CUP2_YEAST
ID CUP2_YEAST Reviewed; 225 AA.
AC P15315; D6VTY6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Transcriptional activator protein CUP2;
DE AltName: Full=Copper-fist transcription factor;
GN Name=CUP2; Synonyms=ACE1; OrderedLocusNames=YGL166W; ORFNames=G1810;
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=3052856; DOI=10.1016/0092-8674(88)90229-2;
RA Fuerst P., Hu S., Hackett R., Hamer D.;
RT "Copper activates metallothionein gene transcription by altering the
RT conformation of a specific DNA binding protein.";
RL Cell 55:705-717(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2651899; DOI=10.1128/mcb.9.2.421-429.1989;
RA Szczypka M.S., Thiele D.J.;
RT "A cysteine-rich nuclear protein activates yeast metallothionein gene
RT transcription.";
RL Mol. Cell. Biol. 9:421-429(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RX PubMed=2674688; DOI=10.1128/mcb.9.9.4091-4095.1989;
RA Buchman C., Skroch P., Welch J., Fogel S., Karin M.;
RT "The CUP2 gene product, regulator of yeast metallothionein expression, is a
RT copper-activated DNA-binding protein.";
RL Mol. Cell. Biol. 9:4091-4095(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RA Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP CHARACTERIZATION.
RX PubMed=8509391; DOI=10.1016/s0021-9258(18)31418-2;
RA Thorvaldsen J.L., Sewell A.K., McCowen C.L., Winge D.R.;
RT "Regulation of metallothionein genes by the ACE1 and AMT1 transcription
RT factors.";
RL J. Biol. Chem. 268:12512-12518(1993).
RN [10]
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).
CC -!- FUNCTION: Trans-acting regulatory protein that activates transcription
CC of the CUP1 gene (metallothionein) in response to copper ions. Binds to
CC the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in
CC presence of copper or silver. Copper seems to alter the conformation of
CC the protein.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M22580; AAA66313.1; -; Genomic_DNA.
DR EMBL; M24390; AAA34386.1; -; Genomic_DNA.
DR EMBL; Z48618; CAA88533.1; -; Genomic_DNA.
DR EMBL; X85757; CAA59765.1; -; Genomic_DNA.
DR EMBL; M28520; AAA34542.1; -; Genomic_DNA.
DR EMBL; Z72688; CAA96877.1; -; Genomic_DNA.
DR EMBL; AY557820; AAS56146.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07947.1; -; Genomic_DNA.
DR PIR; A31926; A31926.
DR RefSeq; NP_011349.3; NM_001181031.3.
DR AlphaFoldDB; P15315; -.
DR SMR; P15315; -.
DR BioGRID; 33088; 89.
DR DIP; DIP-1335N; -.
DR IntAct; P15315; 8.
DR MINT; P15315; -.
DR STRING; 4932.YGL166W; -.
DR MaxQB; P15315; -.
DR PaxDb; P15315; -.
DR PRIDE; P15315; -.
DR EnsemblFungi; YGL166W_mRNA; YGL166W; YGL166W.
DR GeneID; 852710; -.
DR KEGG; sce:YGL166W; -.
DR SGD; S000003134; CUP2.
DR VEuPathDB; FungiDB:YGL166W; -.
DR eggNOG; ENOG502S7CA; Eukaryota.
DR GeneTree; ENSGT00940000176728; -.
DR HOGENOM; CLU_1220290_0_0_1; -.
DR InParanoid; P15315; -.
DR OMA; KEDETRC; -.
DR BioCyc; YEAST:G3O-30654-MON; -.
DR PRO; PR:P15315; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P15315; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0046688; P:response to copper ion; IMP:SGD.
DR Gene3D; 3.90.430.10; -; 1.
DR InterPro; IPR001083; Cu_fist_DNA-bd_dom.
DR InterPro; IPR036395; Cu_fist_DNA-bd_dom_sf.
DR Pfam; PF00649; Copper-fist; 1.
DR PRINTS; PR00617; COPPERFIST.
DR SMART; SM01090; Copper-fist; 1.
DR SMART; SM00412; Cu_FIST; 1.
DR SUPFAM; SSF57879; SSF57879; 1.
DR PROSITE; PS01119; COPPER_FIST_1; 1.
DR PROSITE; PS50073; COPPER_FIST_2; 1.
PE 1: Evidence at protein level;
KW Activator; Copper; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..225
FT /note="Transcriptional activator protein CUP2"
FT /id="PRO_0000194926"
FT DNA_BIND 1..40
FT /note="Copper-fist"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT REGION 1..108
FT /note="Binds copper and DNA"
FT REGION 109..225
FT /note="Required for transcriptional activation"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
SQ SEQUENCE 225 AA; 24425 MW; E3199A3C8CA9CC1B CRC64;
MVVINGVKYA CETCIRGHRA AQCTHTDGPL QMIRRKGRPS TTCGHCKELR RTKNFNPSGG
CMCASARRPA VGSKEDETRC RCDEGEPCKC HTKRKSSRKS KGGSCHRRAN DEAAHVNGLG
IADLDVLLGL NGRSSDVDMT TTLPSLKPPL QNGEIKADSI DNLDLASLDP LEQSPSISME
PVSINETGSA YTTTNTALND IDIPFSINEL NELYKQVSSH NSHSQ
