).
/FTId=PRO_0000010130.
CHAIN 78 210 Frataxin(78-210).
/FTId=PRO_0000399388.
CHAIN 81 210 Frataxin mature form.
/FTId=PRO_0000289331.
VAR_SEQ 161 210 SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLS
SLAYSGKDA -> RLTWLLWLFHP (in isoform 2).
{ECO:0000303|PubMed:8596916}.
/FTId=VSP_001576.
VAR_SEQ 161 210 SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLS
SLAYSGKDA -> RYVVDLSVMTGLGKTGCTPTTACPSMSC
WPQSSLKP (in isoform 3). {ECO:0000305}.
/FTId=VSP_047282.
VARIANT 106 106 L -> S (in FRDA; dbSNP:rs104894105).
{ECO:0000269|PubMed:9779809}.
/FTId=VAR_016065.
VARIANT 122 122 D -> Y (in FRDA; dbSNP:rs142157346).
{ECO:0000269|PubMed:9989622,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
/FTId=VAR_002428.
VARIANT 130 130 G -> V (in FRDA; dbSNP:rs104894107).
{ECO:0000269|PubMed:10732799,
ECO:0000269|PubMed:9150176,
ECO:0000269|PubMed:9989622}.
/FTId=VAR_002429.
VARIANT 154 154 I -> F (in FRDA; reduces interaction with
LYRM4; the interaction is rescued by
nickel; a murine cellular FRDA model,
deleted for endogenous frataxin and
expressing human mutant frataxin cDNA
shows defects in mitochondrial structure,
mitochondrial iron deposits, decreased
enzymatic activity of some mitochondrial
and cytoplasmic iron-sulfur cluster-
containing enzymes, increased RNA-binding
activity of ACO1 and increased
sensitivity to oxidative stress;
dbSNP:rs104894106).
{ECO:0000269|PubMed:17331979,
ECO:0000269|PubMed:19629184,
ECO:0000269|PubMed:8596916,
ECO:0000269|PubMed:9150176}.
/FTId=VAR_002430.
VARIANT 155 155 W -> R (in FRDA; reduces interaction with
LYRM4; the interaction is rescued by
nickel; dbSNP:rs138471431).
{ECO:0000269|PubMed:17331979,
ECO:0000269|Ref.35}.
/FTId=VAR_002431.
VARIANT 165 165 R -> C (in FRDA; mild form;
dbSNP:rs138034837).
{ECO:0000269|PubMed:10732799}.
/FTId=VAR_008139.
VARIANT 182 182 L -> F (in FRDA; dbSNP:rs139616452).
{ECO:0000269|PubMed:10732799}.
/FTId=VAR_008140.
VARIANT 198 198 L -> R (in FRDA; dbSNP:rs144104124).
{ECO:0000269|PubMed:10874325}.
/FTId=VAR_016066.
VARIANT 202 202 S -> C (in dbSNP:rs1052195).
/FTId=VAR_049100.
MUTAGEN 39 40 RR->GG: Abolishes cleavage to yield
frataxin intermediate form and allows
accumulation of frataxin(56-210) and
frataxin(78-210).
{ECO:0000269|PubMed:18725397}.
MUTAGEN 53 54 RR->GG: No effect on processing of wild-
type FXN. {ECO:0000269|PubMed:17468497,
ECO:0000269|PubMed:18725397}.
MUTAGEN 78 79 LR->GG: Abolishes cleavage to yield
frataxin mature form and allows
accumulation of frataxin(56-210) and
frataxin(78-210).
{ECO:0000269|PubMed:18725397}.
MUTAGEN 79 80 RK->GG: Abolishes cleavage to yield
frataxin mature form and allows the
accumulation of frataxin(56-210).
{ECO:0000269|PubMed:17468497,
ECO:0000269|PubMed:18725397}.
CONFLICT 175 175 Y -> F (in Ref. 1; AAA98508/AAA98510).
{ECO:0000305}.
CONFLICT 202 202 S -> W (in Ref. 1; AAA98508/AAA98510).
{ECO:0000305}.
HELIX 92 114 {ECO:0000244|PDB:3T3L}.
STRAND 124 128 {ECO:0000244|PDB:3T3L}.
STRAND 131 135 {ECO:0000244|PDB:3T3L}.
TURN 138 140 {ECO:0000244|PDB:1LY7}.
STRAND 142 148 {ECO:0000244|PDB:3T3L}.
TURN 149 152 {ECO:0000244|PDB:3T3L}.
STRAND 153 157 {ECO:0000244|PDB:3T3L}.
STRAND 159 161 {ECO:0000244|PDB:3T3L}.
STRAND 164 168 {ECO:0000244|PDB:3T3L}.
STRAND 170 175 {ECO:0000244|PDB:3T3L}.
TURN 176 178 {ECO:0000244|PDB:3T3L}.
HELIX 182 194 {ECO:0000244|PDB:3T3L}.
STRAND 206 208 {ECO:0000244|PDB:1LY7}.
SEQUENCE 210 AA; 23135 MW; ECC81738779308CF CRC64;
MWTLGRRAVA GLLASPSPAQ AQTLTRVPRP AELAPLCGRR GLRTDIDATC TPRRASSNQR
GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF
EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV
SLHELLAAEL TKALKTKLDL SSLAYSGKDA


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