GCR1_YEAST
ID GCR1_YEAST Reviewed; 785 AA.
AC P07261; D6W3U1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glycolytic genes transcriptional activator GCR1;
GN Name=GCR1; Synonyms=SIT3; OrderedLocusNames=YPL075W; ORFNames=LPF10W;
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], AND FUNCTION.
RX PubMed=3547083; DOI=10.1128/mcb.7.2.813-820.1987;
RA Holland M.J., Yokoi T., Holland J.P., Myambo K., Innis M.A.;
RT "The GCR1 gene encodes a positive transcriptional regulator of the enolase
RT and glyceraldehyde-3-phosphate dehydrogenase gene families in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 7:813-820(1987).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-785, AND FUNCTION.
RX PubMed=3025612; DOI=10.1128/mcb.6.11.3774-3784.1986;
RA Baker H.V.;
RT "Glycolytic gene expression in Saccharomyces cerevisiae: nucleotide
RT sequence of GCR1, null mutants, and evidence for expression.";
RL Mol. Cell. Biol. 6:3774-3784(1986).
RN [5]
RP DNA-BINDING.
RX PubMed=1588965; DOI=10.1128/mcb.12.6.2690-2700.1992;
RA Huie M.A., Scott E.W., Drazinic C.M., Lopez M.C., Hornstra I.K., Yang T.P.,
RA Baker H.V.;
RT "Characterization of the DNA-binding activity of GCR1: in vivo evidence for
RT two GCR1-binding sites in the upstream activating sequence of TPI of
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:2690-2700(1992).
RN [6]
RP FUNCTION, AND INTERACTION WITH GCR2.
RX PubMed=1508187; DOI=10.1128/mcb.12.9.3834-3842.1992;
RA Uemura H., Jigami Y.;
RT "Role of GCR2 in transcriptional activation of yeast glycolytic genes.";
RL Mol. Cell. Biol. 12:3834-3842(1992).
RN [7]
RP FUNCTION, AND INTERACTION WITH RAP1.
RX PubMed=8508768; DOI=10.1002/j.1460-2075.1993.tb05897.x;
RA Tornow J., Zeng X., Gao W., Santangelo G.M.;
RT "GCR1, a transcriptional activator in Saccharomyces cerevisiae, complexes
RT with RAP1 and can function without its DNA binding domain.";
RL EMBO J. 12:2431-2437(1993).
RN [8]
RP REVISION OF GENE MODEL.
RX PubMed=7851789; DOI=10.1093/genetics/138.3.973;
RA Tornow J., Santangelo G.M.;
RT "The GCR1 gene of Saccharomyces cerevisiae is a split gene with an
RT unusually long intron.";
RL Genetics 138:973-974(1994).
RN [9]
RP HOMODIMERIZATION.
RX PubMed=8601472; DOI=10.1093/genetics/141.4.1263;
RA Deminoff S.J., Tornow J., Santangelo G.M.;
RT "Unigenic evolution: a novel genetic method localizes a putative leucine
RT zipper that mediates dimerization of the Saccharomyces cerevisiae regulator
RT Gcr1p.";
RL Genetics 141:1263-1274(1995).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=9335588; DOI=10.1093/genetics/147.2.493;
RA Zeng X., Deminoff S.J., Santangelo G.M.;
RT "Specialized Rap1p/Gcr1p transcriptional activation through Gcr1p DNA
RT contacts requires Gcr2p, as does hyperphosphorylation of Gcr1p.";
RL Genetics 147:493-505(1997).
RN [11]
RP FUNCTION, AND HOMODIMERIZATION.
RX PubMed=11333224; DOI=10.1093/genetics/158.1.133;
RA Deminoff S.J., Santangelo G.M.;
RT "Rap1p requires Gcr1p and Gcr2p homodimers to activate ribosomal protein
RT and glycolytic genes, respectively.";
RL Genetics 158:133-143(2001).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447; SER-482; SER-489 AND
RP SER-538, 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).
CC -!- FUNCTION: Transcriptional activator required for the expression of
CC glycolytic and ribosomal genes. Forms a transcriptional activation
CC complex with RAP1, RAP1 providing the specific DNA-binding function and
CC GCR1 providing the activation function. Can also bind itself to DNA to
CC a core 5'-CTTCC-3' sequence (CT box). CT box-binding is not essential,
CC but enhances the activation function of the RAP1-GCR1 complex in
CC promoters that contain both DNA signals (only glycolytic genes). CT
CC box-dependent transcriptional activation requires GCR2.
CC {ECO:0000269|PubMed:11333224, ECO:0000269|PubMed:1508187,
CC ECO:0000269|PubMed:3025612, ECO:0000269|PubMed:3547083,
CC ECO:0000269|PubMed:8508768, ECO:0000269|PubMed:9335588}.
CC -!- SUBUNIT: Homodimer via the leucine-zipper domain. Forms a complex with
CC a GCR2 homodimer. Interacts with RAP1. {ECO:0000269|PubMed:1508187,
CC ECO:0000269|PubMed:8508768}.
CC -!- INTERACTION:
CC P07261; P11938: RAP1; NbExp=2; IntAct=EBI-7463, EBI-14821;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a GCR2-dependent manner.
CC {ECO:0000269|PubMed:9335588}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA66911.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB68263.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M15253; AAA34641.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U41849; AAB68263.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M14145; AAA66911.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006949; DAA11357.1; -; Genomic_DNA.
DR PIR; S61112; S61112.
DR RefSeq; NP_015250.1; NM_001183889.1.
DR AlphaFoldDB; P07261; -.
DR BioGRID; 36105; 90.
DR ComplexPortal; CPX-1200; RAP1-GCR1 transcription activation complex.
DR ComplexPortal; CPX-1229; RAP1-GCR1-GCR2 transcription activation complex.
DR DIP; DIP-2514N; -.
DR IntAct; P07261; 2.
DR STRING; 4932.YPL075W; -.
DR iPTMnet; P07261; -.
DR MaxQB; P07261; -.
DR PaxDb; P07261; -.
DR PRIDE; P07261; -.
DR EnsemblFungi; YPL075W_mRNA; YPL075W; YPL075W.
DR GeneID; 856030; -.
DR KEGG; sce:YPL075W; -.
DR SGD; S000005996; GCR1.
DR VEuPathDB; FungiDB:YPL075W; -.
DR eggNOG; ENOG502QTWE; Eukaryota.
DR HOGENOM; CLU_004933_0_0_1; -.
DR InParanoid; P07261; -.
DR OMA; RENKTIW; -.
DR BioCyc; YEAST:G3O-33982-MON; -.
DR PRO; PR:P07261; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P07261; protein.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IPI: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; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR GO; GO:0034728; P:nucleosome organization; IMP:SGD.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061435; P:positive regulation of transcription from a mobile element promoter; IMP:SGD.
DR GO; GO:0006110; P:regulation of glycolytic process; IC:ComplexPortal.
DR InterPro; IPR022210; TF_GCR1-like.
DR Pfam; PF12550; GCR1_C; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..785
FT /note="Glycolytic genes transcriptional activator GCR1"
FT /id="PRO_0000087445"
FT REGION 267..299
FT /note="Leucine-zipper"
FT REGION 342..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..785
FT /note="DNA-binding"
FT COMPBIAS 481..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 399
FT /note="A -> R (in Ref. 4; AAA66911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 87729 MW; FBC508EB89D57338 CRC64;
MVCTSTSSNF YSIAQYILQS YFKVNVDSLN SLKLVDLIVD QTYPDSLTLR KLNEGATGQP
YDYFNTVSRD ADISKCPIFA LTIFFVIRWS HPNPPISIEN FTTVPLLDSN FISLNSNPLL
YIQNQNPNSN SSVKVSRSQT FEPSKELIDL VFPWLSYLKQ DMLLIDRTNY KLYSLCELFE
FMGRVAIQDL RYLSQHPLLL PNIVTFISKF IPELFQNEEF KGIGSIKNSN NNALNNVTGI
ETQFLNPSTE EVSQKVDSYF MELSKKLTTE NIRLSQEITQ LKADMNSVGN VCNQILLLQR
QLLSGNQAIG SKSENIVSST GGGILILDKN SINSNVLSNL VQSIDPNHSK PNGQAQTHQR
GPKGQSHAQV QSTNSPALAP INMFPSLSNS IQPMLGTLAP QPQDIVQKRK LPLPGSIASA
ATGSPFSPSP VGESPYSKRF KLDDKPTPSQ TALDSLLTKS ISSPRLPLST LANTAVTESF
RSPQQFQHSP DFVVGGSSSS TTENNSKKVN EDSPSSSSKL AERPRLPNND STTSMPESPT
EVAGDDVDRE KPPESSKSEP NDNSPESKDP EKNGKNSNPL GTDADKPVPI SNIHNSTEAA
NSSGTVTKTA PSFPQSSSKF EIINKKDTKA GPNEAIKYKL SRENKTIWDL YAEWYIGLNG
KSSIKKLIEN YGWRRWKVSE DSHFFPTRRI IMDYIETECD RGIKLGRFTN PQQPREDIRK
ILVGDLEKFR INNGLTLNSL SLYFRNLTKN NKEICIFENF KNWNVRSMTE EEKLKYCKRR
HNTPS
