Reviewed, UniProtKB/Swiss-Prot P31688 (TPS2_YEAST)

Names and origin

Protein names

Recommended name:
    Trehalose-phosphatase
    EC=3.1.3.12
Alternative name(s):
    Trehalose-6-phosphate phosphatase
      Short name=TPP
    Trehalose synthase complex catalytic subunit TPS2

Gene names

Name:	TPS2
Synonyms:	PFK3
Ordered Locus Names:	YDR074W
ORF Names:	YD8554.07

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	896 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. Ref.5
Catalytic activity	Trehalose 6-phosphate + H2O = trehalose + phosphate.
Cofactor	Magnesium.
Enzyme regulation	Inhibited by EDTA.
Subunit structure	The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2, and at least one of the two regulatory subunits TPS3 or TSL1. Ref.6
Subcellular location	Cytoplasm. Ref.8
Induction	By heat shock. Repressed by glucose.
Miscellaneous	Present with 22700 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	In the N-terminal section; belongs to the glycosyltransferase 20 family. In the C-terminal section; belongs to the trehalose phosphatase family.
Biophysicochemical properties	Kinetic parameters: KM=0.2 mM for trehalose 6-phosphate (at pH 6.0) KM=0.5 mM for trehalose 6-phosphate (at pH 7.5) Vmax=20 nmol/min/mg enzyme (at pH 6.0) Vmax=10 nmol/min/mg enzyme (at pH 7.5) pH dependence: Optimum pH is 6.0.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to stress Ref.1 Inferred from direct assay. Source: SGD trehalose biosynthetic process Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Ref.6 Inferred from genetic interaction. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	trehalose-phosphatase activity Ref.1 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 896	896	Trehalose-phosphatase		PRO_0000122509
Regions
	Region	1 – 554	554	Glycosyltransferase
Amino acid modifications
	Modified residue	890	1	Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12
Experimental info
	Sequence conflict	48	1	F → Y in CAA50025. Ref.1
	Sequence conflict	289	1	N → D in CAA50025. Ref.1
	Sequence conflict	542	1	Q → K in CAA50025. Ref.1
	Sequence conflict	546	1	N → D in CAA50025. Ref.1
	Sequence conflict	549	1	M → V in CAA50025. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31688-1 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: E349672CCCDA9349	FASTA	896	102,976
	10 20 30 40 50 60 MTTTAQDNSP KKRQRIINCV TQLPYKIQLG ESNDDWKISA TTGNSALFSS LEYLQFDSTE 70 80 90 100 110 120 YEQHVVGWTG EITRTERNLF TREAKEKPQD LDDDPLYLTK EQINGLTTTL QDHMKSDKEA 130 140 150 160 170 180 KTDTTQTAPV TNNVHPVWLL RKNQSRWRNY AEKVIWPTFH YILNPSNEGE QEKNWWYDYV 190 200 210 220 230 240 KFNEAYAQKI GEVYRKGDII WIHDYYLLLL PQLLRMKFND ESIIIGYFHH APWPSNEYFR 250 260 270 280 290 300 CLPRRKQILD GLVGANRICF QNESFSRHFV SSCKRLLDAT AKKSKNSSNS DQYQVSVYGG 310 320 330 340 350 360 DVLVDSLPIG VNTTQILKDA FTKDIDSKVL SIKQAYQNKK IIIGRDRLDS VRGVVQKLRA 370 380 390 400 410 420 FETFLAMYPE WRDQVVLIQV SSPTANRNSP QTIRLEQQVN ELVNSINSEY GNLNFSPVQH 430 440 450 460 470 480 YYMRIPKDVY LSLLRVADLC LITSVRDGMN TTALEYVTVK SHMSNFLCYG NPLILSEFSG 490 500 510 520 530 540 SSNVLKDAIV VNPWDSVAVA KSINMALKLD KEEKSNLESK LWKEVPTIQD WTNKFLSSLK 550 560 570 580 590 600 EQASSNDDME RKMTPALNRP VLLENYKQAK RRLFLFDYDG TLTPIVKDPA AAIPSARLYT 610 620 630 640 650 660 ILQKLCADPH NQIWIISGRD QKFLNKWLGG KLPQLGLSAE HGCFMKDVSC QDWVNLTEKV 670 680 690 700 710 720 DMSWQVRVNE VMEEFTTRTP GSFIERKKVA LTWHYRRTVP ELGEFHAKEL KEKLLSFTDD 730 740 750 760 770 780 FDLEVMDGKA NIEVRPRFVN KGEIVKRLVW HQHGKPQDML KGISEKLPKD EMPDFVLCLG 790 800 810 820 830 840 DDFTDEDMFR QLNTIETCWK EKYPDQKNQW GNYGFYPVTV GSASKKTVAK AHLTDPQQVL 850 860 870 880 890 ETLGLLVGDV SLFQSAGTVD LDSRGHVKNS ESSLKSKLAS KAYVMKRSAS YTGAKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity." de Virgilio C., Buerckert N., Bell W., Jenoe P., Boller T., Wiemken A. Eur. J. Biochem. 212:315-323(1993) [PubMed: 8444170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: C13-ABYS86.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis." Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O. Mol. Cell. Biol. 11:4876-4884(1991) [PubMed: 1656215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 608-896. Strain: ATCC 208353 / W303-1A.
[4]	"Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae." Vandercammen A., Francois J., Hers H.-G. Eur. J. Biochem. 182:613-620(1989) [PubMed: 2546763] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Structural analysis of the subunits of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae and their function during heat shock." Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T., Wiemken A., De Virgilio C. Mol. Microbiol. 24:687-695(1997) [PubMed: 9194697] [Abstract] Cited for: FUNCTION, INTERACTION WITH TPS1; TPS3 AND TSL1.
[6]	"Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex." Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C., Wiemken A., Thevelein J.M. J. Biol. Chem. 273:33311-33319(1998) [PubMed: 9837904] [Abstract] Cited for: SUBUNIT.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X70694 Genomic DNA. Translation: CAA50025.1. Z46796 Genomic DNA. Translation: CAA86796.1. Z74370 Genomic DNA. Translation: CAA98893.1. X58858 Genomic DNA. Translation: CAA41661.1.
PIR	S48761.
RefSeq	NP_010359.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:823N.
IntAct	P31688. 13 interactions.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Proteomic databases
PeptideAtlas	P31688.
PRIDE	P31688.
Genome annotation databases
Ensembl	YDR074W. Saccharomyces cerevisiae. [Contig view]
GeneID	851646.
GenomeReviews	Gene locus YDR074W in contig Z71256_GR.
KEGG	sce:YDR074W.
NMPDR	fig|4932.3.peg.1104.
Organism-specific databases
CYGD	YDR074w.
SGD	S000002481. TPS2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P31688.
OMA	P31688. LMQHPEW.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-595.
BRENDA	3.1.3.12. 250.
Gene expression databases
ArrayExpress	P31688.
GermOnline	YDR074W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001830. Glyco_trans_20. IPR006379. HAD-SF_hydro_IIB. IPR003337. Trehalose_PPase. [Graphical view]
Pfam	PF00982. Glyco_transf_20. 1 hit. PF02358. Trehalose_PPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01484. HAD-SF-IIB. 1 hit. TIGR00685. T6PP. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	969224.

Entry information

Entry name

TPS2_YEAST

Accession

Primary (citable) accession number: P31688

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)