GAL80_YEAST
ID GAL80_YEAST Reviewed; 435 AA.
AC P04387; D6VZC4;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Galactose/lactose metabolism regulatory protein GAL80;
GN Name=GAL80; OrderedLocusNames=YML051W; ORFNames=YM9827.01, YM9958.12;
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=6393054; DOI=10.1093/nar/12.24.9287;
RA Nogi Y., Fukasawa T.;
RT "Nucleotide sequence of the yeast regulatory gene GAL80.";
RL Nucleic Acids Res. 12:9287-9298(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 PROTEIN SEQUENCE OF 29-33; 162-171 AND 410-416, FUNCTION, SUBUNIT, AND
RP ACETYLATION AT MET-1.
RX PubMed=1985957; DOI=10.1016/s0021-9258(17)35226-2;
RA Yun S.-J., Hiraoka Y., Nishizawa M., Takio K., Titani K., Nogi Y.,
RA Fukasawa T.;
RT "Purification and characterization of the yeast negative regulatory protein
RT GAL80.";
RL J. Biol. Chem. 266:693-697(1991).
RN [5]
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 [6]
RP 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).
CC -!- FUNCTION: This protein is a negative regulator for the gene expression
CC of the lactose/galactose metabolic genes. It binds to GAL4 and so
CC blocks transcriptional activation by it, in the absence of an inducing
CC sugar. {ECO:0000269|PubMed:1985957}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1985957}.
CC -!- INTERACTION:
CC P04387; P04385: GAL1; NbExp=2; IntAct=EBI-2061197, EBI-7272;
CC P04387; P13045: GAL3; NbExp=5; IntAct=EBI-2061197, EBI-7282;
CC P04387; P04386: GAL4; NbExp=3; IntAct=EBI-2061197, EBI-4407660;
CC P04387; P04387: GAL80; NbExp=7; IntAct=EBI-2061197, EBI-2061197;
CC -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To K.lactis GAL80. {ECO:0000305}.
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DR EMBL; X01667; CAA25827.1; -; Genomic_DNA.
DR EMBL; Z46729; CAA86725.1; -; Genomic_DNA.
DR EMBL; Z47816; CAA87823.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09848.1; -; Genomic_DNA.
DR PIR; A03606; RGBYG8.
DR RefSeq; NP_013661.1; NM_001182409.1.
DR PDB; 3BTS; X-ray; 2.70 A; A/B=1-435.
DR PDB; 3BTU; X-ray; 2.85 A; A/B/C/D/E/F=1-435.
DR PDB; 3BTV; X-ray; 2.10 A; A/B=1-435.
DR PDB; 3V2U; X-ray; 2.10 A; A/B=1-435.
DR PDBsum; 3BTS; -.
DR PDBsum; 3BTU; -.
DR PDBsum; 3BTV; -.
DR PDBsum; 3V2U; -.
DR AlphaFoldDB; P04387; -.
DR SMR; P04387; -.
DR BioGRID; 35117; 222.
DR ComplexPortal; CPX-1042; GAL3-GAL80 transcription regulation complex.
DR ComplexPortal; CPX-1043; GAL1-GAL80 transcription regulation complex.
DR ComplexPortal; CPX-1044; GAL4-GAL80 transcription repressor complex.
DR DIP; DIP-594N; -.
DR IntAct; P04387; 37.
DR MINT; P04387; -.
DR STRING; 4932.YML051W; -.
DR iPTMnet; P04387; -.
DR MaxQB; P04387; -.
DR PaxDb; P04387; -.
DR PRIDE; P04387; -.
DR EnsemblFungi; YML051W_mRNA; YML051W; YML051W.
DR GeneID; 854954; -.
DR KEGG; sce:YML051W; -.
DR SGD; S000004515; GAL80.
DR VEuPathDB; FungiDB:YML051W; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_25_0_1; -.
DR InParanoid; P04387; -.
DR OMA; VDALCYV; -.
DR BioCyc; YEAST:G3O-32648-MON; -.
DR EvolutionaryTrace; P04387; -.
DR PRO; PR:P04387; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P04387; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019210; F:kinase inhibitor activity; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0006012; P:galactose metabolic process; IMP:SGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IMP:ComplexPortal.
DR GO; GO:0000431; P:regulation of transcription from RNA polymerase II promoter by galactose; IMP:ComplexPortal.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Carbohydrate metabolism;
KW Direct protein sequencing; DNA-binding; Galactose metabolism;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..435
FT /note="Galactose/lactose metabolism regulatory protein
FT GAL80"
FT /id="PRO_0000087427"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1985957"
FT CONFLICT 101
FT /note="E -> D (in Ref. 1; CAA25827)"
FT /evidence="ECO:0000305"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3V2U"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3BTS"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3V2U"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3V2U"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 360..376
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:3BTV"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3BTV"
FT HELIX 402..421
FT /evidence="ECO:0007829|PDB:3BTV"
FT TURN 428..432
FT /evidence="ECO:0007829|PDB:3BTV"
SQ SEQUENCE 435 AA; 48323 MW; 1492473684F3894C CRC64;
MDYNKRSSVS TVPNAAPIRV GFVGLNAAKG WAIKTHYPAI LQLSSQFQIT ALYSPKIETS
IATIQRLKLS NATAFPTLES FASSSTIDMI VIAIQVASHY EVVMPLLEFS KNNPNLKYLF
VEWALACSLD QAESIYKAAA ERGVQTIISL QGRKSPYILR AKELISQGYI GDINSIEIAG
NGGWYGYERP VKSPKYIYEI GNGVDLVTTT FGHTIDILQY MTSSYFSRIN AMVFNNIPEQ
ELIDERGNRL GQRVPKTVPD HLLFQGTLLN GNVPVSCSFK GGKPTKKFTK NLVIDIHGTK
GDLKLEGDAG FAEISNLVLY YSGTRANDFP LANGQQAPLD PGYDAGKEIM EVYHLRNYNA
IVGNIHRLYQ SISDFHFNTK KIPELPSQFV MQGFDFEGFP TLMDALILHR LIESVYKSNM
MGSTLNVSNI SHYSL
