Trehalose synthase complex regulatory subunit TSL1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38427 (TSL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Trehalose synthase complex regulatory subunit TSL1

Alternative name(s):
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 123 kDa subunit

Gene names

Name:	TSL1
Ordered Locus Names:	YML100W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1098 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex, and confer sensitivity to physiological concentrations of phosphate and to fructose 6-phosphate. Ref.4
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.5
Subcellular location	Cytoplasm Ref.7.
Induction	Repressed by glucose.
Domain	C-terminal 700 AA are mainly in alpha-helices and beta-sheets.
Miscellaneous	Present with 1960 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	In the C-terminal section; belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	response to stress Inferred from mutant phenotype Ref.5. Source: SGD trehalose biosynthetic process Inferred from physical interaction. Source: SGD
Cellular component	alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Inferred from mutant phenotype Ref.5. Source: SGD
Molecular function	catalytic activity Inferred from electronic annotation. Source: InterPro enzyme regulator activity Inferred from direct assay Ref.1. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TPS1	Q00764	7	EBI-19638,EBI-19430
TPS2	P31688	3	EBI-19638,EBI-19440

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1098

1098

Trehalose synthase complex regulatory subunit TSL1

PRO_0000122511

Regions

Repeat

144 – 150

Repeat

158 – 164

Region

144 – 164

2 X 7 AA repeats of R-I-A-S-P-I-Q

Region

320 – 812

493

TPS complex domain

Compositional bias

42 – 45

Poly-Gln

Compositional bias

164 – 168

Poly-Gln

Amino acid modifications

Modified residue

Phosphoserine Ref.9 Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphothreonine Ref.6 Ref.9 Ref.11

Modified residue

Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12

Modified residue

Phosphoserine Ref.11 Ref.12

Modified residue

113

Phosphoserine Ref.12

Modified residue

115

Phosphothreonine Ref.12

Modified residue

118

Phosphoserine Ref.12

Modified residue

135

Phosphoserine Ref.12

Modified residue

147

Phosphoserine Ref.11 Ref.12

Modified residue

161

Phosphoserine Ref.9 Ref.12

Modified residue

191

Phosphothreonine Ref.12

Modified residue

192

Phosphoserine Ref.11 Ref.12

Modified residue

247

Phosphothreonine Ref.10

Modified residue

251

Phosphothreonine Ref.10

Modified residue

303

Phosphoserine Ref.12

Modified residue

337

Phosphoserine Ref.12

Modified residue

815

Phosphothreonine Ref.12

Modified residue

1042

Phosphoserine Ref.12

Modified residue

1043

Phosphoserine Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P38427 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: EA0A8A86AF178F04
Show »

FASTA

1,098

123,018

        10         20         30         40         50         60 
MALIVASLFL PYQPQFELDT SLPENSQVDS SLVNIQAMAN DQQQQRALSN NISQESLVAP 

        70         80         90        100        110        120 
APEQGVPPAI SRSATRSPSA FNRASSTTNT ATLDDLVSSD IFMENLTANA TTSHTPTSKT 

       130        140        150        160        170        180 
MLKPRKNGSV ERFFSPSSNI PTDRIASPIQ HEHDSGSRIA SPIQQQQQDP TTNLLKNVNK 

       190        200        210        220        230        240 
SLLVHSLLNN TSQTSLEGPN NHIVTPKSRA GNRPTSAATS LVNRTKQGSA SSGSSGSSAP 

       250        260        270        280        290        300 
PSIKRITPHL TASAAKQRPL LAKQPSNLKY SELADISSSE TSSQHNESDP DDLTTAPDEE 

       310        320        330        340        350        360 
YVSDLEMDDA KQDYKVPKFG GYSNKSKLKK YALLRSSQEL FSRLPWSIVP SIKGNGAMKN 

       370        380        390        400        410        420 
AINTAVLENI IPHRHVKWVG TVGIPTDEIP ENILANISDS LKDKYDSYPV LTDDDTFKAA 

       430        440        450        460        470        480 
YKNYCKQILW PTLHYQIPDN PNSKAFEDHS WKFYRNLNQR FADAIVKIYK KGDTIWIHDY 

       490        500        510        520        530        540 
HLMLVPQMVR DVLPFAKIGF TLHVSFPSSE VFRCLAQREK ILEGLTGADF VGFQTREYAR 

       550        560        570        580        590        600 
HFLQTSNRLL MADVVHDEEL KYNGRVVSVR FTPVGIDAFD LQSQLKDGSV MQWRQLIRER 

       610        620        630        640        650        660 
WQGKKLIVCR DQFDRIRGIH KKLLAYEKFL VENPEYVEKS TLIQICIGSS KDVELERQIM 

       670        680        690        700        710        720 
IVVDRINSLS TNISISQPVV FLHQDLDFSQ YLALSSEADL FVVSSLREGM NLTCHEFIVC 

       730        740        750        760        770        780 
SEDKNAPLLL SEFTGSASLL NDGAIIINPW DTKNFSQAIL KGLEMPFDKR RPQWKKLMKD 

       790        800        810        820        830        840 
IINNDSTNWI KTSLQDIHIS WQFNQEGSKI FKLNTKTLME DYQSSKKRMF VFNIAEPPSS 

       850        860        870        880        890        900 
RMISILNDMT SKGNIVYIMN SFPKPILENL YSRVQNIGLI AENGAYVSLN GVWYNIVDQV 

       910        920        930        940        950        960 
DWRNDVAKIL EDKVERLPGS YYKINESMIK FHTENAEDQD RVASVIGDAI THINTVFDHR 

       970        980        990       1000       1010       1020 
GIHAYVYKNV VSVQQVGLSL SAAQFLFRFY NSASDPLDTS SGQITNIQTP SQQNPSDQEQ 

      1030       1040       1050       1060       1070       1080 
QPPASPTVSM NHIDFACVSG SSSPVLEPLF KLVNDEASEG QVKAGHAIVY GDATSTYAKE 

      1090 
HVNGLNELFT IISRIIED

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of two related genes encoding the 56-kDa and 123-kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae." Vuorio O.E., Kalkkinen N., Londesborough J. Eur. J. Biochem. 216:849-861(1993) [PubMed: 8404905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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 AND TPS2.
[5]	"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.
[6]	"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 THR-75 AND SER-77, MASS SPECTROMETRY. Strain: 2124.
[7]	"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].
[8]	"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].
[9]	"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-49; THR-75; SER-77 AND SER-161, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-247 AND THR-251, 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 THR-75; SER-77; SER-79; SER-147 AND SER-192, 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-49; SER-53; SER-56; SER-71; SER-73; SER-77; SER-79; SER-113; THR-115; SER-118; SER-135; SER-147; SER-161; THR-191; SER-192; SER-303; SER-337; THR-815; SER-1042 AND SER-1043, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X72788 Genomic DNA. Translation: CAA51303.1. X80835 Genomic DNA. Translation: CAA56797.1. BK006946 Genomic DNA. Translation: DAA09799.1.
PIR	S36868.
RefSeq	NP_013608.1. NM_001182460.1.
3D structure databases
ProteinModelPortal	P38427.
SMR	P38427. Positions 354-802.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-753N.
IntAct	P38427. 14 interactions.
MINT	MINT-640795.
STRING	P38427.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Proteomic databases
PeptideAtlas	P38427.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML100W; YML100W; YML100W.
GeneID	854872.
KEGG	sce:YML100W.
NMPDR	fig\|4932.3.peg.4645.
Organism-specific databases
CYGD	YML100w.
SGD	S000004566. TSL1.
Phylogenomic databases
eggNOG	fuNOG04259.
GeneTree	EFGT00050000003176.
HOGENOM	HBG325476.
OMA	CHEFIVC.
OrthoDB	EOG4JQ762.
Gene expression databases
ArrayExpress	P38427.
Genevestigator	P38427.
GermOnline	YML100W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001830. Glyco_trans_20. IPR023214. HAD-like_dom. IPR003337. Trehalose_PPase. [Graphical view]
KO	K00697.
Pfam	PF00982. Glyco_transf_20. 1 hit. PF02358. Trehalose_PPase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
ProtoNet	Search...
Other
NextBio	977807.

Entry information

Entry name

TSL1_YEAST

Accession

Primary (citable) accession number: P38427
Secondary accession number(s): D6W0I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents