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Q9SYM4 (TPS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1

EC=2.4.1.15
Alternative name(s):
Trehalose-6-phosphate synthase 1
Short name=AtTPS1
Gene names
Name:TPS1
Ordered Locus Names:At1g78580
ORF Names:T30F21.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal embryo development, vegetative growth and transition to flowering. Regulates embryo growth, cell wall deposition, starch and sucrose degradation, but not cell differentiation. Involved in the regulation of glucose sensing and signaling genes during plant development. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14

Catalytic activity

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

Subcellular location

Vacuole. Secretedcell wall. Cytoplasm. Note: Determined in transgenic tobacco plants expressing TPS1. Ref.15

Tissue specificity

Expressed in seedlings, leaves, roots, stems, flowers and siliques. Ref.1 Ref.6 Ref.8

Developmental stage

Up-regulated during seed development. Ref.8

Induction

Low induction by sucrose after 24 hours. Down-regulated by dark incubation. Ref.6 Ref.10

Domain

The N-terminal part (1-88) has an inhibitory function on the enzymatic activity.

Disruption phenotype

Embryonic lethality. Ref.8 Ref.11 Ref.13 Ref.14

Sequence similarities

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

In the C-terminal section; belongs to the trehalose phosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 942942Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1
PRO_0000324822

Regions

Region92 – 559468Glycosyltransferase
Compositional bias71 – 766Poly-Ala
Compositional bias822 – 89069Ser-rich

Experimental info

Mutagenesis171R → Q: 3-fold increase in activity. Ref.7
Mutagenesis271L → P: 4-fold increase in activity. Ref.7
Sequence conflict1051A → P in CAA69879. Ref.1
Sequence conflict3481I → K in CAA69879. Ref.1
Sequence conflict359 – 3602AG → TD in CAA69879. Ref.1
Sequence conflict4011Q → K in CAA69879. Ref.1
Sequence conflict4081T → P in CAA69879. Ref.1
Sequence conflict4151K → T in CAA69879. Ref.1
Sequence conflict4281N → I in CAA69879. Ref.1
Sequence conflict4311F → L in CAA69879. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9SYM4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B22AC11EA34CDDDB

FASTA942105,976
        10         20         30         40         50         60 
MPGNKYNCSS SHIPLSRTER LLRDRELREK RKSNRARNPN DVAGSSENSE NDLRLEGDSS 

        70         80         90        100        110        120 
RQYVEQYLEG AAAAMAHDDA CERQEVRPYN RQRLLVVANR LPVSAVRRGE DSWSLEISAG 

       130        140        150        160        170        180 
GLVSALLGVK EFEARWIGWA GVNVPDEVGQ KALSKALAEK RCIPVFLDEE IVHQYYNGYC 

       190        200        210        220        230        240 
NNILWPLFHY LGLPQEDRLA TTRSFQSQFA AYKKANQMFA DVVNEHYEEG DVVWCHDYHL 

       250        260        270        280        290        300 
MFLPKCLKEY NSKMKVGWFL HTPFPSSEIH RTLPSRSELL RSVLAADLVG FHTYDYARHF 

       310        320        330        340        350        360 
VSACTRILGL EGTPEGVEDQ GRLTRVAAFP IGIDSDRFIR ALEVPEVIQH MKELKERFAG 

       370        380        390        400        410        420 
RKVMLGVDRL DMIKGIPQKI LAFEKFLEEN ANWRDKVVLL QIAVPTRTDV PEYQKLTSQV 

       430        440        450        460        470        480 
HEIVGRINGR FGTLTAVPIH HLDRSLDFHA LCALYAVTDV ALVTSLRDGM NLVSYEFVAC 

       490        500        510        520        530        540 
QEAKKGVLIL SEFAGAAQSL GAGAILVNPW NITEVAASIG QALNMTAEER EKRHRHNFHH 

       550        560        570        580        590        600 
VKTHTAQEWA ETFVSELNDT VIEAQLRISK VPPELPQHDA IQRYSKSNNR LLILGFNATL 

       610        620        630        640        650        660 
TEPVDNQGRR GDQIKEMDLN LHPELKGPLK ALCSDPSTTI VVLSGSSRSV LDKNFGEYDM 

       670        680        690        700        710        720 
WLAAENGMFL RLTNGEWMTT MPEHLNMEWV DSVKHVFKYF TERTPRSHFE TRDTSLIWNY 

       730        740        750        760        770        780 
KYADIEFGRL QARDLLQHLW TGPISNASVD VVQGSRSVEV RAVGVTKGAA IDRILGEIVH 

       790        800        810        820        830        840 
SKSMTTPIDY VLCIGHFLGK DEDVYTFFEP ELPSDMPAIA RSRPSSDSGA KSSSGDRRPP 

       850        860        870        880        890        900 
SKSTHNNNKS GSKSSSSSNS NNNNKSSQRS LQSERKSGSN HSLGNSRRPS PEKISWNVLD 

       910        920        930        940 
LKGENYFSCA VGRTRTNARY LLGSPDDVVC FLEKLADTTS SP 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and molecular characterization of the Arabidopsis TPS1 gene, encoding trehalose-6-phosphate synthase."
Blazquez M.A., Santos E., Flores C.L., Martinez-Zapater J.M., Salinas J., Gancedo C.
Plant J. 13:685-689(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-942.
Strain: cv. Columbia.
[5]"An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana."
Leyman B., Van Dijck P., Thevelein J.M.
Trends Plant Sci. 6:510-513(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[6]"Trehalose metabolism in Arabidopsis: occurrence of trehalose and molecular cloning and characterization of trehalose-6-phosphate synthase homologues."
Vogel G., Fiehn O., Jean-Richard-dit-Bressel L., Boller T., Wiemken A., Aeschbacher R.A., Wingler A.
J. Exp. Bot. 52:1817-1826(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Landsberg erecta.
[7]"Truncation of Arabidopsis thaliana and Selaginella lepidophylla trehalose-6-phosphate synthase unlocks high catalytic activity and supports high trehalose levels on expression in yeast."
Van Dijck P., Mascorro-Gallardo J.O., De Bus M., Royackers K., Iturriaga G., Thevelein J.M.
Biochem. J. 366:63-71(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-17 AND LEU-27.
[8]"Trehalose-6-phosphate synthase 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo maturation."
Eastmond P.J., van Dijken A.J.H., Spielman M., Kerr A., Tissier A.F., Dickinson H.G., Jones J.D.G., Smeekens S.C., Graham I.A.
Plant J. 29:225-235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[9]"Trehalose 6-phosphate is indispensable for carbohydrate utilization and growth in Arabidopsis thaliana."
Schluepmann H., Pellny T., van Dijken A.J.H., Smeekens S.C.M., Paul M.
Proc. Natl. Acad. Sci. U.S.A. 100:6849-6854(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Trehalose mediated growth inhibition of Arabidopsis seedlings is due to trehalose-6-phosphate accumulation."
Schluepmann H., van Dijken A.J.H., Aghdasi M., Wobbes B., Paul M., Smeekens S.C.M.
Plant Physiol. 135:879-890(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SUCROSE.
[11]"Arabidopsis trehalose-6-phosphate synthase 1 is essential for normal vegetative growth and transition to flowering."
van Dijken A.J.H., Schluepmann H., Smeekens S.C.M.
Plant Physiol. 135:969-977(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[12]"Trehalose metabolism and glucose sensing in plants."
Avonce N., Leyman B., Thevelein J., Iturriaga G.
Biochem. Soc. Trans. 33:276-279(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"The role of trehalose-6-phosphate synthase in Arabidopsis embryo development."
Gomez L.D., Baud S., Graham I.A.
Biochem. Soc. Trans. 33:280-282(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]"Delayed embryo development in the ARABIDOPSIS TREHALOSE-6-PHOSPHATE SYNTHASE 1 mutant is associated with altered cell wall structure, decreased cell division and starch accumulation."
Gomez L.D., Baud S., Gilday A., Li Y., Graham I.A.
Plant J. 46:69-84(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]"Immunogold localization of trehalose-6-phosphate synthase in leaf segments of wild-type and transgenic tobacco plants expressing the AtTPS1 gene from Arabidopsis thaliana."
Almeida A.M., Santos M., Villalobos E., Araujo S.S., van Dijck P., Leyman B., Cardoso L.A., Santos D., Fevereiro P.S., Torne J.M.
Protoplasma 230:41-49(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08568 mRNA. Translation: CAA69879.1.
AC007260 Genomic DNA. Translation: AAD30578.1.
CP002684 Genomic DNA. Translation: AEE36123.1.
AF370287 mRNA. Translation: AAK44102.2.
PIRD96814.
RefSeqNP_177979.1. NM_106505.4.
UniGeneAt.198.
At.71030.

3D structure databases

ProteinModelPortalQ9SYM4.
SMRQ9SYM4. Positions 93-561.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbQ9SYM4.
PRIDEQ9SYM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G78580.1; AT1G78580.1; AT1G78580.
GeneID844194.
KEGGath:AT1G78580.

Organism-specific databases

TAIRAT1G78580.

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191477.
InParanoidQ9SYM4.
KOK16055.
OMAPYAYQAV.
PhylomeDBQ9SYM4.
ProtClustDBPLN03064.

Gene expression databases

GenevestigatorQ9SYM4.

Family and domain databases

Gene3D3.40.50.1000. 3 hits.
InterProIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR012766. Trehalose_OtsA.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02400. trehalose_OtsA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPS1_ARATH
AccessionPrimary (citable) accession number: Q9SYM4
Secondary accession number(s): P93653, Q94K55
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names