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Protein

Probable trehalose-phosphate phosphatase 2

Gene

TPP2

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.1 Publication

Catalytic activityi

Trehalose 6-phosphate + H2O = trehalose + phosphate.1 Publication

Cofactori

Kineticsi

  1. KM=186 µM for trehalose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Pathwayi: trehalose biosynthesis

    This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

    GO - Molecular functioni

    • trehalose-phosphatase activity Source: UniProtKB

    GO - Biological processi

    • trehalose biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BRENDAi3.1.3.12. 8948.
    UniPathwayiUPA00299.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable trehalose-phosphate phosphatase 2 (EC:3.1.3.12)
    Short name:
    OsTPP2
    Alternative name(s):
    Trehalose 6-phosphate phosphatase
    Gene namesi
    Name:TPP2
    Ordered Locus Names:Os10g0553300, LOC_Os10g40550
    ORF Names:OSJNBa0015J15.3
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
    Proteomesi
    • UP000059680 Componenti: Chromosome 10

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 382382Probable trehalose-phosphate phosphatase 2PRO_0000417654Add
    BLAST

    Proteomic databases

    PaxDbiQ9FWQ2.
    PRIDEiQ9FWQ2.

    Expressioni

    Tissue specificityi

    Expressed in roots and shoots.1 Publication

    Inductioni

    By cold, drought, salt stress and abscisic acid (ABA).1 Publication

    Gene expression databases

    ExpressionAtlasiQ9FWQ2. baseline and differential.
    GenevisibleiQ9FWQ2. OS.

    Interactioni

    Protein-protein interaction databases

    STRINGi39947.LOC_Os10g40550.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FWQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the trehalose phosphatase family.Curated

    Phylogenomic databases

    eggNOGiENOG410IMM9. Eukaryota.
    COG1877. LUCA.
    InParanoidiQ9FWQ2.
    KOiK01087.
    OMAiENALMSD.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view]
    PfamiPF02358. Trehalose_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9FWQ2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDLKTSNSPV IADPLPKLAL PSAVMTYTTP TSFPSTGLYL NTPKKKPLPG
    60 70 80 90 100
    KIEEVRAAGW LDLMLASSPP RKRQTKDFAN DVQADELDLL YRNWVVNHPS
    110 120 130 140 150
    ALTSFEDIVN LARGKRLALF LDYDGTLSPI VDNPENAVMS DEMRSAVKHV
    160 170 180 190 200
    ASLFPTAIIS GRSRDKVFDF VKLTELYYAG SHGMDIMGPV RKSDSSGQHV
    210 220 230 240 250
    ECIRSTDSEG KEVNLFQPAS EFLPMISEVY KKLSESIKDI DGARMEDNKF
    260 270 280 290 300
    CVSVHYRNVA PHDYGEVHQR VTAVLKNYPC LRLTHGRKVL EVRPVIDWNK
    310 320 330 340 350
    GKAVEFLLES LGLCGKEDVL PIYVGDDKTD EDAFKVLKAN SIGFGILVSS
    360 370 380
    VPKDTDAFYS VRDPAEVMEF LKKLASWKEE ST
    Length:382
    Mass (Da):42,578
    Last modified:March 1, 2001 - v1
    Checksum:i67940C5634E0773D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB277360 mRNA. Translation: BAF34519.1.
    AC026758 Genomic DNA. Translation: AAG13478.1.
    DP000086 Genomic DNA. Translation: AAP54952.1.
    DP000086 Genomic DNA. Translation: ABB47970.1.
    AP008216 Genomic DNA. Translation: BAF27173.1.
    AP014966 Genomic DNA. Translation: BAT11974.1.
    RefSeqiXP_015612912.1. XM_015757426.1.
    XP_015612914.1. XM_015757428.1.
    XP_015612915.1. XM_015757429.1.
    UniGeneiOs.2884.

    Genome annotation databases

    EnsemblPlantsiOS10T0553300-01; OS10T0553300-01; OS10G0553300.
    GeneIDi4349333.
    GrameneiOS10T0553300-01; OS10T0553300-01; OS10G0553300.
    KEGGiosa:4349333.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB277360 mRNA. Translation: BAF34519.1.
    AC026758 Genomic DNA. Translation: AAG13478.1.
    DP000086 Genomic DNA. Translation: AAP54952.1.
    DP000086 Genomic DNA. Translation: ABB47970.1.
    AP008216 Genomic DNA. Translation: BAF27173.1.
    AP014966 Genomic DNA. Translation: BAT11974.1.
    RefSeqiXP_015612912.1. XM_015757426.1.
    XP_015612914.1. XM_015757428.1.
    XP_015612915.1. XM_015757429.1.
    UniGeneiOs.2884.

    3D structure databases

    ProteinModelPortaliQ9FWQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi39947.LOC_Os10g40550.1.

    Proteomic databases

    PaxDbiQ9FWQ2.
    PRIDEiQ9FWQ2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiOS10T0553300-01; OS10T0553300-01; OS10G0553300.
    GeneIDi4349333.
    GrameneiOS10T0553300-01; OS10T0553300-01; OS10G0553300.
    KEGGiosa:4349333.

    Phylogenomic databases

    eggNOGiENOG410IMM9. Eukaryota.
    COG1877. LUCA.
    InParanoidiQ9FWQ2.
    KOiK01087.
    OMAiENALMSD.

    Enzyme and pathway databases

    UniPathwayiUPA00299.
    BRENDAi3.1.3.12. 8948.

    Gene expression databases

    ExpressionAtlasiQ9FWQ2. baseline and differential.
    GenevisibleiQ9FWQ2. OS.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view]
    PfamiPF02358. Trehalose_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Biochemical characterization of rice trehalose-6-phosphate phosphatases supports distinctive functions of these plant enzymes."
      Shima S., Matsui H., Tahara S., Imai R.
      FEBS J. 274:1192-1201(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. Yukihikari.
    2. "In-depth view of structure, activity, and evolution of rice chromosome 10."
      Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.
      , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
      Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    4. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    5. Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    6. "Functional identification of a trehalose 6-phosphate phosphatase gene that is involved in transient induction of trehalose biosynthesis during chilling stress in rice."
      Pramanik M.H., Imai R.
      Plant Mol. Biol. 58:751-762(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
      Strain: cv. Yukihikari.

    Entry informationi

    Entry nameiTPP2_ORYSJ
    AccessioniPrimary (citable) accession number: Q9FWQ2
    Secondary accession number(s): A0A0P0XX17, Q7XCC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: March 1, 2001
    Last modified: July 6, 2016
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    3. SIMILARITY comments
      Index of protein domains and families

    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.