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   04-NOV-2026, entry version 211.
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; DOI=10.1038/387s090;
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=7; IntAct=EBI-19638, EBI-19430;
CC       P38427; P31688: TPS2; NbExp=4; IntAct=EBI-19638, EBI-19440;
CC       P38427; P38426: TPS3; NbExp=3; IntAct=EBI-19638, EBI-19448;
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; 111.
DR   ComplexPortal; CPX-583; Trehalose-6-phosphate synthase/phosphatase complex, tsl1 variant.
DR   DIP; DIP-753N; -.
DR   FunCoup; P38427; 402.
DR   IntAct; P38427; 31.
DR   STRING; 4932.YML100W; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   GlyGen; P38427; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P38427; -.
DR   PaxDb; 4932-YML100W; -.
DR   PeptideAtlas; P38427; -.
DR   EnsemblFungi; YML100W_mRNA; YML100W; YML100W.
DR   GeneID; 854872; -.
DR   KEGG; sce:YML100W; -.
DR   AGR; SGD:S000004566; -.
DR   SGD; S000004566; TSL1.
DR   VEuPathDB; FungiDB:YML100W; -.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_2_0_1; -.
DR   InParanoid; P38427; -.
DR   OMA; ADLDIFY; -.
DR   OrthoDB; 755951at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-4029; -.
DR   BioCyc; YEAST:MONOMER3O-4029; -.
DR   BioGRID-ORCS; 854872; 0 hits in 10 CRISPR screens.
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   CDD; cd03788; GT20_TPS; 1.
DR   FunFam; 3.40.50.2000:FF:000099; Alpha,alpha-trehalose phosphate synthase subunit, putative; 1.
DR   FunFam; 3.40.50.2000:FF:000036; Alpha,alpha-trehalose-phosphate synthase subunit Tps2; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR10788:SF15; TREHALOSE SYNTHASE COMPLEX REGULATORY SUBUNIT TPS3-RELATED; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..242
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1027
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
//