TPS3_YEAST
ID TPS3_YEAST Reviewed; 1054 AA.
AC P38426; D6W087; Q6B1W2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Trehalose synthase complex regulatory subunit TPS3;
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 115 kDa subunit;
GN Name=TPS3; OrderedLocusNames=YMR261C; ORFNames=YM8156.03C;
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].
RA Manning A.M., Rosenbloom C.L., Beaudet A.L.;
RT "A large open reading frame in the yeast genome containing homology to the
RT cif1 gene.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-181 AND SER-960, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-150; THR-265;
RP SER-267 AND SER-273, 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. {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 regulatory
CC subunits TPS3 or TSL1. {ECO:0000269|PubMed:9837904}.
CC -!- INTERACTION:
CC P38426; Q00764: TPS1; NbExp=5; IntAct=EBI-19448, EBI-19430;
CC P38426; P31688: TPS2; NbExp=7; IntAct=EBI-19448, EBI-19440;
CC P38426; P38426: TPS3; NbExp=4; IntAct=EBI-19448, EBI-19448;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Repressed by glucose.
CC -!- MISCELLANEOUS: Present with 13500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
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DR EMBL; M88172; AAA35224.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89244.1; -; Genomic_DNA.
DR EMBL; AY692968; AAT92987.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10161.1; -; Genomic_DNA.
DR RefSeq; NP_013988.1; NM_001182768.1.
DR AlphaFoldDB; P38426; -.
DR SMR; P38426; -.
DR BioGRID; 35439; 86.
DR ComplexPortal; CPX-582; Trehalose-6-phosphate synthase/phosphatase complex, tps3 variant.
DR DIP; DIP-891N; -.
DR IntAct; P38426; 8.
DR MINT; P38426; -.
DR STRING; 4932.YMR261C; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; P38426; -.
DR MaxQB; P38426; -.
DR PaxDb; P38426; -.
DR PRIDE; P38426; -.
DR EnsemblFungi; YMR261C_mRNA; YMR261C; YMR261C.
DR GeneID; 855303; -.
DR KEGG; sce:YMR261C; -.
DR SGD; S000004874; TPS3.
DR VEuPathDB; FungiDB:YMR261C; -.
DR eggNOG; KOG1050; Eukaryota.
DR GeneTree; ENSGT00940000167933; -.
DR HOGENOM; CLU_002351_2_0_1; -.
DR InParanoid; P38426; -.
DR OMA; FEGHYKS; -.
DR BioCyc; MetaCyc:MON3O-4030; -.
DR BioCyc; YEAST:MON3O-4030; -.
DR PRO; PR:P38426; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38426; 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; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..1054
FT /note="Trehalose synthase complex regulatory subunit TPS3"
FT /id="PRO_0000122510"
FT REGION 112..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..778
FT /note="Glycosyltransferase"
FT COMPBIAS 155..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 186
FT /note="P -> L (in Ref. 1; AAA35224)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="N -> D (in Ref. 1; AAA35224)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="S -> G (in Ref. 1; AAA35224)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="D -> E (in Ref. 1; AAA35224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 118835 MW; 02E1098B94838EA9 CRC64;
MTIIVASLFL PYTPQFEADV TNSDTAKLVE SSMIKVDCNN QELSNNKQER SSSVTSASSH
YIGLPQEAQI NGEPLQRANV GSPATGVNYH NEMEMLSSEQ FLEELTANAT HAANSGIPPA
NNPVSSGSTA QRPSVEEFFS APSARVCSPS QEASASSISA SRSSAHHNDL SSSLMKNPNL
SFDSHPPRVR SSSKSAVITP VSKSVPDVDP AVVDVAKVRE EFQQQASLPS MKRVSGSTAG
DSSIASSSSN LRYSQQFQDN FIEDTDSEDD IDSDLETDAT KKYNVPKFGG YSNNAKLRAS
LMRNSYELFK HLPWTIVDSD KGNGSLKNAV NIAVAEKTVK EPVSWVGTMG IPTDELPHEV
CHKISKKLEQ DFSSFPVVTD DITFKGAYKN YAKQILWPTL HYQIPDNPNS KAFEDHSWDY
YQKVNQKFSD RIVSVYKPGD TIWIHDYHLM LVPQMVREKL PKAKIGFFLH VSFPSSEVFR
CLANRERILE GIIGANFVGF QTKEYKRHFL QTCNRLLAAD VSNDEVKYHC NIVSVMYAPI
GIDYYHLTSQ LRNGSVLEWR QLIKERWRNK KLIVCRDQFD RIRGLQKKML AYERFLIENP
EYIEKVVLIQ ICIGKSSDPE YERQIMVVVD RINSLSSNIS ISQPVVFLHQ DLDFAQYLAL
NCEADVFLVD ALREGMNLTC HEFIVSSFEK NAPLLLSEFT GSSSVLKEGA ILINPWDINH
VAQSIKRSLE MSPEEKRRRW KKLFKSVIEH DSDNWITKCF EYINNAWESN QETSTVFNLA
PEKFCADYKA SKKHLFIFKI SEPPTSRMLS LLSELSSNNI VYVLSSFTKN TFESLYNGVL
NIGLIAENGA YVRVNGSWYN IVEELDWMKE VAKIFDEKVE RLPGSYYKIA DSMIRFHTEN
ADDQDRVPTV IGEAITHINT LFDDRDIHAY VHKDIVFVQQ TGLALAAAEF LMKFYNSGVS
PTDNSRISLS RTSSSMSVGN NKKHFQNQVD FVCVSGSTSP IIEPLFKLVK QEVEKNNLKF
GYTILYGSSR STYAKEHING VNELFTILHD LTAA
