FRDA_CAEEL
ID FRDA_CAEEL Reviewed; 136 AA.
AC Q9TY03;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Frataxin, mitochondrial;
DE Short=Fxn;
DE EC=1.16.3.1;
DE Flags: Precursor;
GN Name=frh-1; ORFNames=F59G1.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Vazquez-Manrique R.P., Baylis H.A., Palau F.;
RT "Characterization of the Caenorhabditis elegans ortholog of the frataxin.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=16293572; DOI=10.1096/fj.05-4212fje;
RA Vazquez-Manrique R.P., Gonzalez-Cabo P., Ros S., Aziz H., Baylis H.A.,
RA Palau F.;
RT "Reduction of Caenorhabditis elegans frataxin increases sensitivity to
RT oxidative stress, reduces lifespan, and causes lethality in a mitochondrial
RT complex II mutant.";
RL FASEB J. 20:172-174(2006).
CC -!- FUNCTION: Promotes the biosynthesis of heme as well as the assembly and
CC repair of iron-sulfur clusters by delivering Fe(2+) to proteins
CC involved in these pathways. May play a role in the protection against
CC iron-catalyzed oxidative stress through its ability to catalyze the
CC oxidation of Fe(2+) to Fe(3+). May be able to store large amounts of
CC the metal in the form of a ferrihydrite mineral by oligomerization.
CC {ECO:0000269|PubMed:16293572}.
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. Oligomer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.
CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000305}.
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DR EMBL; AY048153; AAL05950.1; -; mRNA.
DR EMBL; FO081244; CCD70156.1; -; Genomic_DNA.
DR PIR; T34316; T34316.
DR RefSeq; NP_495183.1; NM_062782.3.
DR AlphaFoldDB; Q9TY03; -.
DR SMR; Q9TY03; -.
DR BioGRID; 39343; 3.
DR IntAct; Q9TY03; 1.
DR STRING; 6239.F59G1.7; -.
DR EPD; Q9TY03; -.
DR PaxDb; Q9TY03; -.
DR PeptideAtlas; Q9TY03; -.
DR EnsemblMetazoa; F59G1.7.1; F59G1.7.1; WBGene00001486.
DR GeneID; 174002; -.
DR KEGG; cel:CELE_F59G1.7; -.
DR UCSC; F59G1.7.1; c. elegans.
DR CTD; 174002; -.
DR WormBase; F59G1.7; CE19476; WBGene00001486; frh-1.
DR eggNOG; KOG3413; Eukaryota.
DR GeneTree; ENSGT00390000005811; -.
DR HOGENOM; CLU_080880_4_0_1; -.
DR InParanoid; Q9TY03; -.
DR OMA; YEVEYHS; -.
DR OrthoDB; 1372185at2759; -.
DR PhylomeDB; Q9TY03; -.
DR Reactome; R-CEL-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q9TY03; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001486; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0034986; F:iron chaperone activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:WormBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:WormBase.
DR GO; GO:0000303; P:response to superoxide; IMP:WormBase.
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 Heme biosynthesis; Ion transport; Iron; Iron storage; Iron transport;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..136
FT /note="Frataxin, mitochondrial"
FT /id="PRO_0000193925"
SQ SEQUENCE 136 AA; 15718 MW; 0ACB254346E38272 CRC64;
MLSTILRNNF VRRSFSSRIF SQNEYETAAD STLERLSDYF DQIADSFPVS EQFDVSHAMG
VLTVNVSKSV GTYVINKQSP NKQIWLSSPM SGPKRYDLEE EGKWTYAHDG EQLDSLLNRE
FRKILADDRI DFSRHV
