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Q84XU2

- PPP5_ARATH

UniProt

Q84XU2 - PPP5_ARATH

Protein

Serine/threonine-protein phosphatase 5

Gene

PAPP5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses, probably by enhancing their stability and their binding affinity for light signal transducers such as NDPK2. Can use para-nitrophenylphosphate (pNPP) as substrate.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Activated by arachidonic acid (AA).

    Kineticsi

    Experiments have been done in the presence of 100 µM arachidonic acid (AA).

    1. KM=160 mM for pNPP (at pH 7.5 and 30 degrees Celsius)1 Publication

    Vmax=22 µmol/min/mg enzyme with pNPP as substrate (at pH 7.5 and 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi282 – 2821Manganese 1By similarity
    Metal bindingi284 – 2841Manganese 1By similarity
    Metal bindingi311 – 3111Manganese 1By similarity
    Metal bindingi311 – 3111Manganese 2By similarity
    Metal bindingi343 – 3431Manganese 2By similarity
    Active sitei344 – 3441Proton donorBy similarity
    Metal bindingi392 – 3921Manganese 2By similarity
    Metal bindingi467 – 4671Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: TAIR
    3. protein binding Source: IntAct
    4. protein serine/threonine phosphatase activity Source: TAIR
    5. tetrapyrrole binding Source: TAIR

    GO - Biological processi

    1. chloroplast-nucleus signaling pathway Source: TAIR
    2. negative regulation of chlorophyll biosynthetic process Source: TAIR
    3. nucleocytoplasmic transport Source: TAIR
    4. protein dephosphorylation Source: InterPro
    5. red or far-red light signaling pathway Source: TAIR
    6. response to cadmium ion Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT2G42810-MONOMER.
    ARA:GQT-1698-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 5 (EC:3.1.3.16)
    Gene namesi
    Name:PAPP5
    Synonyms:PP5
    Ordered Locus Names:At2g42810
    ORF Names:F7D19.19
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G42810.

    Subcellular locationi

    Isoform 2 : Cytoplasm. Nucleusnucleoplasm. Nucleus speckle
    Note: Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with phytochromes into speckles.

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. cytosol Source: TAIR
    3. integral component of endoplasmic reticulum membrane Source: TAIR
    4. nuclear envelope Source: TAIR
    5. nuclear membrane Source: UniProtKB-SubCell
    6. nuclear speck Source: UniProtKB-SubCell
    7. nucleus Source: TAIR
    8. plasmodesma Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538Serine/threonine-protein phosphatase 5PRO_0000308988Add
    BLAST

    Proteomic databases

    PaxDbiQ84XU2.
    PRIDEiQ84XU2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ84XU2.

    Interactioni

    Subunit structurei

    Interacts with PHYA and PHYB, mostly when they are phosphorylated and in Pfr forms.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGO1D6RUV92EBI-4445012,EBI-7498167From a different organism.

    Protein-protein interaction databases

    BioGridi4218. 1 interaction.
    IntActiQ84XU2. 2 interactions.
    MINTiMINT-8375614.

    Structurei

    3D structure databases

    ProteinModelPortaliQ84XU2.
    SMRiQ84XU2. Positions 10-536.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei163 – 18321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei185 – 20521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati13 – 4634TPR 1Add
    BLAST
    Repeati48 – 8033TPR 2Add
    BLAST
    Repeati81 – 11434TPR 3Add
    BLAST

    Domaini

    TPR repeats are required for the binding with phytochromes.

    Sequence similaritiesi

    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172698.
    InParanoidiQ84XU2.
    KOiK04460.
    OMAiFKLLYPN.
    PhylomeDBiQ84XU2.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 2 hits.
    PF00515. TPR_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF033096. PPPtase_5. 1 hit.
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q84XU2-1) [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

    METKNENSDV SRAEEFKSQA NEAFKGHKYS SAIDLYTKAI ELNSNNAVYW    50
    ANRAFAHTKL EEYGSAIQDA SKAIEVDSRY SKGYYRRGAA YLAMGKFKDA 100
    LKDFQQVKRL SPNDPDATRK LKECEKAVMK LKFEEAISVP VSERRSVAES 150
    IDFHTIGNKP RSSSMPTKTA LAAVVAAVMV VAVRGFATTE ILMVLVSVVL 200
    GTFWWGSFSG KVEPQYSGAR IEGEEVTLDF VKTMMEDFKN QKTLHKRYAY 250
    QIVLQTRQIL LALPSLVDIS VPHGKHITVC GDVHGQFYDL LNIFELNGLP 300
    SEENPYLFNG DFVDRGSFSV EIILTLFAFK CMCPSSIYLA RGNHESKSMN 350
    KIYGFEGEVR SKLSEKFVDL FAEVFCYLPL AHVINGKVFV VHGGLFSVDG 400
    VKLSDIRAID RFCEPPEEGL MCELLWSDPQ PLPGRGPSKR GVGLSFGGDV 450
    TKRFLQDNNL DLLVRSHEVK DEGYEVEHDG KLITVFSAPN YCDQMGNKGA 500
    FIRFEAPDMK PNIVTFSAVP HPDVKPMAYA NNFLRMFN 538
    Length:538
    Mass (Da):60,283
    Last modified:June 1, 2003 - v1
    Checksum:i93ECC937F02D3541
    GO
    Isoform 2 (identifier: Q84XU2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         157-211: GNKPRSSSMPTKTALAAVVAAVMVVAVRGFATTEILMVLVSVVLGTFWWGSFSGK → E

    Note: Partial isoform 2 lacking TPR repeats exhibits enhanced activity at pH 7.5 with pNPP as substrate. This partial protein is in addition inhibited by okadaic acid.

    Show »
    Length:484
    Mass (Da):54,702
    Checksum:i04780D6007B69EF8
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei157 – 21155GNKPR…SFSGK → E in isoform 2. 2 PublicationsVSP_029087Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY182779 mRNA. Translation: AAO26216.1.
    AC006931 Genomic DNA. Translation: AAD21727.2.
    CP002685 Genomic DNA. Translation: AEC10171.1.
    CP002685 Genomic DNA. Translation: AEC10172.1.
    AF419574 mRNA. Translation: AAL31906.1.
    AY080674 mRNA. Translation: AAL86350.1.
    BT010180 mRNA. Translation: AAQ22649.1.
    AK221789 mRNA. Translation: BAD93924.1.
    PIRiE84858.
    RefSeqiNP_001031534.1. NM_001036457.2. [Q84XU2-1]
    NP_565985.1. NM_129842.3. [Q84XU2-2]
    UniGeneiAt.23737.

    Genome annotation databases

    EnsemblPlantsiAT2G42810.2; AT2G42810.2; AT2G42810. [Q84XU2-1]
    GeneIDi818881.
    KEGGiath:AT2G42810.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY182779 mRNA. Translation: AAO26216.1 .
    AC006931 Genomic DNA. Translation: AAD21727.2 .
    CP002685 Genomic DNA. Translation: AEC10171.1 .
    CP002685 Genomic DNA. Translation: AEC10172.1 .
    AF419574 mRNA. Translation: AAL31906.1 .
    AY080674 mRNA. Translation: AAL86350.1 .
    BT010180 mRNA. Translation: AAQ22649.1 .
    AK221789 mRNA. Translation: BAD93924.1 .
    PIRi E84858.
    RefSeqi NP_001031534.1. NM_001036457.2. [Q84XU2-1 ]
    NP_565985.1. NM_129842.3. [Q84XU2-2 ]
    UniGenei At.23737.

    3D structure databases

    ProteinModelPortali Q84XU2.
    SMRi Q84XU2. Positions 10-536.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4218. 1 interaction.
    IntActi Q84XU2. 2 interactions.
    MINTi MINT-8375614.

    Proteomic databases

    PaxDbi Q84XU2.
    PRIDEi Q84XU2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G42810.2 ; AT2G42810.2 ; AT2G42810 . [Q84XU2-1 ]
    GeneIDi 818881.
    KEGGi ath:AT2G42810.

    Organism-specific databases

    TAIRi AT2G42810.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172698.
    InParanoidi Q84XU2.
    KOi K04460.
    OMAi FKLLYPN.
    PhylomeDBi Q84XU2.

    Enzyme and pathway databases

    BioCyci ARA:AT2G42810-MONOMER.
    ARA:GQT-1698-MONOMER.

    Miscellaneous databases

    PROi Q84XU2.

    Gene expression databases

    Genevestigatori Q84XU2.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR11668:SF12. PTHR11668:SF12. 1 hit.
    Pfami PF00149. Metallophos. 1 hit.
    PF08321. PPP5. 2 hits.
    PF00515. TPR_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF033096. PPPtase_5. 1 hit.
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The subcellular localization of plant protein phosphatase 5 isoforms is determined by alternative splicing."
      de la Fuente van Bentem S., Vossen J.H., Vermeer J.E.M., de Vroomen M.J., Gadella T.W.J. Jr., Haring M.A., Cornelissen B.J.C.
      Plant Physiol. 133:702-712(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE PRODUCTS.
    2. 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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-538 (ISOFORMS 1 AND 2).
      Strain: cv. Columbia.
    6. "Phy tunes: phosphorylation status and phytochrome-mediated signaling."
      Rubio V., Deng X.W.
      Cell 120:290-292(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer."
      Ryu J.S., Kim J.-I., Kunkel T., Kim B.C., Cho D.S., Hong S.H., Kim S.-H., Fernandez A.P., Kim Y., Alonso J.M., Ecker J.R., Nagy F., Lim P.O., Song P.-S., Schaefer E., Nam H.G.
      Cell 120:395-406(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVATION BY ARACHIDONIC ACID, INTERACTION WITH PHYA AND PHYB.
    8. "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 nameiPPP5_ARATH
    AccessioniPrimary (citable) accession number: Q84XU2
    Secondary accession number(s): Q56X87
    , Q8RXU0, Q8W581, Q9SJH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 92 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