Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O23617 (TPS5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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] 5

EC=2.4.1.15
Alternative name(s):
Trehalose-6-phosphate synthase 5
Short name=AtTPS5
Gene names
Name:TPS5
Ordered Locus Names:At4g17770
ORF Names:dl4920W, FCAALL.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Binds to the phosphopeptide-binding site of GRF/14-3-3 and to MBF1c. Ref.9 Ref.10

Tissue specificity

Low expression in leaves, stems, flower buds, flowers and siliques. Ref.8

Induction

90-fold induction by sucrose after 24 hours and by heat stress. Ref.7 Ref.10

Post-translational modification

Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3. Ref.9

Miscellaneous

2-deoxyglucose, but not phenformin, enhances the phosphorylation of TPS5.

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 caution

The sequence CAB10557.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB78780.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5
PRO_0000324826

Regions

Region60 – 546487Glycosyltransferase

Amino acid modifications

Modified residue51Phosphoserine Ref.9
Modified residue321Phosphothreonine Ref.9

Experimental info

Mutagenesis51S → A: Abolishes binding to GRF/14-3-3. Ref.9
Mutagenesis321T → A: Abolishes binding to GRF/14-3-3. Ref.9

Sequences

Sequence LengthMass (Da)Tools
O23617 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: ADA155DB26DCB470

FASTA86297,454
        10         20         30         40         50         60 
MVSRSYSNLL DLASGNFHSF SREKKRFPRV ATVTGVLSEL DDDNNSNSVC SDAPSSVTQD 

        70         80         90        100        110        120 
RIIIVGNQLP IKSHRNSAGK LSFSWDNDSL LLQLKDGMRE DMEVVYIGCL KEQIDTVEQD 

       130        140        150        160        170        180 
DVSQRLLENF KCVPAYIPPE LFTKYYHGFC KQHLWPLFHY MLPLTPDLGG RFDRSLWQAY 

       190        200        210        220        230        240 
LSVNKIFADK VMEVISPDDD FVWVHDYHLM VLPTFLRKRF NRVKLGFFLH SPFPSSEIYR 

       250        260        270        280        290        300 
TLPVRNELLR ALLNADLIGF HTFDYARHFL SCCSRMLGLS YQSKRGTIGL EYYGRTVSIK 

       310        320        330        340        350        360 
ILPVGIHISQ LQSILNLPET QTKVAELRDQ FLDQKVLLGV DDMDIFKGIS LKLLAMEQLL 

       370        380        390        400        410        420 
TQHPEKRGRV VLVQIANPAR GRGKDVQEVQ SETEATVKRI NEMFGRPGYQ PVVLIDTPLQ 

       430        440        450        460        470        480 
FFERIAYYVI AECCLVTAVR DGMNLIPYEY IICRQGNPKL NETIGLDPSA AKKSMLVVSE 

       490        500        510        520        530        540 
FIGCSPSLSG AIRVNPWNID AVTEAMDYAL IVSEAEKQMR HEKHHKYVST HDVAYWARSF 

       550        560        570        580        590        600 
IQDLERACGD HVRKRCWGIG FGLGFRVVAL DPSFKKLSIE HIVSAYKRTK NRAILLDYDG 

       610        620        630        640        650        660 
TMVQPGSIRT TPTRETIEIL NNLSSDPKNI VYLVSGKDRR TLTEWFSSCD DLGLGAEHGY 

       670        680        690        700        710        720 
FIRPNDGTDW ETSSLVSGFE WKQIAEPVMR LYTETTDGST IETKETALVW NYQFADPDFG 

       730        740        750        760        770        780 
SCQAKELMEH LESVLTNDPV SVKTGQQLVE VKPQGVNKGL VAERLLTTMQ EKGKLLDFIL 

       790        800        810        820        830        840 
CVGDDRSDED MFEVIMSAKD GPALSPVAEI FACTVGQKPS KAKYYLDDTA EIIRMLDGLA 

       850        860 
ATNTTISDQT DSTATVPTKD LF 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. expand/collapse author list , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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].
Strain: cv. Columbia.
[5]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"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.
[7]"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.
[8]"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: TISSUE SPECIFICITY.
[9]"Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose."
Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C., Mackintosh C.
Plant J. 47:211-223(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-5 AND THR-32, MUTAGENESIS OF SER-5 AND THR-32, INTERACTION WITH GRF/14-3-3, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"The transcriptional co-activator MBF1c is a key regulator of thermotolerance in Arabidopsis thaliana."
Suzuki N., Bajad S., Shuman J., Shulaev V., Mittler R.
J. Biol. Chem. 283:9269-9275(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBF1C, INDUCTION BY HEAT.
[11]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z97344 Genomic DNA. Translation: CAB10557.1. Sequence problems.
AL161547 Genomic DNA. Translation: CAB78780.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83948.1.
BT005967 mRNA. Translation: AAO64902.1.
AK118703 mRNA. Translation: BAC43297.1.
PIRH71447.
RefSeqNP_567538.1. NM_117886.2.
UniGeneAt.4501.

3D structure databases

ProteinModelPortalO23617.
SMRO23617. Positions 60-548, 589-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid12791. 2 interactions.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbO23617.
PRIDEO23617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G17770.1; AT4G17770.1; AT4G17770.
GeneID827498.
KEGGath:AT4G17770.

Organism-specific databases

TAIRAT4G17770.

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191476.
InParanoidO23617.
KOK16055.
OMAMEVISPD.
PhylomeDBO23617.
ProtClustDBCLSN2917573.

Gene expression databases

ArrayExpressO23617.
GenevestigatorO23617.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR001830. Glyco_trans_20.
IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR003337. Trehalose_PPase.
[Graphical view]
PfamPF00982. Glyco_transf_20. 1 hit.
PF02358. Trehalose_PPase. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
TIGR00685. T6PP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPS5_ARATH
AccessionPrimary (citable) accession number: O23617
Secondary accession number(s): Q8GWQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 85 of the entry and version 2 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