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O23617

- TPS5_ARATH

UniProt

O23617 - TPS5_ARATH

Protein

Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5

Gene

TPS5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

    GO - Biological processi

    1. trehalose biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:TPS5
    Ordered Locus Names:At4g17770
    ORF Names:dl4920W, FCAALL.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G17770.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51S → A: Abolishes binding to GRF/14-3-3. 1 Publication
    Mutagenesisi32 – 321T → A: Abolishes binding to GRF/14-3-3. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 862862Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5PRO_0000324826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphoserine1 Publication
    Modified residuei32 – 321Phosphothreonine1 Publication

    Post-translational modificationi

    Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO23617.
    PRIDEiO23617.

    Expressioni

    Tissue specificityi

    Low expression in leaves, stems, flower buds, flowers and siliques.1 Publication

    Inductioni

    90-fold induction by sucrose after 24 hours and by heat stress.2 Publications

    Gene expression databases

    ArrayExpressiO23617.
    GenevestigatoriO23617.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi12791. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliO23617.
    SMRiO23617. Positions 144-546, 589-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 546487GlycosyltransferaseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0380.
    HOGENOMiHOG000191476.
    InParanoidiO23617.
    KOiK16055.
    OMAiSHRNSAG.
    PhylomeDBiO23617.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR001830. Glyco_trans_20.
    IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view]
    PfamiPF00982. Glyco_transf_20. 1 hit.
    PF02358. Trehalose_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O23617-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSRSYSNLL DLASGNFHSF SREKKRFPRV ATVTGVLSEL DDDNNSNSVC    50
    SDAPSSVTQD RIIIVGNQLP IKSHRNSAGK LSFSWDNDSL LLQLKDGMRE 100
    DMEVVYIGCL KEQIDTVEQD DVSQRLLENF KCVPAYIPPE LFTKYYHGFC 150
    KQHLWPLFHY MLPLTPDLGG RFDRSLWQAY LSVNKIFADK VMEVISPDDD 200
    FVWVHDYHLM VLPTFLRKRF NRVKLGFFLH SPFPSSEIYR TLPVRNELLR 250
    ALLNADLIGF HTFDYARHFL SCCSRMLGLS YQSKRGTIGL EYYGRTVSIK 300
    ILPVGIHISQ LQSILNLPET QTKVAELRDQ FLDQKVLLGV DDMDIFKGIS 350
    LKLLAMEQLL TQHPEKRGRV VLVQIANPAR GRGKDVQEVQ SETEATVKRI 400
    NEMFGRPGYQ PVVLIDTPLQ FFERIAYYVI AECCLVTAVR DGMNLIPYEY 450
    IICRQGNPKL NETIGLDPSA AKKSMLVVSE FIGCSPSLSG AIRVNPWNID 500
    AVTEAMDYAL IVSEAEKQMR HEKHHKYVST HDVAYWARSF IQDLERACGD 550
    HVRKRCWGIG FGLGFRVVAL DPSFKKLSIE HIVSAYKRTK NRAILLDYDG 600
    TMVQPGSIRT TPTRETIEIL NNLSSDPKNI VYLVSGKDRR TLTEWFSSCD 650
    DLGLGAEHGY FIRPNDGTDW ETSSLVSGFE WKQIAEPVMR LYTETTDGST 700
    IETKETALVW NYQFADPDFG SCQAKELMEH LESVLTNDPV SVKTGQQLVE 750
    VKPQGVNKGL VAERLLTTMQ EKGKLLDFIL CVGDDRSDED MFEVIMSAKD 800
    GPALSPVAEI FACTVGQKPS KAKYYLDDTA EIIRMLDGLA ATNTTISDQT 850
    DSTATVPTKD LF 862
    Length:862
    Mass (Da):97,454
    Last modified:March 18, 2008 - v2
    Checksum:iADA155DB26DCB470
    GO

    Sequence cautioni

    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiH71447.
    RefSeqiNP_567538.1. NM_117886.2.
    UniGeneiAt.4501.

    Genome annotation databases

    EnsemblPlantsiAT4G17770.1; AT4G17770.1; AT4G17770.
    GeneIDi827498.
    KEGGiath:AT4G17770.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi H71447.
    RefSeqi NP_567538.1. NM_117886.2.
    UniGenei At.4501.

    3D structure databases

    ProteinModelPortali O23617.
    SMRi O23617. Positions 144-546, 589-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 12791. 2 interactions.

    Protein family/group databases

    CAZyi GT20. Glycosyltransferase Family 20.

    Proteomic databases

    PaxDbi O23617.
    PRIDEi O23617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G17770.1 ; AT4G17770.1 ; AT4G17770 .
    GeneIDi 827498.
    KEGGi ath:AT4G17770.

    Organism-specific databases

    TAIRi AT4G17770.

    Phylogenomic databases

    eggNOGi COG0380.
    HOGENOMi HOG000191476.
    InParanoidi O23617.
    KOi K16055.
    OMAi SHRNSAG.
    PhylomeDBi O23617.

    Gene expression databases

    ArrayExpressi O23617.
    Genevestigatori O23617.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR001830. Glyco_trans_20.
    IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view ]
    Pfami PF00982. Glyco_transf_20. 1 hit.
    PF02358. Trehalose_PPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.
      , 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. 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].

    Entry informationi

    Entry nameiTPS5_ARATH
    AccessioniPrimary (citable) accession number: O23617
    Secondary accession number(s): Q8GWQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3