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Protein

Trehalose synthase complex regulatory subunit TSL1

Gene

TSL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • catalytic activity Source: InterPro
  • enzyme regulator activity Source: SGD

GO - Biological processi

  • dephosphorylation Source: GOC
  • regulation of catalytic activity Source: GOC
  • trehalose biosynthetic process Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17133.
YEAST:MONOMER3O-4029.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose synthase complex regulatory subunit TSL1
Alternative name(s):
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 123 kDa subunit
Gene namesi
Name:TSL1
Ordered Locus Names:YML100W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML100W.
SGDiS000004566. TSL1.

Subcellular locationi

GO - Cellular componenti

  • alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10981098Trehalose synthase complex regulatory subunit TSL1PRO_0000122511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei161 – 1611PhosphoserineCombined sources
Modified residuei229 – 2291PhosphoserineCombined sources
Modified residuei251 – 2511PhosphothreonineCombined sources
Modified residuei303 – 3031PhosphoserineCombined sources
Modified residuei815 – 8151PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38427.
PeptideAtlasiP38427.

PTM databases

iPTMnetiP38427.

Expressioni

Inductioni

Repressed by glucose.

Interactioni

Subunit structurei

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 TSL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TPS1Q007647EBI-19638,EBI-19430
TPS2P316883EBI-19638,EBI-19440

Protein-protein interaction databases

BioGridi35043. 36 interactions.
DIPiDIP-753N.
IntActiP38427. 12 interactions.
MINTiMINT-640795.

Structurei

3D structure databases

ProteinModelPortaliP38427.
SMRiP38427. Positions 421-797.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati144 – 15071
Repeati158 – 16472

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 164212 X 7 AA repeats of R-I-A-S-P-I-QAdd
BLAST
Regioni320 – 812493TPS complex domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 454Poly-Gln
Compositional biasi164 – 1685Poly-Gln

Domaini

C-terminal 700 AA are mainly in alpha-helices and beta-sheets.

Sequence similaritiesi

In the C-terminal section; belongs to the glycosyltransferase 20 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000179930.
InParanoidiP38427.
KOiK16055.
OMAiCHEFIVC.
OrthoDBiEOG76QFS6.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequencei

Sequence statusi: Complete.

P38427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALIVASLFL PYQPQFELDT SLPENSQVDS SLVNIQAMAN DQQQQRALSN
60 70 80 90 100
NISQESLVAP APEQGVPPAI SRSATRSPSA FNRASSTTNT ATLDDLVSSD
110 120 130 140 150
IFMENLTANA TTSHTPTSKT MLKPRKNGSV ERFFSPSSNI PTDRIASPIQ
160 170 180 190 200
HEHDSGSRIA SPIQQQQQDP TTNLLKNVNK SLLVHSLLNN TSQTSLEGPN
210 220 230 240 250
NHIVTPKSRA GNRPTSAATS LVNRTKQGSA SSGSSGSSAP PSIKRITPHL
260 270 280 290 300
TASAAKQRPL LAKQPSNLKY SELADISSSE TSSQHNESDP DDLTTAPDEE
310 320 330 340 350
YVSDLEMDDA KQDYKVPKFG GYSNKSKLKK YALLRSSQEL FSRLPWSIVP
360 370 380 390 400
SIKGNGAMKN AINTAVLENI IPHRHVKWVG TVGIPTDEIP ENILANISDS
410 420 430 440 450
LKDKYDSYPV LTDDDTFKAA YKNYCKQILW PTLHYQIPDN PNSKAFEDHS
460 470 480 490 500
WKFYRNLNQR FADAIVKIYK KGDTIWIHDY HLMLVPQMVR DVLPFAKIGF
510 520 530 540 550
TLHVSFPSSE VFRCLAQREK ILEGLTGADF VGFQTREYAR HFLQTSNRLL
560 570 580 590 600
MADVVHDEEL KYNGRVVSVR FTPVGIDAFD LQSQLKDGSV MQWRQLIRER
610 620 630 640 650
WQGKKLIVCR DQFDRIRGIH KKLLAYEKFL VENPEYVEKS TLIQICIGSS
660 670 680 690 700
KDVELERQIM IVVDRINSLS TNISISQPVV FLHQDLDFSQ YLALSSEADL
710 720 730 740 750
FVVSSLREGM NLTCHEFIVC SEDKNAPLLL SEFTGSASLL NDGAIIINPW
760 770 780 790 800
DTKNFSQAIL KGLEMPFDKR RPQWKKLMKD IINNDSTNWI KTSLQDIHIS
810 820 830 840 850
WQFNQEGSKI FKLNTKTLME DYQSSKKRMF VFNIAEPPSS RMISILNDMT
860 870 880 890 900
SKGNIVYIMN SFPKPILENL YSRVQNIGLI AENGAYVSLN GVWYNIVDQV
910 920 930 940 950
DWRNDVAKIL EDKVERLPGS YYKINESMIK FHTENAEDQD RVASVIGDAI
960 970 980 990 1000
THINTVFDHR GIHAYVYKNV VSVQQVGLSL SAAQFLFRFY NSASDPLDTS
1010 1020 1030 1040 1050
SGQITNIQTP SQQNPSDQEQ QPPASPTVSM NHIDFACVSG SSSPVLEPLF
1060 1070 1080 1090
KLVNDEASEG QVKAGHAIVY GDATSTYAKE HVNGLNELFT IISRIIED
Length:1,098
Mass (Da):123,018
Last modified:October 1, 1994 - v1
Checksum:iEA0A8A86AF178F04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72788 Genomic DNA. Translation: CAA51303.1.
X80835 Genomic DNA. Translation: CAA56797.1.
BK006946 Genomic DNA. Translation: DAA09799.1.
PIRiS36868.
RefSeqiNP_013608.1. NM_001182460.1.

Genome annotation databases

EnsemblFungiiYML100W; YML100W; YML100W.
GeneIDi854872.
KEGGisce:YML100W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72788 Genomic DNA. Translation: CAA51303.1.
X80835 Genomic DNA. Translation: CAA56797.1.
BK006946 Genomic DNA. Translation: DAA09799.1.
PIRiS36868.
RefSeqiNP_013608.1. NM_001182460.1.

3D structure databases

ProteinModelPortaliP38427.
SMRiP38427. Positions 421-797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35043. 36 interactions.
DIPiDIP-753N.
IntActiP38427. 12 interactions.
MINTiMINT-640795.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

PTM databases

iPTMnetiP38427.

Proteomic databases

MaxQBiP38427.
PeptideAtlasiP38427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML100W; YML100W; YML100W.
GeneIDi854872.
KEGGisce:YML100W.

Organism-specific databases

EuPathDBiFungiDB:YML100W.
SGDiS000004566. TSL1.

Phylogenomic databases

GeneTreeiENSGT00550000075394.
HOGENOMiHOG000179930.
InParanoidiP38427.
KOiK16055.
OMAiCHEFIVC.
OrthoDBiEOG76QFS6.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17133.
YEAST:MONOMER3O-4029.

Miscellaneous databases

PROiP38427.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 204508 / S288c.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-77; SER-135; SER-147; SER-161; SER-303 AND THR-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-53; SER-56; SER-71; SER-161 AND SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTSL1_YEAST
AccessioniPrimary (citable) accession number: P38427
Secondary accession number(s): D6W0I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 8, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.