LEUR_YEAST
ID LEUR_YEAST Reviewed; 886 AA.
AC P08638; D6VZ85;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Regulatory protein LEU3;
GN Name=LEU3; OrderedLocusNames=YLR451W; ORFNames=L9324.1;
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=3299266; DOI=10.1093/nar/15.13.5261;
RA Zhou K., Brisco P.R.G., Hinkkanen A.E., Kohlhaw G.B.;
RT "Structure of yeast regulatory gene LEU3 and evidence that LEU3 itself is
RT under general amino acid control.";
RL Nucleic Acids Res. 15:5261-5273(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2823102; DOI=10.1128/mcb.7.8.2708-2717.1987;
RA Friden P., Schimmel P.;
RT "LEU3 of Saccharomyces cerevisiae encodes a factor for control of RNA
RT levels of a group of leucine-specific genes.";
RL Mol. Cell. Biol. 7:2708-2717(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [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 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 [7]
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: Factor for control of RNA levels of a group of leucine-
CC specific genes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:17467953}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Y00360; CAA68438.1; -; Genomic_DNA.
DR EMBL; M17222; AAA34741.1; -; Genomic_DNA.
DR EMBL; U22382; AAB67526.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09751.1; -; Genomic_DNA.
DR PIR; S00638; RGBYL3.
DR RefSeq; NP_013556.3; NM_001182339.3.
DR PDB; 2ER8; X-ray; 2.85 A; A/B/C/D=32-103.
DR PDB; 2ERE; X-ray; 3.00 A; A/B=32-103.
DR PDB; 2ERG; X-ray; 3.15 A; A/B=32-103.
DR PDBsum; 2ER8; -.
DR PDBsum; 2ERE; -.
DR PDBsum; 2ERG; -.
DR AlphaFoldDB; P08638; -.
DR SMR; P08638; -.
DR BioGRID; 31709; 70.
DR DIP; DIP-2400N; -.
DR IntAct; P08638; 2.
DR MINT; P08638; -.
DR STRING; 4932.YLR451W; -.
DR iPTMnet; P08638; -.
DR MaxQB; P08638; -.
DR PaxDb; P08638; -.
DR PRIDE; P08638; -.
DR EnsemblFungi; YLR451W_mRNA; YLR451W; YLR451W.
DR GeneID; 851172; -.
DR KEGG; sce:YLR451W; -.
DR SGD; S000004443; LEU3.
DR VEuPathDB; FungiDB:YLR451W; -.
DR eggNOG; ENOG502QPVP; Eukaryota.
DR GeneTree; ENSGT00940000176683; -.
DR HOGENOM; CLU_015609_0_0_1; -.
DR InParanoid; P08638; -.
DR OMA; MLWKDVD; -.
DR BioCyc; YEAST:G3O-32504-MON; -.
DR EvolutionaryTrace; P08638; -.
DR PRO; PR:P08638; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P08638; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:2001278; P:positive regulation of leucine biosynthetic process; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 3D-structure; Activator; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; DNA-binding; Leucine biosynthesis;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..886
FT /note="Regulatory protein LEU3"
FT /id="PRO_0000114954"
FT DNA_BIND 37..67
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 874..882
FT /note="9aaTAD"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 504
FT /note="M -> I (in Ref. 2; AAA34741)"
FT /evidence="ECO:0000305"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:2ER8"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2ER8"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2ER8"
FT HELIX 78..97
FT /evidence="ECO:0007829|PDB:2ER8"
SQ SEQUENCE 886 AA; 100153 MW; C5F8EDCD326B1EBB CRC64;
MEGRSDFVAT SQSGSEMSHS ETRNRTGMNA RKRKFACVEC RQQKSKCDAH ERAPEPCTKC
AKKNVPCILK RDFRRTYKRA RNEAIEKRFK ELTRTLTNLT SDEILKKIEE EQEIVLDNSN
FTKEKVKQLR KSAFETTEIE PRSYKTLRGE PISYSTNRRH TDSSPLTLLS SSTNFDPVHS
TNVMTDDQLK CLPKSLGDVY LSSSDIAELF QEFATKYHQF LPVVDLSKGA ERIYHLSPCL
FWVILLIGLR RKFGATDLMT RLSVLVKSVL SEITISPIIR YTPSDKDEPV LNVASVYSVQ
AFLLYTFWPP LTSSLSADTS WNTIGTAMFQ ALRVGLNCAG FSKEYASANS ELVNEQIRTW
ICCNVVSQTV ASSFGFPAYV SFDYLVISSI RVPNSKSQVD IPNELRQMAQ IARFENQIVN
TMNSTPASVT GMVSQEEKQP LLHVLNQQLS QLEISLEENN LDDIRKFLLL VAKVHLLTYY
FTDVTSQSAG KSNGNIYEGS YSIMELDTSF ETKRGLVKVY NAAVNFLIHA NSMWEHDPTI
IKYFPGLFVL NIWQSACIIS KLIHSSLHSM LDVNSGKKAY NNAISLTFNA SVLKYDMAYR
SSGIMRSIWS LFANMYDAWK NDQKEGGGRL NNDFNLGITI KSRMSVNVFF DCLYILKEKC
GMAKLERETK VSTAYNVDEE EEEDEDEEGE EEEEEEELSS KVPENMDSQQ LRTRKFTNVR
HPEKKARKII ETIPLDPNPI NAGSTSSGSS LTTPNSQVAN TISYRGILNK MSPREQLNHA
NLDSSVSTDI KDTEAVNEPL PIGRNAEHPA NQPPLSITQM QENTLPATQA NSSLLETYPI
VQSNPVTTTI KESPNSIMAG WDNWESDMVW RDVDILMNEF AFNPKV
