ID   FRDA_MACFA              Reviewed;         210 AA.
AC   Q8HXX9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Frataxin, mitochondrial;
DE            Short=Fxn;
DE            EC=1.16.3.1;
DE   Contains:
DE     RecName: Full=Frataxin intermediate form;
DE   Contains:
DE     RecName: Full=Frataxin mature form;
DE   Flags: Precursor;
GN   Name=FXN; Synonyms=FRDA1; ORFNames=QnpA-13971;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RA   Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes the biosynthesis of heme and assembly and repair of
CC       iron-sulfur clusters by delivering Fe(2+) to proteins involved in these
CC       pathways. May play a role in the protection against iron-catalyzed
CC       oxidative stress through its ability to catalyze the oxidation of
CC       Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in
CC       vitro ferroxidase activity. May be able to store large amounts of iron
CC       in the form of a ferrihydrite mineral by oligomerization. Modulates the
CC       RNA-binding activity of ACO1 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC   -!- SUBUNIT: Monomer (probable predominant form). Oligomer. Interacts with
CC       LYRM4 and HSPA9. Interacts with ACO1. Interacts with ISCU. Interacts
CC       with FECH; one iron-bound FXN monomer seems to interact with a FECH
CC       homodimer. Interacts with SDHA and SDHB. Interacts with ACO2; the
CC       interaction is dependent on citrate. {ECO:0000250|UniProtKB:D3ZYW7,
CC       ECO:0000250|UniProtKB:Q16595}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q16595}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q16595}.
CC   -!- PTM: Processed in two steps by mitochondrial processing peptidase
CC       (MPP). MPP first cleaves the precursor to intermediate form and
CC       subsequently converts the intermediate to yield frataxin mature form
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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DR   EMBL; AB083310; BAC20589.1; -; mRNA.
DR   RefSeq; NP_001271967.1; NM_001285038.1.
DR   AlphaFoldDB; Q8HXX9; -.
DR   SMR; Q8HXX9; -.
DR   STRING; 9541.XP_005581933.1; -.
DR   GeneID; 102120656; -.
DR   CTD; 2395; -.
DR   eggNOG; KOG3413; Eukaryota.
DR   OrthoDB; 1372185at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   Gene3D; 3.30.920.10; -; 1.
DR   InterPro; IPR017789; Frataxin.
DR   InterPro; IPR002908; Frataxin/CyaY.
DR   InterPro; IPR036524; Frataxin/CyaY_sf.
DR   InterPro; IPR020895; Frataxin_CS.
DR   PANTHER; PTHR16821; PTHR16821; 1.
DR   Pfam; PF01491; Frataxin_Cyay; 1.
DR   PRINTS; PR00904; FRATAXIN.
DR   SMART; SM01219; Frataxin_Cyay; 1.
DR   SUPFAM; SSF55387; SSF55387; 1.
DR   TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR   TIGRFAMs; TIGR03422; mito_frataxin; 1.
DR   PROSITE; PS01344; FRATAXIN_1; 1.
DR   PROSITE; PS50810; FRATAXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Heme biosynthesis; Ion transport; Iron; Iron storage;
KW   Iron transport; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           42..210
FT                   /note="Frataxin intermediate form"
FT                   /id="PRO_0000010131"
FT   CHAIN           81..210
FT                   /note="Frataxin mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000399389"
SQ   SEQUENCE   210 AA;  23133 MW;  C90A50A3F3E7D581 CRC64;
     MWTFGRRAVA GLLASPSPAQ AQTLTRAPRL AELAQLCSRR GLRTGINATR TTHHTSSNLR
     GLNQIRNVKR QSVYLMNLRK SGTLGHPGSL DDTTYERLAE ETLDSLAEFF EDLADKPYTF
     EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDRTG KNWVYSHDGV
     SLHELLGAEL TKALKTKLDL SSLAYSGKDA