GAL4_YEAST
ID GAL4_YEAST Reviewed; 881 AA.
AC P04386; D6W3C3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Regulatory protein GAL4;
GN Name=GAL4; OrderedLocusNames=YPL248C;
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].
RX PubMed=6366516; DOI=10.1128/mcb.4.2.260-267.1984;
RA Laughon A., Gesteland R.F.;
RT "Primary structure of the Saccharomyces cerevisiae GAL4 gene.";
RL Mol. Cell. Biol. 4:260-267(1984).
RN [2]
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 [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 MUTAGENESIS OF PRO-26, AND ZINC REQUIREMENT.
RX PubMed=3299106; DOI=10.1038/328353a0;
RA Johnston M.;
RT "Genetic evidence that zinc is an essential co-factor in the DNA binding
RT domain of GAL4 protein.";
RL Nature 328:353-355(1987).
RN [5]
RP INTERACTION WITH SRB4.
RX PubMed=9660972; DOI=10.1016/s1097-2765(00)80088-x;
RA Koh S.S., Ansari A.Z., Ptashne M., Young R.A.;
RT "An activator target in the RNA polymerase II holoenzyme.";
RL Mol. Cell 1:895-904(1998).
RN [6]
RP INTERACTION WITH GAL11.
RX PubMed=11478912; DOI=10.1021/bi010011k;
RA Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.;
RT "Evidence that Gal11 protein is a target of the Gal4 activation domain in
RT the mediator.";
RL Biochemistry 40:9421-9427(2001).
RN [7]
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 [8]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694; SER-696; SER-699 AND
RP SER-703, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-65.
RX PubMed=1557122; DOI=10.1038/356408a0;
RA Marmorstein R., Carey M., Ptashne M., Harrison S.C.;
RT "DNA recognition by GAL4: structure of a protein-DNA complex.";
RL Nature 356:408-414(1992).
RN [12]
RP STRUCTURE BY NMR OF ZINC-BINDING REGION.
RX PubMed=2107541; DOI=10.1073/pnas.87.6.2077;
RA Pan T., Coleman J.E.;
RT "GAL4 transcription factor is not a 'zinc finger' but forms a Zn(II)2Cys6
RT binuclear cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2077-2081(1990).
RN [13]
RP STRUCTURE BY NMR OF ZINC-BINDING REGION.
RX PubMed=2021614; DOI=10.1021/bi00231a016;
RA Pan T., Coleman J.E.;
RT "Sequential assignments of the 1H NMR resonances of Zn(II)2 and 113Cd(II)2
RT derivatives of the DNA-binding domain of the GAL4 transcription factor
RT reveal a novel structural motif for specific DNA recognition.";
RL Biochemistry 30:4212-4222(1991).
RN [14]
RP STRUCTURE BY NMR OF ZINC-BINDING REGION.
RX PubMed=2265711; DOI=10.1016/0014-5793(90)80504-c;
RA Gadhavi P.L., Raine A.R.C., Alefounder P.R., Laue E.D.;
RT "Complete assignment of the 1H NMR spectrum and secondary structure of the
RT DNA binding domain of GAL4.";
RL FEBS Lett. 276:49-53(1990).
RN [15]
RP STRUCTURE BY NMR OF ZINC-BINDING REGION.
RX PubMed=1557129; DOI=10.1038/356448a0;
RA Kraulis P.J., Raine A.R.C., Gadhavi P.L., Laue E.D.;
RT "Structure of the DNA-binding domain of zinc GAL4.";
RL Nature 356:448-450(1992).
RN [16]
RP STRUCTURE BY NMR OF ZINC-BINDING REGION.
RX PubMed=1557130; DOI=10.1038/356450a0;
RA Baleja J.D., Marmorstein R., Harrison S.C., Wagner G.;
RT "Solution structure of the DNA-binding domain of Cd2-GAL4 from S.
RT cerevisiae.";
RL Nature 356:450-453(1992).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 8-96 IN COMPLEX WITH ZINC IONS.
RX PubMed=18611375; DOI=10.1016/j.str.2008.03.015;
RA Hong M., Fitzgerald M.X., Harper S., Luo C., Speicher D.W., Marmorstein R.;
RT "Structural basis for dimerization in DNA recognition by Gal4.";
RL Structure 16:1019-1026(2008).
CC -!- FUNCTION: This protein is a positive regulator for the gene expression
CC of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and
CC MEL1 which code for the enzymes used to convert galactose to glucose.
CC It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the
CC upstream activating sequence (UAS-G) of these genes.
CC -!- SUBUNIT: Binds DNA as a homodimer. Interacts directly with the mediator
CC subunits GAL11/MED15 and SRB4/MED17. {ECO:0000269|PubMed:11478912,
CC ECO:0000269|PubMed:9660972}.
CC -!- INTERACTION:
CC P04386; P04386: GAL4; NbExp=3; IntAct=EBI-4407660, EBI-4407660;
CC P04386; P04387: GAL80; NbExp=3; IntAct=EBI-4407660, EBI-2061197;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: the 9aaTAD motif (residues 862 to 870) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000269|PubMed:17467953}.
CC -!- PTM: Association between GAL11 and GAL4 may serve to expedite
CC phosphorylation of GAL4.
CC -!- MISCELLANEOUS: Present with 166 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K01486; AAA34626.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91596.1; -; Genomic_DNA.
DR EMBL; Z73604; CAA97969.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11189.1; -; Genomic_DNA.
DR PIR; A05022; RGBYG4.
DR RefSeq; NP_015076.1; NM_001184062.1.
DR PDB; 1AW6; NMR; -; A=1-43.
DR PDB; 1D66; X-ray; 2.70 A; A/B=1-65.
DR PDB; 1HBW; NMR; -; A/B=50-106.
DR PDB; 3BTS; X-ray; 2.70 A; E/F=854-874.
DR PDB; 3COQ; X-ray; 2.40 A; A/B=8-96.
DR PDBsum; 1AW6; -.
DR PDBsum; 1D66; -.
DR PDBsum; 1HBW; -.
DR PDBsum; 3BTS; -.
DR PDBsum; 3COQ; -.
DR AlphaFoldDB; P04386; -.
DR BMRB; P04386; -.
DR SMR; P04386; -.
DR BioGRID; 35915; 176.
DR ComplexPortal; CPX-1044; GAL4-GAL80 transcription repressor complex.
DR DIP; DIP-593N; -.
DR IntAct; P04386; 6.
DR MINT; P04386; -.
DR STRING; 4932.YPL248C; -.
DR iPTMnet; P04386; -.
DR PaxDb; P04386; -.
DR PRIDE; P04386; -.
DR EnsemblFungi; YPL248C_mRNA; YPL248C; YPL248C.
DR GeneID; 855828; -.
DR KEGG; sce:YPL248C; -.
DR SGD; S000006169; GAL4.
DR VEuPathDB; FungiDB:YPL248C; -.
DR eggNOG; ENOG502QSMN; Eukaryota.
DR HOGENOM; CLU_008599_2_0_1; -.
DR InParanoid; P04386; -.
DR OMA; SYPFIHE; -.
DR BioCyc; YEAST:G3O-34134-MON; -.
DR EvolutionaryTrace; P04386; -.
DR PRO; PR:P04386; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P04386; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006012; P:galactose metabolic process; IMP:SGD.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IDA:SGD.
DR GO; GO:0000431; P:regulation of transcription from RNA polymerase II promoter by galactose; IMP:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd14654; ZIP_Gal4; 1.
DR DisProt; DP02132; -.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005600; Gal4_dimer_dom.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF03902; Gal4_dimer; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Carbohydrate metabolism; DNA-binding;
KW Galactose metabolism; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..881
FT /note="Regulatory protein GAL4"
FT /id="PRO_0000114951"
FT DNA_BIND 11..38
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 723..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 862..870
FT /note="9aaTAD"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611375,
FT ECO:0007744|PDB:3COQ"
FT MOD_RES 694
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 26
FT /note="P->L: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:3299106"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:3COQ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3COQ"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:3COQ"
FT HELIX 51..71
FT /evidence="ECO:0007829|PDB:3COQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3COQ"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:3COQ"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:3COQ"
SQ SEQUENCE 881 AA; 99403 MW; 29D7FF68B0B05880 CRC64;
MKLLSSIEQA CDICRLKKLK CSKEKPKCAK CLKNNWECRY SPKTKRSPLT RAHLTEVESR
LERLEQLFLL IFPREDLDMI LKMDSLQDIK ALLTGLFVQD NVNKDAVTDR LASVETDMPL
TLRQHRISAT SSSEESSNKG QRQLTVSIDS AAHHDNSTIP LDFMPRDALH GFDWSEEDDM
SDGLPFLKTD PNNNGFFGDG SLLCILRSIG FKPENYTNSN VNRLPTMITD RYTLASRSTT
SRLLQSYLNN FHPYCPIVHS PTLMMLYNNQ IEIASKDQWQ ILFNCILAIG AWCIEGESTD
IDVFYYQNAK SHLTSKVFES GSIILVTALH LLSRYTQWRQ KTNTSYNFHS FSIRMAISLG
LNRDLPSSFS DSSILEQRRR IWWSVYSWEI QLSLLYGRSI QLSQNTISFP SSVDDVQRTT
TGPTIYHGII ETARLLQVFT KIYELDKTVT AEKSPICAKK CLMICNEIEE VSRQAPKFLQ
MDISTTALTN LLKEHPWLSF TRFELKWKQL SLIIYVLRDF FTNFTQKKSQ LEQDQNDHQS
YEVKRCSIML SDAAQRTVMS VSSYMDNHNV TPYFAWNCSY YLFNAVLVPI KTLLSNSKSN
AENNETAQLL QQINTVLMLL KKLATFKIQT CEKYIQVLEE VCAPFLLSQC AIPLPHISYN
NSNGSAIKNI VGSATIAQYP TLPEENVNNI SVKYVSPGSV GPSPVPLKSG ASFSDLVKLL
SNRPPSRNSP VTIPRSTPSH RSVTPFLGQQ QQLQSLVPLT PSALFGGANF NQSGNIADSS
LSFTFTNSSN GPNLITTQTN SQALSQPIAS SNVHDNFMNN EITASKIDDG NNSKPLSPGW
TDQTAYNAFG ITTGMFNTTT MDDVYNYLFD DEDTPPNPKK E
