D3ZYW7 (FRDA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Frataxin, mitochondrial
Short name=Fxn
EC=1.16.3.1

Cleaved into the following 2 chains:

1. Frataxin intermediate form
2. Frataxin mature form

Gene names

Name:

Fxn

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe2+ 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 Fe2+ to Fe3+; 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. Ref.2
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Subunit structure	Monomer (probable predominant form). Oligomer. Interacts with LYRM4 AND HSPA9. Interacts with ACO1. Interacts with ISCU. Interacts with FECH; one iron-bound FXN monomer seems to interact with a FECH homodimer. Interacts with SDHA and SDHB By similarity. Interacts with ACO2; the interaction is dependent on citrate. Ref.2
Subcellular location	Cytoplasm By similarity. Mitochondrion By similarity.
Post-translational modification	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 By similarity.
Sequence similarities	Belongs to the frataxin family.

Ontologies

Keywords
Biological process	Heme biosynthesis Ion transport Iron storage Iron transport Transport
Cellular component	Cytoplasm Mitochondrion
Domain	Transit peptide
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara aerobic respiration Inferred from electronic annotation. Source: Compara cellular iron ion homeostasis Non-traceable author statement Ref.2. Source: RGD cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara embryo development ending in birth or egg hatching Inferred from electronic annotation. Source: Compara heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW iron incorporation into metallo-sulfur cluster Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara negative regulation of organ growth Inferred from electronic annotation. Source: Compara negative regulation of release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara oxidative phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of axon extension Inferred from mutant phenotype PubMed 18809400. Source: RGD positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of lyase activity Inferred from electronic annotation. Source: Compara positive regulation of metalloenzyme activity Inferred from electronic annotation. Source: Compara positive regulation of oxidoreductase activity Inferred from electronic annotation. Source: Compara positive regulation of transferase activity Inferred from electronic annotation. Source: Compara proprioception Inferred from electronic annotation. Source: Compara protein autoprocessing Inferred from electronic annotation. Source: Compara regulation of ferrochelatase activity Inferred from electronic annotation. Source: Compara response to drug Inferred from expression pattern PubMed 18809400. Source: RGD response to iron ion Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from expression pattern PubMed 18809400. Source: RGD
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay Ref.2. Source: RGD
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: Compara ferric iron binding Inferred from electronic annotation. Source: InterPro ferrous iron binding Inferred from electronic annotation. Source: Compara ferroxidase activity Inferred from electronic annotation. Source: EC iron chaperone activity Inferred from electronic annotation. Source: Compara metallochaperone activity Non-traceable author statement Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 40	40	Mitochondrion By similarity
	Chain	41 – 208	168	Frataxin intermediate form		PRO_0000399465
	Chain	79 – 208	130	Frataxin mature form By similarity		PRO_0000399391

Sequences

	Sequence		Length	Mass (Da)
	D3ZYW7 [UniParc]. Last modified April 20, 2010. Version 1. Checksum: 401B8210F5CEDD35	FASTA	208	23,066
	10 20 30 40 50 60 MWTFGRRAAA GLLPRTASRA SAWVRNPRGR ERIGTCGRRG LHVTANADAI RHSHLNLHYL 70 80 90 100 110 120 GQILNIKKQS VCVVHLRNSG TLGNPSSLDE TAYERLAEET LDALAEFFED LADKPYTLKD 130 140 150 160 170 180 YDVSFGDGVL TIKLGGDLGT YVINKQTPLL YLWFSGPCSG PKRYDWTGKN WVYSHDGVSL 190 200 HELLARELTE ALNTKLDLSS LAYSGKGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity." Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., Szweda L.I. Science 305:242-245(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS IRON CHAPERONE, INTERACTION WITH ACO2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03005338 Genomic DNA. No translation available. AABR03006217 Genomic DNA. No translation available. AABR03009513 Genomic DNA. No translation available.
IPI	IPI00389333.
UniGene	Rn.13133.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	D3ZYW7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:1565754. rat.
Organism-specific databases
RGD	1565754. Fxn.
Phylogenomic databases
OrthoDB	EOG4ZCT5S.
Family and domain databases
Gene3D	3.30.920.10. 1 hit.
InterPro	IPR017789. Frataxin. IPR002908. Frataxin/CyaY. [Graphical view]
PANTHER	PTHR16821. PTHR16821. 1 hit.
Pfam	PF01491. Frataxin_Cyay. 1 hit. [Graphical view]
PRINTS	PR00904. FRATAXIN.
SUPFAM	SSF55387. Frataxin_like. 1 hit.
TIGRFAMs	TIGR03421. FeS_CyaY. 1 hit. TIGR03422. mito_frataxin. 1 hit.
PROSITE	PS50810. FRATAXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRDA_RAT

Accession

Primary (citable) accession number: D3ZYW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	April 20, 2010
Last modified:	April 3, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program