ID   ACE2_YEAST              Reviewed;         770 AA.
AC   P21192; D6VYC6;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   04-NOV-2026, entry version 227.
DE   RecName: Full=Metallothionein expression activator;
GN   Name=ACE2; OrderedLocusNames=YLR131C; ORFNames=L3123, L9606.10;
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 [GENOMIC DNA].
RC   STRAIN=DBY939;
RX   PubMed=1986241; DOI=10.1128/mcb.11.1.476-485.1991;
RA   Butler G., Thiele D.J.;
RT   "ACE2, an activator of yeast metallothionein expression which is homologous
RT   to SWI5.";
RL   Mol. Cell. Biol. 11:476-485(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871; DOI=10.1038/387s087;
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   [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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-122, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP   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   [7]
RP   IDENTIFICATION BY 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-247; SER-249;
RP   SER-253; THR-259; SER-385; SER-392; SER-483; THR-486; THR-501; SER-564 AND
RP   SER-714, 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: Plays a role in regulating basal-level expression of CUP1.
CC       Activates EGT2 transcription in the absence of SWI5.
CC   -!- INTERACTION:
CC       P21192; P53894: CBK1; NbExp=3; IntAct=EBI-2073, EBI-4110;
CC       P21192; P30822: CRM1; NbExp=3; IntAct=EBI-2073, EBI-20589;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M55619; AAA34387.1; -; Genomic_DNA.
DR   EMBL; X91258; CAA62643.1; -; Genomic_DNA.
DR   EMBL; Z73303; CAA97702.1; -; Genomic_DNA.
DR   EMBL; U53881; AAB82398.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09442.1; -; Genomic_DNA.
DR   PIR; S12943; TWBYA2.
DR   RefSeq; NP_013232.1; NM_001182018.1.
DR   AlphaFoldDB; P21192; -.
DR   BioGRID; 31400; 438.
DR   DIP; DIP-2012N; -.
DR   ELM; P21192; -.
DR   FunCoup; P21192; 825.
DR   IntAct; P21192; 9.
DR   STRING; 4932.YLR131C; -.
DR   GlyCosmos; P21192; 2 sites, 1 glycan.
DR   GlyGen; P21192; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P21192; -.
DR   PaxDb; 4932-YLR131C; -.
DR   PeptideAtlas; P21192; -.
DR   EnsemblFungi; YLR131C_mRNA; YLR131C; YLR131C.
DR   GeneID; 850822; -.
DR   KEGG; sce:YLR131C; -.
DR   AGR; SGD:S000004121; -.
DR   SGD; S000004121; ACE2.
DR   VEuPathDB; FungiDB:YLR131C; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_021006_0_0_1; -.
DR   InParanoid; P21192; -.
DR   OMA; AAKTHEC; -.
DR   OrthoDB; 3437960at2759; -.
DR   BioCyc; YEAST:G3O-32273-MONOMER; -.
DR   BioGRID-ORCS; 850822; 2 hits in 13 CRISPR screens.
DR   PRO; PR:P21192; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P21192; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0060196; P:positive regulation of antisense RNA transcription; IMP:SGD.
DR   GO; GO:2001043; P:positive regulation of septum digestion after cytokinesis; IMP:SGD.
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   CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR   FunFam; 3.30.160.60:FF:002021; Transcription factor; 1.
DR   FunFam; 3.30.160.60:FF:001752; Transcriptional factor SWI5; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR050329; GLI_C2H2-zinc-finger.
DR   InterPro; IPR013087; Zf-C2H2_type.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR19818:SF144; METALLOTHIONEIN EXPRESSION ACTIVATOR-RELATED; 1.
DR   PANTHER; PTHR19818; ZINC FINGER PROTEIN ZIC AND GLI; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..770
FT                   /note="Metallothionein expression activator"
FT                   /id="PRO_0000046800"
FT   ZN_FING         603..627
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         633..657
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         662..685
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          77..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         253
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         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         486
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         501
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         564
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         709
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   770 AA;  86634 MW;  A7FCA8C506A2FD75 CRC64;
     MDNVVDPWYI NPSGFAKDTQ DEEYVQHHDN VNPTIPPPDN YILNNENDDG LDNLLGMDYY
     NIDDLLTQEL RDLDIPLVPS PKTGDGSSDK KNIDRTWNLG DENNKVSHYS KKSMSSHKRG
     LSGTAIFGFL GHNKTLSISS LQQSILNMSK DPQPMELINE LGNHNTVKNN NDDFDHIREN
     DGENSYLSQV LLKQQEELRI ALEKQKEVNE KLEKQLRDNQ IQQEKLRKVL EEQEEVAQKL
     VSGATNSNSK PGSPVILKTP AMQNGRMKDN AIIVTTNSAN GGYQFPPPTL ISPRMSNTSI
     NGSPSRKYHR QRYPNKSPES NGLNLFSSNS GYLRDSELLS FSPQNYNLNL DGLTYNDHNN
     TSDKNNNDKK NSTGDNIFRL FEKTSPGGLS ISPRINGNSL RSPFLVGTDK SRDDRYAAGT
     FTPRTQLSPI HKKRESVVST VSTISQLQDD TEPIHMRNTQ NPTLRNANAL ASSSVLPPIP
     GSSNNTPIKN SLPQKHVFQH TPVKAPPKNG SNLAPLLNAP DLTDHQLEIK TPIRNNSHCE
     VESYPQVPPV THDIHKSPTL HSTSPLPDEI IPRTTPMKIT KKPTTLPPGT IDQYVKELPD
     KLFECLYPNC NKVFKRRYNI RSHIQTHLQD RPYSCDFPGC TKAFVRNHDL IRHKISHNAK
     KYICPCGKRF NREDALMVHR SRMICTGGKK LEHSINKKLT SPKKSLLDSP HDTSPVKETI
     ARDKDGSVLM KMEEQLRDDM RKHGLLDPPP STAAHEQNSN RTLSNETDAL
//