STD1_YEAST
ID STD1_YEAST Reviewed; 444 AA.
AC Q02794; D6W2B3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein STD1;
DE AltName: Full=Glucose repression modulator MSN3;
DE AltName: Full=Suppressor of Tbp deletion protein 1;
DE AltName: Full=Suppressor of fluoride sensitivity 3;
GN Name=STD1; Synonyms=MSN3, SFS3; OrderedLocusNames=YOR047C;
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.
RX PubMed=8497275; DOI=10.1128/mcb.13.6.3650-3659.1993;
RA Ganster R.W., Shen W., Schmidt M.C.;
RT "Isolation of STD1, a high-copy-number suppressor of a dominant negative
RT mutation in the yeast TATA-binding protein.";
RL Mol. Cell. Biol. 13:3650-3659(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND INTERACTION WITH SNF1.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8114728; DOI=10.1128/mcb.14.3.1972-1978.1994;
RA Hubbard E.J.A., Jiang R., Carlson M.;
RT "Dosage-dependent modulation of glucose repression by MSN3 (STD1) in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 14:1972-1978(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNF3 AND RGT2.
RX PubMed=10373505; DOI=10.1128/mcb.19.7.4561;
RA Schmidt M.C., McCartney R.R., Zhang X., Tillman T.S., Solimeo H., Wolfl S.,
RA Almonte C., Watkins S.C.;
RT "Std1 and Mth1 proteins interact with the glucose sensors to control
RT glucose-regulated gene expression in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:4561-4571(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=12618390; DOI=10.1093/genetics/163.2.507;
RA Kuchin S., Vyas V.K., Kanter E., Hong S.P., Carlson M.;
RT "Std1p (Msn3p) positively regulates the Snf1 kinase in Saccharomyces
RT cerevisiae.";
RL Genetics 163:507-514(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 PRION IDENTIFICATION, AND INTERACTION WITH PMA1.
RX PubMed=19797769; DOI=10.1101/gad.1839109;
RA Brown J.C., Lindquist S.;
RT "A heritable switch in carbon source utilization driven by an unusual yeast
RT prion.";
RL Genes Dev. 23:2320-2332(2009).
CC -!- FUNCTION: Involved in modulation of glucose-regulated gene expression.
CC Together with MTH1, represses the hexose transporter (HXT) genes in
CC conditions of low glucose. Stimulates the SNF1 kinase by an interaction
CC with the catalytic domain that antagonizes autoinhibition and promotes
CC an active conformation of the kinase. {ECO:0000269|PubMed:10373505,
CC ECO:0000269|PubMed:12618390}.
CC -!- SUBUNIT: Interacts with SNF1 kinase; via catalytic domain. Interacts
CC with the glucose sensors SNF3 and RGT2. {ECO:0000269|PubMed:10373505,
CC ECO:0000269|PubMed:12618390, ECO:0000269|PubMed:19797769,
CC ECO:0000269|PubMed:8114728}.
CC -!- INTERACTION:
CC Q02794; P32790: SLA1; NbExp=3; IntAct=EBI-18344, EBI-17313;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10373505};
CC Peripheral membrane protein {ECO:0000269|PubMed:10373505}. Nucleus
CC {ECO:0000269|PubMed:10373505}.
CC -!- MISCELLANEOUS: The prion state [GAR+] is provoked by the interaction of
CC the two proteins STD1 and PMA1. It involves a complex between a small
CC fraction of the cellular complement of PMA1, and STD1, a much lower-
CC abundance protein, and it is transmissible by non-Mendelian,
CC cytoplasmic inheritance. [GAR+] makes cells resistant to the glucose-
CC associated repression of alternative carbon sources. In contrast to
CC other prion forms, [GAR+] cannot be cured by GdnHCl or by inactivation
CC of the molecular chaperone HSP104. {ECO:0000305|PubMed:19797769}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast MTH1. {ECO:0000305}.
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DR EMBL; L06011; AAA16951.1; -; Unassigned_DNA.
DR EMBL; L21932; AAA18535.1; -; Unassigned_DNA.
DR EMBL; Z74955; CAA99238.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10829.1; -; Genomic_DNA.
DR PIR; B48129; B48129.
DR RefSeq; NP_014690.1; NM_001183466.1.
DR AlphaFoldDB; Q02794; -.
DR BioGRID; 34448; 112.
DR DIP; DIP-1300N; -.
DR IntAct; Q02794; 17.
DR MINT; Q02794; -.
DR STRING; 4932.YOR047C; -.
DR PaxDb; Q02794; -.
DR PRIDE; Q02794; -.
DR EnsemblFungi; YOR047C_mRNA; YOR047C; YOR047C.
DR GeneID; 854212; -.
DR KEGG; sce:YOR047C; -.
DR SGD; S000005573; STD1.
DR VEuPathDB; FungiDB:YOR047C; -.
DR eggNOG; ENOG502QPKX; Eukaryota.
DR GeneTree; ENSGT00940000176732; -.
DR HOGENOM; CLU_049491_0_0_1; -.
DR InParanoid; Q02794; -.
DR OMA; ENANIQH; -.
DR BioCyc; YEAST:G3O-33591-MON; -.
DR PRO; PR:Q02794; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q02794; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR GO; GO:0006006; P:glucose metabolic process; IMP:SGD.
DR GO; GO:0071590; P:nicotinamide riboside biosynthetic process; IMP:SGD.
DR GO; GO:0071592; P:nicotinic acid riboside biosynthetic process; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0009651; P:response to salt stress; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
DR InterPro; IPR035189; Std1/Mth1.
DR Pfam; PF17235; STD1; 1.
PE 1: Evidence at protein level;
KW Activator; Amyloid; Cell membrane; Membrane; Nucleus; Prion;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..444
FT /note="Protein STD1"
FT /id="PRO_0000072260"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 139
FT /note="E -> D (in Ref. 2; AAA18535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50261 MW; 888D2D78A72A6507 CRC64;
MFVSPPPATA RNQVLGKRKS KRHDENPKNV QPNADTEMTN SVPSIGFNSN LPHNNQEINT
PNHYNLSSNS GNVRSNNNFV TTPPEYADRA RIEIIKRLLP TAGTKPMEVN SNTAENANIQ
HINTPDSQSF VSDHSSSYES SIFSQPSTAL TDITTGSSLI DTKTPKFVTE VTLEDALPKT
FYDMYSPEVL MSDPANILYN GRPKFTKREL LDWDLNDIRS LLIVEQLRPE WGSQLPTVVT
SGINLPQFRL QLLPLSSSDE FIIATLVNSD LYIEANLDRN FKLTSAKYTV ASARKRHEEM
TGSKEPIMRL SKPEWRNIIE NYLLNVAVEA QCRYDFKQKR SEYKRWKLLN SNLKRPDMPP
PSLIPHGFKI HDCTNSGSLL KKALMKNLQL KNYKNDAKTL GAGTQKNVVN KVSLTSEERA
AIWFQCQTQV YQRLGLDWKP DGMS
