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Transcriptional activator of sulfur metabolism MET4 (Methionine-requiring protein 4)

 MET4_YEAST              Reviewed;         672 AA.
P32389; D6W176;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 2.
22-NOV-2017, entry version 169.
RecName: Full=Transcriptional activator of sulfur metabolism MET4;
AltName: Full=Methionine-requiring protein 4;
Name=MET4; OrderedLocusNames=YNL103W; ORFNames=N2177;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=1549123; DOI=10.1128/MCB.12.4.1719;
Thomas D., Jacquemin I., Surdin-Kerjan Y.;
"MET4, a leucine zipper protein, and centromere-binding factor 1 are
both required for transcriptional activation of sulfur metabolism in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 12:1719-1727(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=8446029; DOI=10.1111/j.1365-2958.1993.tb01113.x;
Mountain H.A., Bystroem A.S., Korch C.;
"The general amino acid control regulates MET4, which encodes a
methionine-pathway-specific transcriptional activator of Saccharomyces
cerevisiae.";
Mol. Microbiol. 7:215-228(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8701612;
DOI=10.1002/(SICI)1097-0061(19960330)12:4<403::AID-YEA923>3.3.CO;2-8;
Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
"The sequence of a 21.3 kb DNA fragment from the left arm of yeast
chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open
reading frames.";
Yeast 12:403-409(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
FUNCTION, AND FUNCTIONAL REGIONS.
PubMed=7799928; DOI=10.1128/MCB.15.1.208;
Kuras L., Thomas D.;
"Functional analysis of Met4, a yeast transcriptional activator
responsive to S-adenosylmethionine.";
Mol. Cell. Biol. 15:208-216(1995).
[7]
INTERACTION WITH MET30.
PubMed=8524217; DOI=10.1128/MCB.15.12.6526;
Thomas D., Kuras L., Barbey R., Cherest H., Blaiseau P.L.,
Surdin-Kerjan Y.;
"Met30p, a yeast transcriptional inhibitor that responds to S-
adenosylmethionine, is an essential protein with WD40 repeats.";
Mol. Cell. Biol. 15:6526-6534(1995).
[8]
FUNCTION, AND SUBUNIT.
PubMed=8665859;
Kuras L., Cherest H., Surdin-Kerjan Y., Thomas D.;
"A heteromeric complex containing the centromere binding factor 1 and
two basic leucine zipper factors, Met4 and Met28, mediates the
transcription activation of yeast sulfur metabolism.";
EMBO J. 15:2519-2529(1996).
[9]
FUNCTION, AND SUBUNIT.
PubMed=9171357; DOI=10.1093/emboj/16.9.2441;
Kuras L., Barbey R., Thomas D.;
"Assembly of a bZIP-bHLH transcription activation complex: formation
of the yeast Cbf1-Met4-Met28 complex is regulated through Met28
stimulation of Cbf1 DNA binding.";
EMBO J. 16:2441-2451(1997).
[10]
FUNCTION, AND SUBUNIT.
PubMed=9799240; DOI=10.1093/emboj/17.21.6327;
Blaiseau P.L., Thomas D.;
"Multiple transcriptional activation complexes tether the yeast
activator Met4 to DNA.";
EMBO J. 17:6327-6336(1998).
[11]
FUNCTION, AND SUBUNIT.
PubMed=10637232; DOI=10.1093/emboj/19.2.282;
Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D.;
"Feedback-regulated degradation of the transcriptional activator Met4
is triggered by the SCF(Met30) complex.";
EMBO J. 19:282-294(2000).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION, ACTIVATION BY CADMIUM AND ARSENIC, AND INACTIVATION BY
HYDROGEN PEROXIDE.
PubMed=15689486; DOI=10.1091/mbc.E04-12-1130;
Yen J.L., Su N.Y., Kaiser P.;
"The yeast ubiquitin ligase SCFMet30 regulates heavy metal response.";
Mol. Biol. Cell 16:1872-1882(2005).
[15]
INTERACTION WITH MET30.
PubMed=15883825; DOI=10.1007/s00438-005-1137-6;
Brunson L.E., Dixon C., LeFebvre A., Sun L., Mathias N.;
"Identification of residues in the WD-40 repeat motif of the F-box
protein Met30p required for interaction with its substrate Met4p.";
Mol. Genet. Genomics 273:361-370(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND SER-564, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Positive trans-acting factor capable of stimulating the
transcription of the MET genes from the methionine biosynthetic
pathway. MET4, MET28 and CBF1 are required for full induction of
MET25 and MET16 gene transcription. MET4 controls as well the
derepression of MET6. Required for the transcription of genes
necessary for sulfur amino acid biosynthesis. Involved in the
transcription activation of MET28 and MET30. Required for MET3
gene expression via assembly of the MET4-MET28-MET31 and MET4-
MET28-MET32 complexes. Involved in response to cadmium and
arsenic. Cadmium-activated MET4 also induces glutathione
biosynthesis. {ECO:0000269|PubMed:10637232,
ECO:0000269|PubMed:1549123, ECO:0000269|PubMed:15689486,
ECO:0000269|PubMed:7799928, ECO:0000269|PubMed:8446029,
ECO:0000269|PubMed:8665859, ECO:0000269|PubMed:9171357,
ECO:0000269|PubMed:9799240}.
-!- SUBUNIT: Interacts with MET30. Tethered to DNA through two
alternate complexes associating MET4 with MET28 and either MET31
or MET32. Interacts with MET28 and CBF1 through its leucine zipper
to form a heteromeric complex. {ECO:0000269|PubMed:10637232,
ECO:0000269|PubMed:15883825, ECO:0000269|PubMed:8524217,
ECO:0000269|PubMed:8665859, ECO:0000269|PubMed:9171357,
ECO:0000269|PubMed:9799240}.
-!- INTERACTION:
P40573:MET28; NbExp=3; IntAct=EBI-10757, EBI-11503;
P39014:MET30; NbExp=7; IntAct=EBI-10757, EBI-11507;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: Regulated by the general amino acid control.
{ECO:0000269|PubMed:8446029}.
-!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Transcriptional activation function is inhibited by
the elevation of intracellular S-adenosylmethionine (AdoMet), but
is activated by cadmium and arsenic which leads to phosphorylation
and prevents ubiquitination. Inactivation by oxidative stress
induced by hydrogen peroxide promotes ubiquitination.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA34776.1; Type=Frameshift; Positions=659; Evidence={ECO:0000305};
Sequence=CAA78109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA90523.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M84455; AAA34776.1; ALT_FRAME; Genomic_DNA.
EMBL; Z12126; CAA78109.1; ALT_INIT; Genomic_DNA.
EMBL; Z50161; CAA90523.1; ALT_INIT; Genomic_DNA.
EMBL; Z71379; CAA95979.1; -; Genomic_DNA.
EMBL; BK006947; DAA10442.1; -; Genomic_DNA.
PIR; S63043; S63043.
RefSeq; NP_014296.4; NM_001182941.3.
ProteinModelPortal; P32389; -.
BioGrid; 35720; 43.
DIP; DIP-2241N; -.
IntAct; P32389; 11.
MINT; MINT-438010; -.
STRING; 4932.YNL103W; -.
iPTMnet; P32389; -.
MaxQB; P32389; -.
PRIDE; P32389; -.
TopDownProteomics; P32389; -.
GeneID; 855620; -.
KEGG; sce:YNL103W; -.
EuPathDB; FungiDB:YNL103W; -.
SGD; S000005047; MET4.
InParanoid; P32389; -.
OrthoDB; EOG092C5FM7; -.
BioCyc; YEAST:G3O-33131-MONOMER; -.
PRO; PR:P32389; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0089713; C:Cbf1-Met4-Met28 complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IPI:SGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:SGD.
GO; GO:0046685; P:response to arsenic-containing substance; IDA:SGD.
GO; GO:0046686; P:response to cadmium ion; IDA:SGD.
GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
1: Evidence at protein level;
Activator; Amino-acid biosynthesis; Coiled coil; Complete proteome;
Cysteine biosynthesis; DNA-binding; Methionine biosynthesis; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 672 Transcriptional activator of sulfur
metabolism MET4.
/FTId=PRO_0000076519.
DOMAIN 586 649 bZIP.
REGION 95 144 Transcriptional activation.
REGION 188 235 Inhibitory region; AdoMet responsiveness;
required for interaction with MET30.
REGION 312 375 Auxiliary; required for high
transcriptional activity under
nonrepressive growth conditions.
REGION 375 403 Required for interaction with MET31 and
MET32.
REGION 601 612 Basic motif. {ECO:0000250}.
REGION 614 642 Leucine-zipper. {ECO:0000250}.
COILED 609 648 {ECO:0000255}.
COMPBIAS 53 57 Poly-Ser.
COMPBIAS 106 242 Asn-rich.
MOD_RES 416 416 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
CONFLICT 441 442 RG -> AA (in Ref. 1; AAA34776 and 4;
DAA10442). {ECO:0000305}.
SEQUENCE 672 AA; 74373 MW; D65745E1FA40C09D CRC64;
MKQEQSHEGD SYSTEFINLF GKDTATHPSS NNGANNNGMG STNSLDQFVA TASSSSSLVT
SSENRRPLIG DVTNRGNTNL YDHAVTPEIL LEQLAYVDNF IPSLDNEFSN VDWNVNTTHN
NANNNGADTF SSINANPFDL DEQLAIELSA FADDSFIFPD EDKPSNNNNN SNNGNDDHSN
HDVLHEDPST NNRQRNPHFL TQRRNTFLTS QYDQSKSRFS SKNKRNGNNG ETNNFGDNMQ
NNHPFEPNFM GSPSQFPADA TNMTSIDHGG FTNVDITSTE NNTTGDNGVD ALSNLLHRTT
HTPNRSSPLS NVTSAQNSSS QQRKHSESKV DSNSDNNSSN KAPNITVPDY SIIPTSVLVT
LLPRVNVPNG AYNSLISAGF DNDQIDAIAA IMAYHHQKKI RENNSNNNKN INTNDSQEAP
ILKNINELLS VLIPPSPAET RGPTTLSTSP SFNEHGVVAE ASFLSSILEL GIKHPKSNNI
HNQRQPSRND HKISRESDGN NGNDNVHHNN AVIKSSTTRG DEIAKIRSEP TLNASSSDHK
ENSLKRSHSG DLKNKKVPVD RKYSDNEDDE YDDADLHGFE KKQLIKKELG DDDEDLLIQS
KKSHQKKKLK EKELESSIHE LTEIAASLQK RIHTLETENK LLKNLVLSSG ETEGIKKAES
LKKQIFEKVQ KE


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