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AFT1_YEAST
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   03-AUG-2022, entry version 166.
DE   RecName: Full=Iron-regulated transcriptional activator AFT1;
DE   AltName: Full=Activator of iron transcription protein 1;
GN   Name=AFT1; Synonyms=RCS1; 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;
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: Probable transcription factor that activates the genes for
CC       FRE1, FRE2 and FET3 in response to iron deprivation (PubMed:7720713,
CC       PubMed:9200812). Also required for the expression of LSO1
CC       (PubMed:26450372). Iron could interact directly with AFT1 and inhibits
CC       its activity (PubMed:7720713). {ECO:0000269|PubMed:26450372,
CC       ECO:0000269|PubMed:7720713, ECO:0000269|PubMed:9200812}.
CC   -!- INTERACTION:
CC       P22149; Q03835: GRX3; NbExp=4; IntAct=EBI-2332, EBI-22178;
CC       P22149; P32642: GRX4; NbExp=2; IntAct=EBI-2332, EBI-22211;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; 317.
DR   DIP; DIP-1351N; -.
DR   IntAct; P22149; 63.
DR   MINT; P22149; -.
DR   STRING; 4932.YGL071W; -.
DR   iPTMnet; P22149; -.
DR   MaxQB; P22149; -.
DR   PaxDb; P22149; -.
DR   PRIDE; P22149; -.
DR   EnsemblFungi; YGL071W_mRNA; YGL071W; YGL071W.
DR   GeneID; 852809; -.
DR   KEGG; sce:YGL071W; -.
DR   SGD; S000003039; AFT1.
DR   VEuPathDB; FungiDB:YGL071W; -.
DR   eggNOG; KOG4818; Eukaryota.
DR   GeneTree; ENSGT00940000176694; -.
DR   HOGENOM; CLU_025287_0_0_1; -.
DR   InParanoid; P22149; -.
DR   OMA; EHNEYIL; -.
DR   BioCyc; YEAST:G3O-30574-MON; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032048; P:cardiolipin metabolic process; 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   GO; GO:0036086; P:positive regulation of transcription from RNA polymerase II promoter in response to iron ion starvation; IMP:SGD.
DR   GO; GO:1990641; P:response to iron ion starvation; IMP: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.
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   COMPBIAS        159..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
 
 
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