AFT2_YEAST
ID AFT2_YEAST Reviewed; 416 AA.
AC Q08957; D6W3G7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Iron-regulated transcriptional activator AFT2;
DE AltName: Full=Activator of iron transcription protein 2;
GN Name=AFT2; OrderedLocusNames=YPL202C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11448968; DOI=10.1074/jbc.m104987200;
RA Blaiseau P.-L., Lesuisse E., Camadro J.-M.;
RT "Aft2p, a novel iron-regulated transcription activator that modulates, with
RT Aft1p, intracellular iron use and resistance to oxidative stress in
RT yeast.";
RL J. Biol. Chem. 276:34221-34226(2001).
RN [4]
RP FUNCTION.
RX PubMed=11734641; DOI=10.1073/pnas.261381198;
RA Rutherford J.C., Jaron S., Ray E., Brown P.O., Winge D.R.;
RT "A second iron-regulatory system in yeast independent of Aft1p.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14322-14327(2001).
RN [5]
RP FUNCTION.
RX PubMed=12756250; DOI=10.1074/jbc.m300076200;
RA Rutherford J.C., Jaron S., Winge D.R.;
RT "Aft1p and Aft2p mediate iron-responsive gene expression in yeast through
RT related promoter elements.";
RL J. Biol. Chem. 278:27636-27643(2003).
RN [6]
RP FUNCTION.
RX PubMed=15649888; DOI=10.1074/jbc.m413731200;
RA Rutherford J.C., Ojeda L., Balk J., Muehlenhoff U., Lill R., Winge D.R.;
RT "Activation of the iron regulon by the yeast Aft1/Aft2 transcription
RT factors depends on mitochondrial but not cytosolic iron-sulfur protein
RT biogenesis.";
RL J. Biol. Chem. 280:10135-10140(2005).
RN [7]
RP FUNCTION.
RX PubMed=16024809; DOI=10.1128/mcb.25.15.6760-6771.2005;
RA Courel M., Lallet S., Camadro J.-M., Blaiseau P.-L.;
RT "Direct activation of genes involved in intracellular iron use by the yeast
RT iron-responsive transcription factor Aft2 without its paralog Aft1.";
RL Mol. Cell. Biol. 25:6760-6771(2005).
CC -!- FUNCTION: Transcription factor required for iron homeostasis and
CC resistance to oxidative stress. With RCS1, activates the gene
CC expression in response to low-iron conditions, also called iron
CC regulon. {ECO:0000269|PubMed:11448968, ECO:0000269|PubMed:11734641,
CC ECO:0000269|PubMed:12756250, ECO:0000269|PubMed:15649888,
CC ECO:0000269|PubMed:16024809}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: The transcription activation by RCS1 and AST2 depends on
CC the mitochondrial iron-sulfur protein biosynthesis pathway.
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DR EMBL; Z73558; CAA97916.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11233.1; -; Genomic_DNA.
DR PIR; S65221; S65221.
DR RefSeq; NP_015122.1; NM_001184016.1.
DR PDB; 4LMG; X-ray; 2.20 A; A/B/C/D=38-193.
DR PDBsum; 4LMG; -.
DR AlphaFoldDB; Q08957; -.
DR SMR; Q08957; -.
DR BioGRID; 35982; 64.
DR MINT; Q08957; -.
DR STRING; 4932.YPL202C; -.
DR MaxQB; Q08957; -.
DR PaxDb; Q08957; -.
DR PRIDE; Q08957; -.
DR EnsemblFungi; YPL202C_mRNA; YPL202C; YPL202C.
DR GeneID; 855899; -.
DR KEGG; sce:YPL202C; -.
DR SGD; S000006123; AFT2.
DR VEuPathDB; FungiDB:YPL202C; -.
DR eggNOG; ENOG502S28S; Eukaryota.
DR GeneTree; ENSGT00940000176694; -.
DR HOGENOM; CLU_674652_0_0_1; -.
DR InParanoid; Q08957; -.
DR BioCyc; YEAST:G3O-34094-MON; -.
DR PRO; PR:Q08957; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08957; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IMP:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0032048; P:cardiolipin metabolic process; IMP:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IGI:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0036086; P:positive regulation of transcription from RNA polymerase II promoter in response to iron ion starvation; IGI:SGD.
DR GO; GO:2000185; P:regulation of phosphate transmembrane transport; IMP:SGD.
DR InterPro; IPR014842; AFT.
DR Pfam; PF08731; AFT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Iron; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..416
FT /note="Iron-regulated transcriptional activator AFT2"
FT /id="PRO_0000227599"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4LMG"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:4LMG"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4LMG"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4LMG"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4LMG"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:4LMG"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:4LMG"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4LMG"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:4LMG"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:4LMG"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:4LMG"
SQ SEQUENCE 416 AA; 47105 MW; 0DAC56291EE56EFA CRC64;
MKAKSMKSII SVPISVSKTG KMKLTASPDN LASMMSKDQN KLIHLDPVPS FEDRHEIKPW
LQKIFYPQGI DIVIERSDSS KVTFKCRSVR SKVGLNPKSK GSSSRSHACP FRIRAAYSVR
LQKWNVVVMN NIHSHELRFD LITKTDDYKK FKENLRQKND EKAIKTFDEL EYKASLNLPL
VTPIISCDCG LTKEIEAFNN IFLPLSNPPL TSKKNLLKTN KNSVSKIKSR QMDNSKPRPR
LKTKLDADLH DTGFLDNFKT RNSCVKIEKE DSLTNLNEID FTNMFCNDNF IQNYNQGLME
LLTEPTPGPS SSSCILPSTP TRPLSQSKMD IALSESTTSS PNFMETDAPY GDEIIKVSKD
TKSNAPTADT DIATNLGKER NENFGMLNYN YEALLHFNDE HFNELNSIDP ALISKY
