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UniProtKB/Swiss-Prot entry Q07540


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FRDA_YEAST
Primary accession number Q07540
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 87)
Name and origin of the protein
Protein name Frataxin homolog, mitochondrial [Precursor]
Synonyms None
Contains Frataxin homolog intermediate form
Gene name
Name: YFH1
OrderedLocusNames: YDL120W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1126/science.276.5319.1709; PubMed=9180083 [NCBI, ExPASy, EBI, Israel, Japan]
Babcock M., de Silva D., Oaks R., Davis-Kaplan S., Jiralerspong S., Montermini L., Pandolfo M., Kaplan J.;
"Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin.";
Science 276:1709-1712(1997).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.274.8.4497; PubMed=9988680 [NCBI, ExPASy, EBI, Israel, Japan]
Radisky D.C., Babcock M.C., Kaplan J.;
"The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle.";
J. Biol. Chem. 274:4497-4499(1999).
[5]
PROCESSING.
DOI=10.1093/hmg/8.12.2255; PubMed=10545606 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROCESSING.
DOI=10.1074/jbc.274.32.22763; PubMed=10428860 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
INTERACTION WITH ISU1.
DOI=10.1006/jmbi.1999.3294; PubMed=10588895 [NCBI, ExPASy, EBI, Israel, Japan]
Garland S.A., Hoff K., Vickery L.E., Culotta V.C.;
"Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly.";
J. Mol. Biol. 294:897-907(1999).
[8]
INTERACTION WITH ISU1.
DOI=10.1038/sj.embor.embor918; PubMed=12947415 [NCBI, ExPASy, EBI, Israel, Japan]
Gerber J., Muhlenhoff U., Lill R.;
"An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1.";
EMBO Rep. 4:906-911(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
  • FUNCTION: Seems to be involved in the regulation of mitochondrial iron efflux.
  • SUBUNIT: Interacts with ISU1.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • PTM: Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to mature size protein.
  • MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the frataxin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z74168; CAA98688.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558160; AAS56486.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67663; S67663.
RefSeq NP_010163.1; -.
3D structure databases
PDB
2FQL; X-ray; 3.01 A; A=52-174.[ExPASy / RCSB / EBI]
2GA5; NMR; -; A=53-174.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2FQL; -.
2GA5; -.
ModBase Q07540.
Protein-protein interaction databases
DIP DIP:7485N; -.
Organism-specific databases
CYGD YDL120w; -.
SGD S000002278; YFH1.
Yeast-GFP YDL120W.
Gene expression databases
GermOnline YDL120W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from direct assay from SGD).
GO:0008198; Molecular function: ferrous iron binding (inferred from direct assay from SGD).
GO:0004322; Molecular function: ferroxidase activity (inferred from direct assay from SGD).
GO:0034986; Molecular function: iron chaperone activity (inferred from direct assay from SGD).
GO:0006879; Biological process: cellular iron ion homeostasis (inferred from direct assay from SGD).
GO:0006749; Biological process: glutathione metabolic process (inferred from mutant phenotype from SGD).
GO:0006826; Biological process: iron ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0016226; Biological process: iron-sulfur cluster assembly (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR017789; Frataxin.
IPR002908; Frataxin-like.
Graphical view of domain structure.
Gene3D G3DSA:3.30.920.10; Frataxin_like; 1.
Pfam PF01491; Frataxin_Cyay; 1.
Pfam graphical view of domain structure.
ProDom PD238818; Frataxin_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03421; FeS_CyaY; 1.
TIGR03422; mito_frataxin; 1.
PROSITE PS01344; FRATAXIN_1; 1.
PS50810; FRATAXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl YDL120W; Saccharomyces cerevisiae. [Contig view]
GeneID 851437; -.
GenomeReviews Z71256_GR; YDL120W.
KEGG sce:YDL120W; -.
NMPDR fig|4932.3.peg.900; -.
Phylogenomic databases
HOGENOM Q07540; -.
OMA Q07540; HIPEVEY.
Other
NextBio 968672; -.
ProtoNet Q07540.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Ion transport; Iron; Iron transport; Mitochondrion; Transit peptide; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    21  21     Mitochondrion (Probable). 
CHAIN   22   174  153     Frataxin homolog intermediate form. PRO_0000010135
CHAIN   52   174  123     Frataxin homolog, mitochondrial. PRO_0000010136
TURN   63    67  5      
HELIX   76    89  14      
STRAND   92    94  3      
STRAND   96    99  4      
STRAND   101   103  3      
STRAND   106   113  8      
TURN   114   116  3      
STRAND   117   123  7      
STRAND   126   134  9      
TURN   135   137  3      
STRAND   138   147  10      
STRAND   149   151  3      
TURN   152   154  3      
HELIX   158   171  14      
Sequence information
Length: 174 AA [This is the length of the unprocessed precursor] Molecular weight: 19490 Da [This is the MW of the unprocessed precursor] CRC64: AB1FF7478EF0E5D6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIKRSLASLV RVSSVMGRRY MIAAAGGERA RFCPAVTNKK NHTVNTFQKR FVESSTDGQV 

        70         80         90        100        110        120 
VPQEVLNLPL EKYHEEADDY LDHLLDSLEE LSEAHPDCIP DVELSHGVMT LEIPAFGTYV 

       130        140        150        160        170 
INKQPPNKQI WLASPLSGPN RFDLLNGEWV SLRNGTKLTD ILTEEVEKAI SKSQ 

Q07540 in FASTA format

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