UPC2_YEAST
ID UPC2_YEAST Reviewed; 913 AA.
AC Q12151; D6VSJ7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sterol uptake control protein 2;
DE AltName: Full=Mannoprotein regulation by oxygen protein 4;
GN Name=UPC2; Synonyms=MOX4; OrderedLocusNames=YDR213W;
GN ORFNames=YD8142.14, YD8142B.05;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 MUTAGENESIS OF GLY-888.
RX PubMed=3059715; DOI=10.1002/yea.320040203;
RA Lewis T.L., Keesler G.A., Fenner G.P., Parks L.W.;
RT "Pleiotropic mutations in Saccharomyces cerevisiae affecting sterol uptake
RT and metabolism.";
RL Yeast 4:93-106(1988).
RN [4]
RP MUTAGENESIS OF GLY-888.
RX PubMed=9696767; DOI=10.1128/jb.180.16.4177-4183.1998;
RA Crowley J.H., Leak F.W. Jr., Shianna K.V., Tove S., Parks L.W.;
RT "A mutation in a purported regulatory gene affects control of sterol uptake
RT in Saccharomyces cerevisiae.";
RL J. Bacteriol. 180:4177-4183(1998).
RN [5]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF GLY-888.
RX PubMed=11238402; DOI=10.1093/genetics/157.3.1169;
RA Abramova N.E., Cohen B.D., Sertil O., Kapoor R., Davies K.J., Lowry C.V.;
RT "Regulatory mechanisms controlling expression of the DAN/TIR mannoprotein
RT genes during anaerobic remodeling of the cell wall in Saccharomyces
RT cerevisiae.";
RL Genetics 157:1169-1177(2001).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=12077145; DOI=10.1074/jbc.m204707200;
RA Wilcox L.J., Balderes D.A., Wharton B., Tinkelenberg A.H., Rao G.,
RA Sturley S.L.;
RT "Transcriptional profiling identifies two members of the ATP-binding
RT cassette transporter superfamily required for sterol uptake in yeast.";
RL J. Biol. Chem. 277:32466-32472(2002).
RN [9]
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 [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).
RN [11]
RP FUNCTION.
RX PubMed=12673627; DOI=10.1002/yea.975;
RA Ter Linde J.J., Regnacq M., Steensma H.Y.;
RT "Transcriptional regulation of YML083c under aerobic and anaerobic
RT conditions.";
RL Yeast 20:439-454(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 AND SER-519, AND
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: Transcription factor that is involved in activation of
CC anaerobic genes such as DAN/TIR cell wall mannoprotein genes and
CC YML083c. Appears to bind to anaerobic response elements (AR1) with the
CC consensus sequence 5'-TCGTTYAG-3' present in the promoter regions of
CC DAN/TIR genes. Involved in sterol uptake and regulation of the sterol
CC biosynthesis. Binds to sterol regulatory elements (SRE) with the
CC consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters.
CC May be involved in down-regulation of CWP2 during anaerobic adaptation.
CC {ECO:0000269|PubMed:11238402, ECO:0000269|PubMed:11292809,
CC ECO:0000269|PubMed:11533229, ECO:0000269|PubMed:12077145,
CC ECO:0000269|PubMed:12673627}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Induced by anaerobic conditions, hypoxia and cold. Repressed
CC by heme. {ECO:0000269|PubMed:11238402}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: ECM22 and UPC2 (in combination) null mutants are not
CC viable.
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DR EMBL; Z68194; CAA92356.1; -; Genomic_DNA.
DR EMBL; Z68195; CAA92364.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12057.1; -; Genomic_DNA.
DR PIR; S61580; S61580.
DR RefSeq; NP_010499.1; NM_001180521.1.
DR PDB; 4N9N; X-ray; 2.90 A; A/B=598-714, A/B=726-878.
DR PDBsum; 4N9N; -.
DR AlphaFoldDB; Q12151; -.
DR SMR; Q12151; -.
DR BioGRID; 32267; 132.
DR DIP; DIP-6262N; -.
DR MINT; Q12151; -.
DR STRING; 4932.YDR213W; -.
DR iPTMnet; Q12151; -.
DR MaxQB; Q12151; -.
DR PaxDb; Q12151; -.
DR PRIDE; Q12151; -.
DR EnsemblFungi; YDR213W_mRNA; YDR213W; YDR213W.
DR GeneID; 851799; -.
DR KEGG; sce:YDR213W; -.
DR SGD; S000002621; UPC2.
DR VEuPathDB; FungiDB:YDR213W; -.
DR eggNOG; ENOG502QRM1; Eukaryota.
DR GeneTree; ENSGT00940000176420; -.
DR HOGENOM; CLU_011669_0_0_1; -.
DR InParanoid; Q12151; -.
DR OMA; EVWPTIT; -.
DR BioCyc; YEAST:G3O-29795-MON; -.
DR PRO; PR:Q12151; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12151; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; 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 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 3D-structure; Activator; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..913
FT /note="Sterol uptake control protein 2"
FT /id="PRO_0000114988"
FT DNA_BIND 50..80
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 103..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..346
FT /evidence="ECO:0000255"
FT COILED 440..472
FT /evidence="ECO:0000255"
FT COMPBIAS 109..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 888
FT /note="G->A: Increased aerobic expression of DAN1."
FT /evidence="ECO:0000269|PubMed:11238402,
FT ECO:0000269|PubMed:3059715, ECO:0000269|PubMed:9696767"
FT MUTAGEN 888
FT /note="G->D: In upc2-1; increases aerobic sterol synthesis
FT and uptake. Increases also aerobic expression of DAN1 and
FT sensibility to NaCl and LiCl."
FT /evidence="ECO:0000269|PubMed:11238402,
FT ECO:0000269|PubMed:3059715, ECO:0000269|PubMed:9696767"
FT HELIX 607..618
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 621..626
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 632..636
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 647..661
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 670..686
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 687..692
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 695..711
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 732..744
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:4N9N"
FT TURN 767..769
FT /evidence="ECO:0007829|PDB:4N9N"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:4N9N"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:4N9N"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 800..811
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 817..824
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 831..839
FT /evidence="ECO:0007829|PDB:4N9N"
FT HELIX 842..861
FT /evidence="ECO:0007829|PDB:4N9N"
FT TURN 871..873
FT /evidence="ECO:0007829|PDB:4N9N"
SQ SEQUENCE 913 AA; 100340 MW; 6937B82B5F8B2D63 CRC64;
MSEVGIQNHK KAVTKPRRRE KVIELIEVDG KKVSTTSTGK RKFHNKSKNG CDNCKRRRVK
CDEGKPACRK CTNMKLECQY TPIHLRKGRG ATVVKYVTRK ADGSVESDSS VDLPPTIKKE
QTPFNDIQSA VKASGSSNDS FPSSASTTKS ESEEKSSAPI EDKNNMTPLS MGLQGTINKK
DMMNNFFSQN GTIGFGSPER LNSGIDGLLL PPLPSGNMGA FQLQQQQQVQ QQSQPQTQAQ
QASGTPNERY GSFDLAGSPA LQSTGMSLSN SLSGMLLCNR IPSGQNYTQQ QLQYQLHQQL
QLQQHQQVQL QQYQQLRQEQ HQQVQQQQQE QLQQYQQHFL QQQQQVLLQQ EQQPNDEEGG
VQEENSKKVK EGPLQSQTSE TTLNSDAATL QADALSQLSK MGLSLKSLST FPTAGIGGVS
YDFQELLGIK FPINNGNSRA TKASNAEEAL ANMQEHHERA AASVKENDGQ LSDTKSPAPS
NNAQGGSASI MEPQAADAVS TMAPISMIER NMNRNSNISP STPSAVLNDR QEMQDSISSL
GNLTKAALEN NEPTISLQTS QTENEDDASR QDMTSKINNE ADRSSVSAGT SNIAKLLDLS
TKGNLNLIDM KLFHHYCTKV WPTITAAKVS GPEIWRDYIP ELAFDYPFLM HALLAFSATH
LSRTETGLEQ YVSSHRLDAL RLLREAVLEI SENNTDALVA SALILIMDSL ANASGNGTVG
NQSLNSMSPS AWIFHVKGAA TILTAVWPLS ERSKFHNIIS VDLSDLGDVI NPDVGTITEL
VCFDESIADL YPVGLDSPYL ITLAYLDKLH REKNQGDFIL RVFTFPALLD KTFLALLMTG
DLGAMRIMRS YYKLLRGFAT EVKDKVWFLE GVTQVLPQDV DEYSGGGGMH MMLDFLGGGL
PSMTTTNFSD FSL
