TSL1_YEAST
ID TSL1_YEAST Reviewed; 1098 AA.
AC P38427; D6W0I5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Trehalose synthase complex regulatory subunit TSL1;
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 123 kDa subunit;
GN Name=TSL1; OrderedLocusNames=YML100W;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8404905; DOI=10.1111/j.1432-1033.1993.tb18207.x;
RA Vuorio O.E., Kalkkinen N., Londesborough J.;
RT "Cloning of two related genes encoding the 56-kDa and 123-kDa subunits of
RT trehalose synthase from the yeast Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 216:849-861(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION, AND INTERACTION WITH TPS1 AND TPS2.
RX PubMed=9194697; DOI=10.1046/j.1365-2958.1997.3861749.x;
RA Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T.,
RA Wiemken A., De Virgilio C.;
RT "Structural analysis of the subunits of the trehalose-6-phosphate
RT synthase/phosphatase complex in Saccharomyces cerevisiae and their function
RT during heat shock.";
RL Mol. Microbiol. 24:687-695(1997).
RN [5]
RP SUBUNIT.
RX PubMed=9837904; DOI=10.1074/jbc.273.50.33311;
RA Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C.,
RA Wiemken A., Thevelein J.M.;
RT "Composition and functional analysis of the Saccharomyces cerevisiae
RT trehalose synthase complex.";
RL J. Biol. Chem. 273:33311-33319(1998).
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 THR-251, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-77; SER-135; SER-147;
RP SER-161; SER-303 AND THR-815, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-53; SER-56; SER-71;
RP SER-161 AND SER-229, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Regulatory subunit of the trehalose synthase complex that
CC catalyzes the production of trehalose from glucose-6-phosphate and UDP-
CC glucose in a two step process. May stabilize the trehalose synthase
CC complex, and confer sensitivity to physiological concentrations of
CC phosphate and to fructose 6-phosphate. {ECO:0000269|PubMed:9194697}.
CC -!- SUBUNIT: The trehalose synthase complex is composed of the two
CC catalytic subunits TPS1 and TPS2, and at least one of the two
CC regulatory subunits TPS3 or TSL1. {ECO:0000269|PubMed:9837904}.
CC -!- INTERACTION:
CC P38427; Q00764: TPS1; NbExp=6; IntAct=EBI-19638, EBI-19430;
CC P38427; P31688: TPS2; NbExp=3; IntAct=EBI-19638, EBI-19440;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Repressed by glucose.
CC -!- DOMAIN: C-terminal 700 AA are mainly in alpha-helices and beta-sheets.
CC -!- MISCELLANEOUS: Present with 1960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
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DR EMBL; X72788; CAA51303.1; -; Genomic_DNA.
DR EMBL; X80835; CAA56797.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09799.1; -; Genomic_DNA.
DR PIR; S36868; S36868.
DR RefSeq; NP_013608.1; NM_001182460.1.
DR AlphaFoldDB; P38427; -.
DR SMR; P38427; -.
DR BioGRID; 35043; 78.
DR ComplexPortal; CPX-583; Trehalose-6-phosphate synthase/phosphatase complex, tsl1 variant.
DR DIP; DIP-753N; -.
DR IntAct; P38427; 16.
DR MINT; P38427; -.
DR STRING; 4932.YML100W; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; P38427; -.
DR MaxQB; P38427; -.
DR PaxDb; P38427; -.
DR PRIDE; P38427; -.
DR EnsemblFungi; YML100W_mRNA; YML100W; YML100W.
DR GeneID; 854872; -.
DR KEGG; sce:YML100W; -.
DR SGD; S000004566; TSL1.
DR VEuPathDB; FungiDB:YML100W; -.
DR eggNOG; KOG1050; Eukaryota.
DR GeneTree; ENSGT00940000167933; -.
DR HOGENOM; CLU_002351_2_0_1; -.
DR InParanoid; P38427; -.
DR OMA; CHEFIVC; -.
DR BioCyc; MetaCyc:MON3O-4029; -.
DR BioCyc; YEAST:MON3O-4029; -.
DR PRO; PR:P38427; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38427; protein.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:SGD.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1098
FT /note="Trehalose synthase complex regulatory subunit TSL1"
FT /id="PRO_0000122511"
FT REPEAT 144..150
FT /note="1"
FT REPEAT 158..164
FT /note="2"
FT REGION 59..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..164
FT /note="2 X 7 AA repeats of R-I-A-S-P-I-Q"
FT REGION 192..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..812
FT /note="TPS complex domain"
FT REGION 1000..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 815
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1098 AA; 123018 MW; EA0A8A86AF178F04 CRC64;
MALIVASLFL PYQPQFELDT SLPENSQVDS SLVNIQAMAN DQQQQRALSN NISQESLVAP
APEQGVPPAI SRSATRSPSA FNRASSTTNT ATLDDLVSSD IFMENLTANA TTSHTPTSKT
MLKPRKNGSV ERFFSPSSNI PTDRIASPIQ HEHDSGSRIA SPIQQQQQDP TTNLLKNVNK
SLLVHSLLNN TSQTSLEGPN NHIVTPKSRA GNRPTSAATS LVNRTKQGSA SSGSSGSSAP
PSIKRITPHL TASAAKQRPL LAKQPSNLKY SELADISSSE TSSQHNESDP DDLTTAPDEE
YVSDLEMDDA KQDYKVPKFG GYSNKSKLKK YALLRSSQEL FSRLPWSIVP SIKGNGAMKN
AINTAVLENI IPHRHVKWVG TVGIPTDEIP ENILANISDS LKDKYDSYPV LTDDDTFKAA
YKNYCKQILW PTLHYQIPDN PNSKAFEDHS WKFYRNLNQR FADAIVKIYK KGDTIWIHDY
HLMLVPQMVR DVLPFAKIGF TLHVSFPSSE VFRCLAQREK ILEGLTGADF VGFQTREYAR
HFLQTSNRLL MADVVHDEEL KYNGRVVSVR FTPVGIDAFD LQSQLKDGSV MQWRQLIRER
WQGKKLIVCR DQFDRIRGIH KKLLAYEKFL VENPEYVEKS TLIQICIGSS KDVELERQIM
IVVDRINSLS TNISISQPVV FLHQDLDFSQ YLALSSEADL FVVSSLREGM NLTCHEFIVC
SEDKNAPLLL SEFTGSASLL NDGAIIINPW DTKNFSQAIL KGLEMPFDKR RPQWKKLMKD
IINNDSTNWI KTSLQDIHIS WQFNQEGSKI FKLNTKTLME DYQSSKKRMF VFNIAEPPSS
RMISILNDMT SKGNIVYIMN SFPKPILENL YSRVQNIGLI AENGAYVSLN GVWYNIVDQV
DWRNDVAKIL EDKVERLPGS YYKINESMIK FHTENAEDQD RVASVIGDAI THINTVFDHR
GIHAYVYKNV VSVQQVGLSL SAAQFLFRFY NSASDPLDTS SGQITNIQTP SQQNPSDQEQ
QPPASPTVSM NHIDFACVSG SSSPVLEPLF KLVNDEASEG QVKAGHAIVY GDATSTYAKE
HVNGLNELFT IISRIIED
