ACE2_YEAST
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 03-AUG-2022, entry version 209.
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;
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}.
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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; 429.
DR DIP; DIP-2012N; -.
DR ELM; P21192; -.
DR IntAct; P21192; 8.
DR MINT; P21192; -.
DR STRING; 4932.YLR131C; -.
DR iPTMnet; P21192; -.
DR MaxQB; P21192; -.
DR PaxDb; P21192; -.
DR PRIDE; P21192; -.
DR EnsemblFungi; YLR131C_mRNA; YLR131C; YLR131C.
DR GeneID; 850822; -.
DR KEGG; sce:YLR131C; -.
DR SGD; S000004121; ACE2.
DR VEuPathDB; FungiDB:YLR131C; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176710; -.
DR HOGENOM; CLU_021006_0_0_1; -.
DR InParanoid; P21192; -.
DR OMA; FQHTPTK; -.
DR BioCyc; YEAST:G3O-32273-MON; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
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; 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 286..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..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
