ADR1_YEAST
ID ADR1_YEAST Reviewed; 1323 AA.
AC P07248; D6VSJ9; Q04919;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Regulatory protein ADR1;
GN Name=ADR1; OrderedLocusNames=YDR216W; ORFNames=YD8142.16, YD8142B.08;
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=3515197; DOI=10.1038/320283a0;
RA Hartshorne T.A., Blumberg H., Young E.T.;
RT "Sequence homology of the yeast regulatory protein ADR1 with Xenopus
RT transcription factor TFIIIA.";
RL Nature 320:283-287(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND THR-327, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-188; THR-193;
RP SER-230; SER-258; THR-259; SER-299 AND SER-325, AND IDENTIFICATION BY MASS
RP 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 [8]
RP STRUCTURE BY NMR OF ZINC-FINGERS.
RX PubMed=3047872; DOI=10.1126/science.3047872;
RA Parraga G., Horvath S.J., Eisen A., Taylor W.E., Hood L., Young E.T.,
RA Klevit R.E.;
RT "Zinc-dependent structure of a single-finger domain of yeast ADR1.";
RL Science 241:1489-1492(1988).
RN [9]
RP STRUCTURE BY NMR OF 131-159.
RX PubMed=2012802; DOI=10.1021/bi00228a003;
RA Xu R.X., Horvath S.J., Klevit R.E.;
RT "ADR1a, a zinc finger peptide, exists in two folded conformations.";
RL Biochemistry 30:3365-3371(1991).
RN [10]
RP STRUCTURE BY NMR OF 102-161.
RX PubMed=10331877; DOI=10.1038/8283;
RA Bowers P.M., Schaufler L.E., Klevit R.E.;
RT "A folding transition and novel zinc finger accessory domain in the
RT transcription factor ADR1.";
RL Nat. Struct. Biol. 6:478-485(1999).
RN [11]
RP MUTAGENESIS.
RX PubMed=3112579; DOI=10.1038/328443a0;
RA Blumberg H., Eisen A., Sledziewski A., Bader D., Young E.T.;
RT "Two zinc fingers of a yeast regulatory protein shown by genetic evidence
RT to be essential for its function.";
RL Nature 328:443-445(1987).
RN [12]
RP MUTAGENESIS.
RX PubMed=1924382; DOI=10.1073/pnas.88.20.9188;
RA Thukral S.K., Morrison M.L., Young E.T.;
RT "Alanine scanning site-directed mutagenesis of the zinc fingers of
RT transcription factor ADR1: residues that contact DNA and that
RT transactivate.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9188-9192(1991).
RN [13]
RP MUTAGENESIS.
RX PubMed=1588970; DOI=10.1128/mcb.12.6.2784-2792.1992;
RA Thukral S.K., Morrison M.L., Young E.T.;
RT "Mutations in the zinc fingers of ADR1 that change the specificity of DNA
RT binding and transactivation.";
RL Mol. Cell. Biol. 12:2784-2792(1992).
RN [14]
RP MUTAGENESIS, AND PHOSPHORYLATION AT SER-230.
RX PubMed=1549108; DOI=10.1128/mcb.12.4.1507-1514.1992;
RA Denis C.L., Fontaine S.C., Chase D., Kemp B.E., Bemis L.T.;
RT "ADR1c mutations enhance the ability of ADR1 to activate transcription by a
RT mechanism that is independent of effects on cyclic AMP-dependent protein
RT kinase phosphorylation of Ser-230.";
RL Mol. Cell. Biol. 12:1507-1514(1992).
RN [15]
RP MUTAGENESIS.
RX PubMed=1448103; DOI=10.1128/mcb.12.12.5758-5767.1992;
RA Camier S., Kacherovsky N., Young E.T.;
RT "A mutation outside the two zinc fingers of ADR1 can suppress defects in
RT either finger.";
RL Mol. Cell. Biol. 12:5758-5767(1992).
RN [16]
RP MUTAGENESIS.
RX PubMed=8132676; DOI=10.1016/s0021-9258(17)37118-1;
RA Cook W.J., Mosley S.P., Audino D.C., Mullaney D.L., Rovelli A., Stewart G.,
RA Denis C.L.;
RT "Mutations in the zinc-finger region of the yeast regulatory protein ADR1
RT affect both DNA binding and transcriptional activation.";
RL J. Biol. Chem. 269:9374-9379(1994).
CC -!- FUNCTION: Required for transcriptional activation of glucose-
CC repressible alcohol dehydrogenase (ADH2).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does
CC not affect DNA binding but appears to prevent transcription of ADH2
CC during glucose repression. {ECO:0000269|PubMed:1549108}.
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DR EMBL; U28414; AAA73863.1; -; Genomic_DNA.
DR EMBL; Z48612; CAA88496.1; -; Genomic_DNA.
DR EMBL; Z68194; CAA92359.1; -; Genomic_DNA.
DR EMBL; Z68195; CAA92367.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12059.1; -; Genomic_DNA.
DR PIR; A24534; A24534.
DR RefSeq; NP_010502.3; NM_001180524.3.
DR PDB; 1ARD; NMR; -; A=102-130.
DR PDB; 1ARE; NMR; -; A=102-130.
DR PDB; 1ARF; NMR; -; A=102-130.
DR PDB; 1PAA; NMR; -; A=130-159.
DR PDB; 2ADR; NMR; -; A=102-161.
DR PDB; 5A7U; EM; 4.80 A; A=130-158.
DR PDBsum; 1ARD; -.
DR PDBsum; 1ARE; -.
DR PDBsum; 1ARF; -.
DR PDBsum; 1PAA; -.
DR PDBsum; 2ADR; -.
DR PDBsum; 5A7U; -.
DR AlphaFoldDB; P07248; -.
DR BMRB; P07248; -.
DR SMR; P07248; -.
DR BioGRID; 32269; 150.
DR DIP; DIP-7N; -.
DR IntAct; P07248; 32.
DR MINT; P07248; -.
DR STRING; 4932.YDR216W; -.
DR iPTMnet; P07248; -.
DR MaxQB; P07248; -.
DR PaxDb; P07248; -.
DR PRIDE; P07248; -.
DR EnsemblFungi; YDR216W_mRNA; YDR216W; YDR216W.
DR GeneID; 851802; -.
DR KEGG; sce:YDR216W; -.
DR SGD; S000002624; ADR1.
DR VEuPathDB; FungiDB:YDR216W; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_006588_0_0_1; -.
DR InParanoid; P07248; -.
DR OMA; ATPNFKL; -.
DR BioCyc; YEAST:G3O-29797-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; P07248; -.
DR PRO; PR:P07248; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P07248; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPI:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IDA:SGD.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IPI:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0061425; P:positive regulation of ethanol catabolic process by positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061429; P:positive regulation of transcription from RNA polymerase II promoter by oleic acid; IMP:SGD.
DR GO; GO:0061410; P:positive regulation of transcription from RNA polymerase II promoter in response to ethanol; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR DisProt; DP00077; -.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1323
FT /note="Regulatory protein ADR1"
FT /id="PRO_0000046801"
FT ZN_FING 104..126
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..155
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 175..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 230
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:1549108,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:19779198"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 106
FT /note="C->Y: Suppresses activity."
FT MUTAGEN 109
FT /note="C->Y: Suppresses activity."
FT MUTAGEN 114
FT /note="A->V: Lowers activity."
FT MUTAGEN 118
FT /note="H->Y: Suppresses activity."
FT MUTAGEN 122
FT /note="H->Y: Suppresses activity."
FT MUTAGEN 134
FT /note="C->Y: Suppresses activity."
FT MUTAGEN 142
FT /note="T->I: Lowers activity."
FT CONFLICT 1216
FT /note="D -> H (in Ref. 1; AAA73863)"
FT /evidence="ECO:0000305"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1ARF"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1ARD"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1ARF"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:1ARD"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2ADR"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1PAA"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1PAA"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:1PAA"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2ADR"
SQ SEQUENCE 1323 AA; 150941 MW; EE807290EA6CC5C2 CRC64;
MANVEKPNDC SGFPVVDLNS CFSNGFNNEK QEIEMETDDS PILLMSSSAS RENSNTFSVI
QRTPDGKIIT TNNNMNSKIN KQLDKLPENL RLNGRTPSGK LRSFVCEVCT RAFARQEHLK
RHYRSHTNEK PYPCGLCNRC FTRRDLLIRH AQKIHSGNLG ETISHTKKVS RTITKARKNS
ASSVKFQTPT YGTPDNGNFL NRTTANTRRK ASPEANVKRK YLKKLTRRAS FSAQSASSYA
LPDQSSLEQH PKDRVKFSTP ELVPLDLKNP ELDSSFDLNM NLDLNLNLDS NFNIALNRSD
SSGSTMNLDY KLPESANNYT YSSGSPTRAY VGANTNSKNA SFNDADLLSS SYWIKAYNDH
LFSVSESDET SPMNSELNDT KLIVPDFKST IHHLKDSRSS SWTVAIDNNS NNNKVSDNQP
DFVDFQELLD NDTLGNDLLE TTAVLKEFEL LHDDSVSATA TSNEIDLSHL NLSNSPISPH
KLIYKNKEGT NDDMLISFGL DHPSNREDDL DKLCNMTRDV QAIFSQYLKG EESKRSLEDF
LSTSNRKEKP DSGNYTFYGL DCLTLSKISR ALPASTVNNN QPSHSIESKL FNEPMRNMCI
KVLRYYEKFS HDSSESVMDS NPNLLSKELL MPAVSELNEY LDLFKNNFLP HFPIIHPSLL
DLDLDSLQRY TNEDGYDDAE NAQLFDRLSQ GTDKEYDYEH YQILSISKIV CLPLFMATFG
SLHKFGYKSQ TIELYEMSRR ILHSFLETKR RCRSTTVNDS YQNIWLMQSL ILSFMFALVA
DYLEKIDSSL MKRQLSALCS TIRSNCLPTI SANSEKSINN NNEPLTFGSP LQYIIFESKI
RCTLMAYDFC QFLKCFFHIK FDLSIKEKDV ETIYIPDNES KWASESIICN GHVVQKQNFY
DFRNFYYSFT YGHLHSIPEF LGSSMIYYEY DLRKGTKSHV FLDRIDTKRL ERSLDTSSYG
NDNMAATNKN IAILIDDTII LKNNLMSMRF IKQIDRSFTE KVRKGQIAKI YDSFLNSVRL
NFLKNYSVEV LCEFLVALNF SIRNISSLYV EEESDCSQRM NSPELPRIHL NNQALSVFNL
QGYYYCFILI IKFLLDFEAT PNFKLLRIFI ELRSLANSIL LPTLSRLYPQ EFSGFPDVVF
TQQFINKDNG MLVPGLSANE HHNGASAAVK TKLAKKINVE GLAMFINEIL VNSFNDTSFL
NMEDPIRNEF SFDNGDRAVT DLPRSAHFLS DTGLEGINFS GLNDSHQTVS TLNLLRYGEN
HSSKHKNGGK GQGFAEKYQL SLKYVTIAKL FFTNVKENYI HCHMLDKMAS DFHTLENHLK
GNS
