ECM22_YEAST
ID ECM22_YEAST Reviewed; 814 AA.
AC Q05958; D6VYN0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sterol regulatory element-binding protein ECM22;
DE AltName: Full=Extracellular mutant protein 22;
GN Name=ECM22; OrderedLocusNames=YLR228C;
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=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 [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 FUNCTION, MUTAGENESIS OF GLY-790, AND DISRUPTION PHENOTYPE.
RX PubMed=11208779; DOI=10.1128/jb.183.3.830-834.2001;
RA Shianna K.V., Dotson W.D., Tove S., Parks L.W.;
RT "Identification of a UPC2 homolog in Saccharomyces cerevisiae and its
RT involvement in aerobic sterol uptake.";
RL J. Bacteriol. 183:830-834(2001).
RN [4]
RP FUNCTION.
RX PubMed=11292809; DOI=10.1128/jb.183.9.2881-2887.2001;
RA Abramova N.E., Sertil O., Mehta S., Lowry C.V.;
RT "Reciprocal regulation of anaerobic and aerobic cell wall mannoprotein gene
RT expression in Saccharomyces cerevisiae.";
RL J. Bacteriol. 183:2881-2887(2001).
RN [5]
RP FUNCTION.
RX PubMed=11533229; DOI=10.1128/mcb.21.19.6395-6405.2001;
RA Vik A., Rine J.;
RT "Upc2p and Ecm22p, dual regulators of sterol biosynthesis in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 21:6395-6405(2001).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-445 AND SER-464, AND
RP IDENTIFICATION BY 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-464, AND IDENTIFICATION BY
RP 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: Transcription factor involved in sterol uptake and regulation
CC of sterol biosynthesis. Binds to sterol regulatory elements (SRE) with
CC the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters
CC and regulates transcription of ERG2 and ERG3 in response to sterol
CC levels. Seems to be involved in activation of DAN2 and DAN3 cell wall
CC mannoproteins. {ECO:0000269|PubMed:11208779,
CC ECO:0000269|PubMed:11292809, ECO:0000269|PubMed:11533229}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: ECM22 and UPC2 (in combination) null mutants are
CC not viable. {ECO:0000269|PubMed:11208779}.
CC -!- MISCELLANEOUS: Present with 79 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U19027; AAB67415.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09546.1; -; Genomic_DNA.
DR PIR; S51451; S51451.
DR RefSeq; NP_013329.1; NM_001182115.1.
DR AlphaFoldDB; Q05958; -.
DR SMR; Q05958; -.
DR BioGRID; 31498; 107.
DR DIP; DIP-5951N; -.
DR IntAct; Q05958; 5.
DR STRING; 4932.YLR228C; -.
DR iPTMnet; Q05958; -.
DR MaxQB; Q05958; -.
DR PaxDb; Q05958; -.
DR PRIDE; Q05958; -.
DR EnsemblFungi; YLR228C_mRNA; YLR228C; YLR228C.
DR GeneID; 850928; -.
DR KEGG; sce:YLR228C; -.
DR SGD; S000004218; ECM22.
DR VEuPathDB; FungiDB:YLR228C; -.
DR eggNOG; ENOG502QRM1; Eukaryota.
DR GeneTree; ENSGT00940000176420; -.
DR HOGENOM; CLU_011669_0_0_1; -.
DR InParanoid; Q05958; -.
DR OMA; FHVKGAV; -.
DR BioCyc; YEAST:G3O-32342-MON; -.
DR PRO; PR:Q05958; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05958; protein.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; 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: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 CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR021858; Fun_TF.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF11951; Fungal_trans_2; 1.
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 Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..814
FT /note="Sterol regulatory element-binding protein ECM22"
FT /id="PRO_0000114948"
FT DNA_BIND 43..73
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 790
FT /note="G->D: Increases aerobic sterol uptake."
FT /evidence="ECO:0000269|PubMed:11208779"
SQ SEQUENCE 814 AA; 89286 MW; 48E3BDF32D7C668F CRC64;
MTSDDGNAGQ EREKDAELIE VGGKKVSKTS TGKRKFHNKS KTGCDNCKRR RVKCDEGKPF
CKKCTNMKLD CVYSPIQPRR RKDSSSSKFA SAVHDRVGKK NLSDNAIMLQ QQQQQLHHQQ
EQQFRQQQQV QLQQQLLPHV GTDEQSNSPN SVPPSVSNNM ENLLLPHLLA SLVNNTSNST
NSSANGAEAH NNITQTAPSS MINNNHPNMA LPGNSPLSIP ITPSFQSTAM NLSSSLNGLL
SPGRLNSVTN GLQQPQLQQQ NQQIPQQQGT QSPFSNIPFD QLAQLNKMGL NFNMKSFNTL
FPYGAANGMA SEFQELFGLG KFATSNNRAI KVSTAEEALA NMQQEQEDKN KQFTKNPLDN
TKTDAVNSGN NPLNGNENKV TASDILSHNK NLIIDNTGLT ISPPHTLSKP SIDQNIASPS
TGVSNVTSTK SLLSIPDNRT ALGNSPTLKT SPMGDLLSNS EALSPRSSNS HTQQQSSPHS
NASSASRLVP ELVGLSRKSN LNLIDLKLFH HYCTDVWHTI TEAGISGPEV WSTYIPDLAF
HFPFLMHTIL AFSATHLSRT EAGLDNYVSS HRLEALRLLR EAVLEISDDN TDALVASALI
LILDSLANAS SSSPTAWIFH VKGAVTILTA VWPLSETSKF YNLISVDLSD LGEAVINQSN
HNNDNDNSNN GDGNNNNTIS ELVCFDESIA DLYPVEIDSP YLITLAYLDK LHREKNQLDF
MLRVFSFPAL LDRTFLALLM TGDLGAMRIM RSYYTLLRGY TTEIKDKVWF LDSVSQVLPQ
DVDEYSGGGG MHMMLDFLGG GLPSMTTTNF SAFM
