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Protein

Serine/threonine-protein phosphatase 7

Gene

PP7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphatase active on para-nitrophenylphosphate (pNPP) and on various phosphoproteins such as myelin basic protein. Seems to act as a positive regulator of cryptochrome signaling involved in hypocotyl growth inhibition and cotyledon expansion under white and blue light conditions. Confers thermotolerance. Required for heat shock mediated-signaling pathway that leads to the expression of heat shock proteins (HSPs).3 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Enzyme regulationi

Inhibited by NaF and orthovanadate, as well as by divalent cations such as Ni2+ and Zn2+. Inhibited by polylysine with myelin basic protein as substrate, but activated by polylysine with pNPP as substrate. Reversibly regulated by redox agents. Inhibited by submillimolar Pi concentrations. Slightly repressed by calmodulin (CaM).1 Publication

Kineticsi

  1. KM=1.7 mM for pNPP (at pH 7.8 and 25 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is around 7.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi84 – 841Manganese 1By similarity
    Metal bindingi86 – 861Manganese 1By similarity
    Metal bindingi113 – 1131Manganese 1By similarity
    Metal bindingi113 – 1131Manganese 2By similarity
    Metal bindingi145 – 1451Manganese 2By similarity
    Active sitei146 – 1461Proton donorBy similarity
    Metal bindingi197 – 1971Manganese 2By similarity
    Metal bindingi303 – 3031Manganese 2By similarity

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • protein serine/threonine phosphatase activity Source: TAIR

    GO - Biological processi

    • blue light signaling pathway Source: TAIR
    • dephosphorylation Source: GOC
    • response to heat Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G63870-MONOMER.
    ARA:GQT-397-MONOMER.
    ARA:GQT-398-MONOMER.
    BRENDAi3.1.3.16. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 7 (EC:3.1.3.16)
    Gene namesi
    Name:PP7
    Ordered Locus Names:At5g63870
    ORF Names:MGI19.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G63870.

    Subcellular locationi

    GO - Cellular componenti

    • nucleoplasm Source: UniProtKB-SubCell
    • nucleus Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi207 – 23125PKRTT…SSMKL → GGGGGGGGGGGGGGGGGGGG GGGGG: Normal subcellular location. 1 PublicationAdd
    BLAST
    Mutagenesisi209 – 23123Missing : Reduced activity, but enhanced inducibility by polylysine with pNPP as substrate; reduced binding with calmodulin. 1 PublicationAdd
    BLAST
    Mutagenesisi369 – 41345Missing : Loss of activity; normal binding with calmodulin; cytoplasmic instead of nuclear subcellular location. 2 PublicationsAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 413413Serine/threonine-protein phosphatase 7PRO_0000308991Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 671 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9FN02.
    PRIDEiQ9FN02.

    Expressioni

    Tissue specificityi

    Expressed in leaves, and, to a lower extent, in stems and flowers.1 Publication

    Inductioni

    By heat shock.1 Publication

    Gene expression databases

    GenevestigatoriQ9FN02.

    Interactioni

    Subunit structurei

    Monomer, homodimer, and heteropolymer. Interacts with calmodulin (CaM3 and CaM4) and HSFA1A/HSF1.3 Publications

    Protein-protein interaction databases

    BioGridi21749. 4 interactions.
    MINTiMINT-222502.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FN02.
    SMRiQ9FN02. Positions 52-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-7 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000242900.
    KOiK15423.
    OMAiHREPNIV.
    PhylomeDBiQ9FN02.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 2 hits.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9FN02-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    METVPPSPIT WPDGGALTND WVHGLMSCFE WSSWNLPPSQ LPSLLPVNVF
    60 70 80 90 100
    DSLVLTAHKI LHKERNCVHI DDLDSVSNVV VVGDIHGQLH DLLFLLKDTG
    110 120 130 140 150
    FPCQNRCYVF NGDYVDRGAW GLETFLVLLS WKVLMPDRVY LLRGNHESKY
    160 170 180 190 200
    CTSMYGFEKE VLTKYGDKGK HVYRKCLGCF EGLPLASIIS GRVYTAHGGL
    210 220 230 240 250
    FRSPVLPKRT TRGKKNRRVV LLEPEPSSMK LGTLDELMQA RRSVLDPPWE
    260 270 280 290 300
    GSNLIPGDVL WSDPSMTPGL SPNEQRGIGL LWGPDCTEDF LKKYELKLII
    310 320 330 340 350
    RSHEGPDARE KRTGLGGMDN GYTIDHNVES GKLITIFSAP DYPQFQATEE
    360 370 380 390 400
    RYKNKGAYII LQAPDFSDPQ FHSFEAVKPR PKAHPYYDFE NVIDSDDEMD
    410
    KSAMDTNNEQ PNS
    Length:413
    Mass (Da):46,619
    Last modified:March 1, 2001 - v1
    Checksum:i111A9E01A222A058
    GO
    Isoform 2 (identifier: Q9FN02-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         298-301: LIIR → VTPK
         302-413: Missing.

    Note: May be due to an intron retention. No experimental confirmation available.

    Show »
    Length:301
    Mass (Da):33,880
    Checksum:iA8D09318702B0C62
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti266 – 2661M → I in CAA03886 (PubMed:9584984).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei298 – 3014LIIR → VTPK in isoform 2. 1 PublicationVSP_029088
    Alternative sequencei302 – 413112Missing in isoform 2. 1 PublicationVSP_029089Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ000057 mRNA. Translation: CAA03886.1.
    AB007646 Genomic DNA. Translation: BAB11035.1.
    CP002688 Genomic DNA. Translation: AED97806.1.
    CP002688 Genomic DNA. Translation: AED97807.1.
    CP002688 Genomic DNA. Translation: AED97808.1.
    AY050898 mRNA. No translation available.
    PIRiT51611.
    RefSeqiNP_568979.1. NM_125782.3. [Q9FN02-2]
    NP_851258.2. NM_180927.3. [Q9FN02-1]
    NP_851259.1. NM_180928.1. [Q9FN02-1]
    UniGeneiAt.20661.

    Genome annotation databases

    EnsemblPlantsiAT5G63870.1; AT5G63870.1; AT5G63870. [Q9FN02-1]
    AT5G63870.2; AT5G63870.2; AT5G63870. [Q9FN02-1]
    GeneIDi836507.
    KEGGiath:AT5G63870.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ000057 mRNA. Translation: CAA03886.1.
    AB007646 Genomic DNA. Translation: BAB11035.1.
    CP002688 Genomic DNA. Translation: AED97806.1.
    CP002688 Genomic DNA. Translation: AED97807.1.
    CP002688 Genomic DNA. Translation: AED97808.1.
    AY050898 mRNA. No translation available.
    PIRiT51611.
    RefSeqiNP_568979.1. NM_125782.3. [Q9FN02-2]
    NP_851258.2. NM_180927.3. [Q9FN02-1]
    NP_851259.1. NM_180928.1. [Q9FN02-1]
    UniGeneiAt.20661.

    3D structure databases

    ProteinModelPortaliQ9FN02.
    SMRiQ9FN02. Positions 52-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi21749. 4 interactions.
    MINTiMINT-222502.

    Proteomic databases

    PaxDbiQ9FN02.
    PRIDEiQ9FN02.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G63870.1; AT5G63870.1; AT5G63870. [Q9FN02-1]
    AT5G63870.2; AT5G63870.2; AT5G63870. [Q9FN02-1]
    GeneIDi836507.
    KEGGiath:AT5G63870.

    Organism-specific databases

    TAIRiAT5G63870.

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000242900.
    KOiK15423.
    OMAiHREPNIV.
    PhylomeDBiQ9FN02.

    Enzyme and pathway databases

    BioCyciARA:AT5G63870-MONOMER.
    ARA:GQT-397-MONOMER.
    ARA:GQT-398-MONOMER.
    BRENDAi3.1.3.16. 399.

    Miscellaneous databases

    PROiQ9FN02.

    Gene expression databases

    GenevestigatoriQ9FN02.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 2 hits.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "PP7, a plant phosphatase representing a novel evolutionary branch of eukaryotic protein Ser/Thr phosphatases."
      Andreeva A.V., Evans D.E., Hawes C.R., Bennett N., Kutuzov M.A.
      Biochem. Mol. Biol. Int. 44:703-715(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
      Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 4:401-414(1997) [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] (ISOFORM 2).
      Strain: cv. Columbia.
    5. "Expression and characterization of PP7, a novel plant protein Ser/Thr phosphatase distantly related to RdgC/PPEF and PP5."
      Kutuzov M.A., Evans D.E., Andreeva A.V.
      FEBS Lett. 440:147-152(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION, DISULFIDE BOND, COFACTOR.
    6. "Purification of plant protein phosphatase PP7 and evidence for its redox regulation."
      Andreeva A.V., Solov'eva O.V., Kakuev D.L., Kutuzov M.A.
      Arch. Biochem. Biophys. 396:65-70(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBUNIT.
    7. "Noncompetitive inhibition of plant protein Ser/Thr phosphatase PP7 by phosphate."
      Kutuzov M.A., Andreeva A.V.
      Biochem. Biophys. Res. Commun. 283:93-96(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION BY INORGANIC PHOSPHATE.
    8. "Interaction of plant protein Ser/Thr phosphatase PP7 with calmodulin."
      Kutuzov M.A., Bennett N., Andreeva A.V.
      Biochem. Biophys. Res. Commun. 289:634-640(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF 209-ARG--LEU-231 AND 369-PRO--SER-413.
    9. "Nuclear localization of the plant protein Ser/Thr phosphatase PP7."
      Andreeva A.V., Kutuzov M.A.
      Mol. Cell Biol. Res. Commun. 4:345-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 207-PRO--LEU-231 AND 369-PRO--SER-413, SUBCELLULAR LOCATION.
    10. "PP7 is a positive regulator of blue light signaling in Arabidopsis."
      Moeller S.G., Kim Y.-S., Kunkel T., Chua N.-H.
      Plant Cell 15:1111-1119(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "Calmodulin-binding protein phosphatase PP7 is involved in thermotolerance in Arabidopsis."
      Liu H.-T., Li G.-L., Chang H., Sun D.-Y., Zhou R.-G., Li B.
      Plant Cell Environ. 30:156-164(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CALMODULIN AND HSFA1A, INDUCTION BY HEAT SHOCK.
    12. "Arabidopsis PPP family of serine/threonine phosphatases."
      Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
      Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiPPP7_ARATH
    AccessioniPrimary (citable) accession number: Q9FN02
    Secondary accession number(s): O49346, Q3E865
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: March 1, 2001
    Last modified: April 29, 2015
    This is version 94 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. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.