ID   AFT1_YEAST              Reviewed;         690 AA.
AC   P22149; D6VU71; Q06993;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   02-SEP-2026, entry version 180.
DE   RecName: Full=Iron-regulated transcriptional activator AFT1 {ECO:0000303|PubMed:7720713};
DE   AltName: Full=Activator of iron transcription protein 1 {ECO:0000303|PubMed:7720713};
GN   Name=AFT1 {ECO:0000303|PubMed:7720713}; Synonyms=RCS1;
GN   OrderedLocusNames=YGL071W;
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 [MRNA], AND FUNCTION.
RX   PubMed=7720713; DOI=10.1002/j.1460-2075.1995.tb07106.x;
RA   Yamaguchi-Iwai Y., Dancis A., Klausner R.D.;
RT   "AFT1: a mediator of iron regulated transcriptional control in
RT   Saccharomyces cerevisiae.";
RL   EMBO J. 14:1231-1239(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9200812;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<621::aid-yea121>3.0.co;2-u;
RA   Casas C., Aldea M., Espinet C., Gallego C., Gil R., Herrero E.;
RT   "The AFT1 transcriptional factor is differentially required for expression
RT   of high-affinity iron uptake genes in Saccharomyces cerevisiae.";
RL   Yeast 13:621-637(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869; DOI=10.1038/387s081;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [5]
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   [6]
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., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 283-690.
RC   STRAIN=ATCC 26786 / X2180-1A;
RX   PubMed=2021081; DOI=10.1002/yea.320070102;
RA   Gil R., Zueco J., Sentandreu R., Herrero E.;
RT   "RCS1, a gene involved in controlling cell size in Saccharomyces
RT   cerevisiae.";
RL   Yeast 7:1-14(1991).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26450372; DOI=10.1002/mbo3.303;
RA   An X., Zhang C., Sclafani R.A., Seligman P., Huang M.;
RT   "The late-annotated small ORF LSO1 is a target gene of the iron regulon of
RT   Saccharomyces cerevisiae.";
RL   MicrobiologyOpen 4:941-951(2015).
CC   -!- FUNCTION: Transcription factor that activates the genes for FRE1, FRE2
CC       and FET3 in response to iron deprivationand thereby plays a central
CC       role in iron homeostasis (PubMed:7720713, PubMed:9200812). Also
CC       required for the expression of LSO1 (PubMed:26450372). Recognizes the
CC       consensus iron-responsive element (Fe-RE) sequence 5'-CACCC-3' in the
CC       promoters of target genes (By similarity). Iron could interact directly
CC       with AFT1 and inhibits its activity (PubMed:7720713). In high iron
CC       condition, the presence of Fe(2+) or [2Fe-2S] cluster leads to
CC       dimerization, which in turn leads to a decrease in DNA affinity (By
CC       similarity). {ECO:0000250|UniProtKB:Q08957,
CC       ECO:0000269|PubMed:26450372, ECO:0000269|PubMed:7720713,
CC       ECO:0000269|PubMed:9200812}.
CC   -!- ACTIVITY REGULATION: Dimerization via the binding of Fe(2+) or a [2Fe-
CC       2S] cluster decreases the DNA-binding activity.
CC       {ECO:0000250|UniProtKB:Q08957}.
CC   -!- SUBUNIT: Homodimer (By similarity). Dimerization decreases the DNA-
CC       binding activity (By similarity). {ECO:0000250|UniProtKB:Q08957}.
CC   -!- INTERACTION:
CC       P22149; Q03835: GRX3; NbExp=4; IntAct=EBI-2332, EBI-22178;
CC       P22149; P32642: GRX4; NbExp=3; IntAct=EBI-2332, EBI-22211;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The CDC motif is involved in iron-sensong via binding to Fe(2+)
CC       or [2Fe-2S] cluster, which leads to dimerization and loss of DNA-
CC       binding. {ECO:0000250|UniProtKB:Q08957}.
CC   -!- DISRUPTION PHENOTYPE: Two-fold reduction in expression of LSO1.
CC       {ECO:0000269|PubMed:26450372}.
CC   -!- MISCELLANEOUS: Present with 2730 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA37215.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA54586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z48004; CAA88044.1; -; mRNA.
DR   EMBL; X77413; CAA54586.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z72593; CAA96775.1; -; Genomic_DNA.
DR   EMBL; AY723805; AAU09722.1; -; Genomic_DNA.
DR   EMBL; X53046; CAA37215.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006941; DAA08032.1; -; Genomic_DNA.
DR   PIR; S54775; S54775.
DR   RefSeq; NP_011444.1; NM_001180936.1.
DR   AlphaFoldDB; P22149; -.
DR   SMR; P22149; -.
DR   BioGRID; 33177; 329.
DR   DIP; DIP-1351N; -.
DR   FunCoup; P22149; 1623.
DR   IntAct; P22149; 64.
DR   MINT; P22149; -.
DR   STRING; 4932.YGL071W; -.
DR   iPTMnet; P22149; -.
DR   PaxDb; 4932-YGL071W; -.
DR   PeptideAtlas; P22149; -.
DR   EnsemblFungi; YGL071W_mRNA; YGL071W; YGL071W.
DR   GeneID; 852809; -.
DR   KEGG; sce:YGL071W; -.
DR   AGR; SGD:S000003039; -.
DR   SGD; S000003039; AFT1.
DR   VEuPathDB; FungiDB:YGL071W; -.
DR   eggNOG; KOG4818; Eukaryota.
DR   HOGENOM; CLU_025287_0_0_1; -.
DR   InParanoid; P22149; -.
DR   OMA; EHNEYIL; -.
DR   OrthoDB; 4068596at2759; -.
DR   BioCyc; YEAST:G3O-30574-MONOMER; -.
DR   BioGRID-ORCS; 852809; 5 hits in 13 CRISPR screens.
DR   PRO; PR:P22149; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P22149; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0043515; F:kinetochore binding; IDA:SGD.
DR   GO; GO:0032048; P:cardiolipin metabolic process; IMP:SGD.
DR   GO; GO:0010106; P:cellular response to iron ion starvation; IMP:SGD.
DR   GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0034758; P:positive regulation of iron ion transport; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR   InterPro; IPR014842; AFT.
DR   Pfam; PF08731; AFT; 1.
PE   1: Evidence at protein level;
KW   Activator; Iron; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..690
FT                   /note="Iron-regulated transcriptional activator AFT1"
FT                   /id="PRO_0000064487"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           291..293
FT                   /note="CDC [2Fe-2S] cluster binding motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   COMPBIAS        148..159
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..638
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         111
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         115
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         131
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         132
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         133
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         134
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         135
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         138
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         226
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   BINDING         263
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250|UniProtKB:Q08957"
FT   VARIANT         291
FT                   /note="C -> F (in allele AFT1-1UP; which is constitutively
FT                   activated)"
FT   CONFLICT        8
FT                   /note="D -> H (in Ref. 2; CAA54586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="I -> S (in Ref. 2; CAA54586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="A -> T (in Ref. 2; CAA54586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="D -> N (in Ref. 2; CAA54586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="S -> L (in Ref. 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="S -> L (in Ref. 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="D -> G (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="N -> T (in Ref. 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        507
FT                   /note="N -> S (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="S -> F (in Ref. 2; CAA54586)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="S -> L (in Ref. 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="S -> P (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="S -> T (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        644
FT                   /note="H -> I (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        649
FT                   /note="H -> L (in Ref. 2; CAA54586 and 7; CAA37215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  77683 MW;  38641F26B76FCBDD CRC64;
     MEGFNPADIE HASPINSSDS HSSSFVYALP KSASEYVVNH NEGRASASGN PAAVPSPIMT
     LNLKSTHSLN IDQHVHTSTS PTETIGHIHH VEKLNQNNLI HLDPVPNFED KSDIKPWLQK
     IFYPQGIELV IERSDAFKVV FKCKAAKRGR NARRKRKDKP KGQDHEDEKS KINDDELEYA
     SPSNATVTNG PQTSPDQTSS IKPKKKRCVS RFNNCPFRVR ATYSLKRKRW SIVVMDNNHS
     HQLKFNPDSE EYKKFKEKLR KDNDVDAIKK FDELEYRTLA NLPIPTATIP CDCGLTNEIQ
     SFNVVLPTNS NVTSSASSST VSSISLDSSN ASKRPCLPSV NNTGSINTNN VRKPKSQCKN
     KDTLLKRTTM QNFLTTKSRL RKTGTPTSSQ HSSTAFSGYI DDPFNLNEIL PLPASDFKLN
     TVTNLNEIDF TNIFTKSPHP HSGSTHPRQV FDQLDDCSSI LFSPLTTNTN NEFEGESDDF
     VHSPYLNSEA DFSQILSSAP PVHHDPNETH QENQDIIDRF ANSSQEHNEY ILQYLTHSDA
     ANHNNIGVPN NNSHSLNTQH NVSDLGNSLL RQEALVGSSS TKIFDELKFV QNGPHGSQHP
     IDFQHVDHRH LSSNEPQVRS HQYGPQQQPP QQLQYHQNQP HDGHNHEQHQ TVQKDMQTHE
     SLEIMGNTLL EEFKDIKMVN GELKYVKPED
//