ARO80_YEAST
ID ARO80_YEAST Reviewed; 950 AA.
AC Q04052; D6VT51;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transcriptional activator ARO80;
GN Name=ARO80; OrderedLocusNames=YDR421W; ORFNames=D9461.10;
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 [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 [2]
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 [3]
RP CHARACTERIZATION.
RX PubMed=10207060; DOI=10.1128/mcb.19.5.3360;
RA Iraqui I., Vissers S., Andre B., Urrestarazu A.;
RT "Transcriptional induction by aromatic amino acids in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 19:3360-3371(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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].
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).
CC -!- FUNCTION: Transcription activator required for the expression of genes
CC involved in the catabolism of aromatic amino acids such as the aromatic
CC aminotransferase II ARO9 and the phenylpyruvate decarboxylase ARO10.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U33007; AAB64863.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12261.1; -; Genomic_DNA.
DR PIR; S69704; S69704.
DR RefSeq; NP_010709.1; NM_001180729.1.
DR AlphaFoldDB; Q04052; -.
DR SMR; Q04052; -.
DR BioGRID; 32480; 60.
DR DIP; DIP-1012N; -.
DR IntAct; Q04052; 2.
DR MINT; Q04052; -.
DR STRING; 4932.YDR421W; -.
DR iPTMnet; Q04052; -.
DR MaxQB; Q04052; -.
DR PaxDb; Q04052; -.
DR PRIDE; Q04052; -.
DR EnsemblFungi; YDR421W_mRNA; YDR421W; YDR421W.
DR GeneID; 852031; -.
DR KEGG; sce:YDR421W; -.
DR SGD; S000002829; ARO80.
DR VEuPathDB; FungiDB:YDR421W; -.
DR eggNOG; ENOG502QQTI; Eukaryota.
DR GeneTree; ENSGT00940000176681; -.
DR HOGENOM; CLU_005663_0_0_1; -.
DR InParanoid; Q04052; -.
DR OMA; AQDMGFM; -.
DR BioCyc; YEAST:G3O-29962-MON; -.
DR PRO; PR:Q04052; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04052; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009074; P:aromatic amino acid family catabolic process; IMP:SGD.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; DNA-binding; Metal-binding; Nucleus;
KW Phenylalanine catabolism; Reference proteome; Transcription;
KW Transcription regulation; Tryptophan catabolism; Tyrosine catabolism; Zinc.
FT CHAIN 1..950
FT /note="Transcriptional activator ARO80"
FT /id="PRO_0000114938"
FT DNA_BIND 25..58
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 108205 MW; 3F86083C127D32A7 CRC64;
MSAKKRPSGN AAFELPKRRR TYQACISCRS RKVKCDLGPV DNPHDPPCAR CKRELKKCIF
SSNKGTSNDL PPNSINAISL PSLGKSKQEI QNDSTSPILS DVPLSRKGIS SEKSFKSEGM
KWKLELSSMQ NALEFLAQAA GTVAKEGAKE IIKEKSTTPK PLKSSLDATN KSATDEGLKR
LSKSDSTNTL YENTADMLNH TLNTNRKTSQ LMEEIGKVRP PPTRKIDDFD YIGPDSLLTK
EEAIELIEAF FLTMHPFFPN IPLQLHDPKE LAEYPILFCA ILTVSARYHP FDTLGLDNGE
DGMRHIEVHD KLWVYCQKLI SQTIWAEAST RSIGTVLAFI IFTEWNPRSI HYKWSDYAND
PELNNVNARG SKNISTRKDE EGLTGVGAIR RSDRMSWMLT GSAVRLAQDM GFIENSSKVF
IVTHISETTS AMNMNQRSLL AESFSVLNLN LGKIENDGNE SNEDYLGNEK FYLNEILPDE
ESKLRWKRVF ENSENDHDNE KNFLTDWERE FLNDEYVLYY SNKKDDTNLA QNHIPPFPLR
FSFAQRAKIE IIRILSIAYE TIYCEKNKRK LATTDQRHNL SVLSVFSPLI EGWLSNYREL
LVPLSDVPFS LADRKNKKQI FDNIDRINGE SIITDFNYCQ LYIFSLALQV DGKTSRLNMN
EIVTSARYVE LAYRSAKEIL SSAKRVSRQG MLKYMPVRWV IRIIRSIAFI VKCYLTLTGS
ELATNPDARN ILKLSAISVD ETFDIIRDTA VTLKEATPDE LHLCQRYAAI LMYLCTEMKL
RKKSYLERPP LLRDGTTPLE SNRESSLEGQ DLTKKPIFSK RIGYNKTETT FEPSERPLTE
EINSNSQNSN DTSSKGIVDP FVEQNNDITT ALLNNELFQG PSLSDEVTDW FGASEDIGLE
FVEPWTELIE QRYMQCGDGD NNNFENLYNL FVNSNNINND INNSRPITRK
