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MET28_YEAST
ID   MET28_YEAST             Reviewed;         187 AA.
AC   P40573; D6VVU7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Transcriptional activator of sulfur metabolism MET28;
DE   AltName: Full=Methionine-requiring protein 28;
GN   Name=MET28; OrderedLocusNames=YIR017C;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, AND DNA-BINDING.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=8665859; DOI=10.1002/j.1460-2075.1996.tb00609.x;
RA   Kuras L., Cherest H., Surdin-Kerjan Y., Thomas D.;
RT   "A heteromeric complex containing the centromere binding factor 1 and two
RT   basic leucine zipper factors, Met4 and Met28, mediates the transcription
RT   activation of yeast sulfur metabolism.";
RL   EMBO J. 15:2519-2529(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
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   [4]
RP   FUNCTION, SUBUNIT, AND INDUCTION.
RX   PubMed=9171357; DOI=10.1093/emboj/16.9.2441;
RA   Kuras L., Barbey R., Thomas D.;
RT   "Assembly of a bZIP-bHLH transcription activation complex: formation of the
RT   yeast Cbf1-Met4-Met28 complex is regulated through Met28 stimulation of
RT   Cbf1 DNA binding.";
RL   EMBO J. 16:2441-2451(1997).
RN   [5]
RP   SUBUNIT.
RX   PubMed=9799240; DOI=10.1093/emboj/17.21.6327;
RA   Blaiseau P.L., Thomas D.;
RT   "Multiple transcriptional activation complexes tether the yeast activator
RT   Met4 to DNA.";
RL   EMBO J. 17:6327-6336(1998).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
CC   -!- FUNCTION: Acts as an accessory factor in the activation of sulfur amino
CC       acids metabolism genes. Possesses no intrinsic transcription activation
CC       abilities. Binds to the MET16 promoter as a complex with MET4 and CBF1.
CC       Enhances the DNA-binding activity of CBF1. {ECO:0000269|PubMed:8665859,
CC       ECO:0000269|PubMed:9171357}.
CC   -!- SUBUNIT: Interacts with MET4 to form a heteromeric complex which also
CC       includes CBF1. Forms two alternate complexes associating MET28 with
CC       MET4 and either MET31 or MET32. Binds to DNA through the MET4-MET28-
CC       CBF1 complex. {ECO:0000269|PubMed:8665859, ECO:0000269|PubMed:9171357,
CC       ECO:0000269|PubMed:9799240}.
CC   -!- INTERACTION:
CC       P40573; P32389: MET4; NbExp=5; IntAct=EBI-11503, EBI-10757;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Expression requires MET4, and is repressed by an increase of
CC       intracellular S-adenosylmethionine (AdoMet).
CC       {ECO:0000269|PubMed:9171357}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U17015; AAC49425.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z37996; CAA86087.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08563.1; -; Genomic_DNA.
DR   PIR; S48361; S48361.
DR   RefSeq; NP_012282.3; NM_001179539.3.
DR   AlphaFoldDB; P40573; -.
DR   SMR; P40573; -.
DR   BioGRID; 35009; 160.
DR   ComplexPortal; CPX-1015; MET4-MET28-MET32 sulfur metabolism transcription factor complex.
DR   ComplexPortal; CPX-1016; CBF1-MET4-MET28 sulfur metabolism transcription factor complex.
DR   ComplexPortal; CPX-999; MET4-MET28-MET31 sulfur metabolism transcription factor complex.
DR   DIP; DIP-2242N; -.
DR   IntAct; P40573; 6.
DR   MINT; P40573; -.
DR   STRING; 4932.YIR017C; -.
DR   PaxDb; P40573; -.
DR   PRIDE; P40573; -.
DR   EnsemblFungi; YIR017C_mRNA; YIR017C; YIR017C.
DR   GeneID; 854834; -.
DR   KEGG; sce:YIR017C; -.
DR   SGD; S000001456; MET28.
DR   VEuPathDB; FungiDB:YIR017C; -.
DR   eggNOG; ENOG502S9W2; Eukaryota.
DR   HOGENOM; CLU_098757_0_0_1; -.
DR   InParanoid; P40573; -.
DR   BioCyc; YEAST:G3O-31437-MON; -.
DR   PRO; PR:P40573; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40573; protein.
DR   GO; GO:0089713; C:Cbf1-Met4-Met28 complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005667; C:transcription regulator complex; IC:ComplexPortal.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR   GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:SGD.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IMP:SGD.
DR   GO; GO:0042762; P:regulation of sulfur metabolic process; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Activator; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   DNA-binding; Methionine biosynthesis; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..187
FT                   /note="Transcriptional activator of sulfur metabolism
FT                   MET28"
FT                   /id="PRO_0000076520"
FT   DOMAIN          105..168
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          106..136
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          137..151
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
SQ   SEQUENCE   187 AA;  21590 MW;  042976B185EACD34 CRC64;
     MSAKQGWEKK STNIDIASRK GMNVNNLSEH LQNLISSDSE LGSRLLSLLL VSSGNAEELI
     SMINNGQDVS QFKKLREPRK GKVAATTAVV VKEEEAPVST SNELDKIKQE RRRKNTEASQ
     RFRIRKKQKN FENMNKLQNL NTQINKLRDR IEQLNKENEF WKAKLNDINE IKSLKLLNDI
     KRRNMGR
 
 
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