ID   FRDA_YEAST              Reviewed;         174 AA.
AC   Q07540;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   22-JUL-2008, entry version 78.
DE   RecName: Full=Frataxin homolog, mitochondrial;
DE   Contains:
DE     RecName: Full=Frataxin homolog intermediate form;
DE   Flags: Precursor;
GN   Name=YFH1; OrderedLocusNames=YDL120W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=97324273; PubMed=9180083; DOI=10.1126/science.276.5319.1709;
RA   Babcock M., de Silva D., Oaks R., Davis-Kaplan S., Jiralerspong S.,
RA   Montermini L., Pandolfo M., Kaplan J.;
RT   "Regulation of mitochondrial iron accumulation by Yfh1p, a putative
RT   homolog of frataxin.";
RL   Science 276:1709-1712(1997).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=99143100; PubMed=9988680; DOI=10.1074/jbc.274.8.4497;
RA   Radisky D.C., Babcock M.C., Kaplan J.;
RT   "The yeast frataxin homologue mediates mitochondrial iron efflux.
RT   Evidence for a mitochondrial iron cycle.";
RL   J. Biol. Chem. 274:4497-4499(1999).
RN   [5]
RP   PROCESSING.
RX   MEDLINE=20014717; PubMed=10545606; DOI=10.1093/hmg/8.12.2255;
RA   Gordon D.M., Shi Q., Dancis A., Pain D.;
RT   "Maturation of frataxin within mammalian and yeast mitochondria: one-
RT   step processing by matrix processing peptidase.";
RL   Hum. Mol. Genet. 8:2255-2262(1999).
RN   [6]
RP   PROCESSING.
RX   MEDLINE=99357816; PubMed=10428860; DOI=10.1074/jbc.274.32.22763;
RA   Branda S.S., Cavadini P., Adamec J., Kalousek F., Taroni F., Isaya G.;
RT   "Yeast and human frataxin are processed to mature form in two
RT   sequential steps by the mitochondrial processing peptidase.";
RL   J. Biol. Chem. 274:22763-22769(1999).
RN   [7]
RP   INTERACTION WITH ISU1.
RX   PubMed=10588895; DOI=10.1006/jmbi.1999.3294;
RA   Garland S.A., Hoff K., Vickery L.E., Culotta V.C.;
RT   "Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved
RT   gene family for iron-sulfur cluster assembly.";
RL   J. Mol. Biol. 294:897-907(1999).
RN   [8]
RP   INTERACTION WITH ISU1.
RX   PubMed=12947415; DOI=10.1038/sj.embor.embor918;
RA   Gerber J., Muhlenhoff U., Lill R.;
RT   "An interaction between frataxin and Isu1/Nfs1 that is crucial for
RT   Fe/S cluster synthesis on Isu1.";
RL   EMBO Rep. 4:906-911(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Seems to be involved in the regulation of mitochondrial
CC       iron efflux.
CC   -!- SUBUNIT: Interacts with ISU1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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 mature size protein.
CC   -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the frataxin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z74168; CAA98688.1; -; Genomic_DNA.
DR   EMBL; AY558160; AAS56486.1; -; Genomic_DNA.
DR   PIR; S67663; S67663.
DR   RefSeq; NP_010163.1; -.
DR   PDB; 2FQL; X-ray; 3.01 A; A=52-174.
DR   PDB; 2GA5; NMR; -; A=52-174.
DR   PDBsum; 2FQL; -.
DR   PDBsum; 2GA5; -.
DR   DIP; DIP:7485N; -.
DR   Ensembl; YDL120W; Saccharomyces cerevisiae.
DR   GeneID; 851437; -.
DR   GenomeReviews; Z71256_GR; YDL120W.
DR   KEGG; sce:YDL120W; -.
DR   NMPDR; fig|4932.3.peg.900; -.
DR   CYGD; YDL120w; -.
DR   SGD; S000002278; YFH1.
DR   HOGENOM; Q07540; -.
DR   LinkHub; Q07540; -.
DR   GermOnline; YDL120W; Saccharomyces cerevisiae.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:SGD.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:SGD.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IDA:SGD.
DR   GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IGI:SGD.
DR   GO; GO:0006800; P:oxygen and reactive oxygen species metaboli...; IMP:SGD.
DR   InterPro; IPR017789; Frataxin.
DR   InterPro; IPR002908; Frataxin_like.
DR   InterPro; IPR001794; Frataxin_sub.
DR   Gene3D; G3DSA:3.30.920.10; Frataxin_like; 1.
DR   Pfam; PF01491; Frataxin_Cyay; 1.
DR   PRINTS; PR00904; FRATAXIN.
DR   ProDom; PD238818; Frataxin_like; 1.
DR   TIGRFAMs; TIGR03421; FeS_CyaY; 1.
DR   PROSITE; PS01344; FRATAXIN_1; 1.
DR   PROSITE; PS50810; FRATAXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Ion transport; Iron; Iron transport;
KW   Mitochondrion; Transit peptide; Transport.
FT   TRANSIT       1     21       Mitochondrion (Probable).
FT   CHAIN        22    174       Frataxin homolog intermediate form.
FT                                /FTId=PRO_0000010135.
FT   CHAIN        52    174       Frataxin homolog.
FT                                /FTId=PRO_0000010136.
FT   TURN         63     67
FT   HELIX        76     89
FT   STRAND       92     94
FT   STRAND       96     99
FT   STRAND      101    103
FT   STRAND      106    113
FT   TURN        114    116
FT   STRAND      117    123
FT   STRAND      126    134
FT   TURN        135    137
FT   STRAND      138    147
FT   STRAND      149    151
FT   TURN        152    154
FT   HELIX       158    171
SQ   SEQUENCE   174 AA;  19490 MW;  AB1FF7478EF0E5D6 CRC64;
     MIKRSLASLV RVSSVMGRRY MIAAAGGERA RFCPAVTNKK NHTVNTFQKR FVESSTDGQV
     VPQEVLNLPL EKYHEEADDY LDHLLDSLEE LSEAHPDCIP DVELSHGVMT LEIPAFGTYV
     INKQPPNKQI WLASPLSGPN RFDLLNGEWV SLRNGTKLTD ILTEEVEKAI SKSQ
//