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P48485

- PP15_ARATH

UniProt

P48485 - PP15_ARATH

Protein

Serine/threonine-protein phosphatase PP1 isozyme 5

Gene

TOPP5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Manganese 1By similarity
    Metal bindingi72 – 721Manganese 1By similarity
    Metal bindingi98 – 981Manganese 1By similarity
    Metal bindingi98 – 981Manganese 2By similarity
    Metal bindingi130 – 1301Manganese 2By similarity
    Active sitei131 – 1311Proton donorBy similarity
    Metal bindingi179 – 1791Manganese 2By similarity
    Metal bindingi254 – 2541Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein serine/threonine phosphatase activity Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G46820-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1 isozyme 5 (EC:3.1.3.16)
    Gene namesi
    Name:TOPP5
    Ordered Locus Names:At3g46820
    ORF Names:T6H20.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G46820.

    Subcellular locationi

    GO - Cellular componenti

    1. protein phosphatase type 1 complex Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 312311Serine/threonine-protein phosphatase PP1 isozyme 5PRO_0000058801Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP48485.
    PRIDEiP48485.

    Expressioni

    Gene expression databases

    GenevestigatoriP48485.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-8060796.

    Structurei

    3D structure databases

    ProteinModelPortaliP48485.
    SMRiP48485. Positions 14-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    InParanoidiP48485.
    KOiK06269.
    OMAiQIKNIER.
    PhylomeDBiP48485.

    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. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P48485-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQQGQGSMD PAVLDDIIRR LLDYRNPKAG TKQAMLNDSE IRQLCFVSRE    50
    IFLQQPCLLE LAAPVKICGD IHGQYSDLLR LFEYGGFPPA ANYLFLGDYV 100
    DRGKQSLETI CLLLAYKIKY PENFFLLRGN HECASINRIY GFYDECKRRF 150
    NVKLWKVFTD TFNCLPVAAV IDEKILCMHG GLSPELINVE QIKNIERPTD 200
    VPDAGLLCDL LWSDPSKDVK GWGMNDRGVS YTFGADKVAE FLIKNDMDLV 250
    CRAHQVVEDG YEFFADRQLV TMFSAPNYCG EFDNAGALMS VDESLMCSFQ 300
    ILKPVDRRSR FF 312
    Length:312
    Mass (Da):35,519
    Last modified:February 1, 1996 - v1
    Checksum:i937084D580708A68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti245 – 2462ND → IP in CAA78152. (PubMed:8220477)Curated
    Sequence conflicti288 – 2881L → M in CAA78152. (PubMed:8220477)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93412 mRNA. Translation: AAA32840.1.
    AL096859 Genomic DNA. Translation: CAB51183.1.
    CP002686 Genomic DNA. Translation: AEE78208.1.
    BT024715 mRNA. Translation: ABD59053.1.
    AK220755 mRNA. Translation: BAD93940.1.
    AK227072 mRNA. Translation: BAE99129.1.
    Z12162 mRNA. Translation: CAA78152.1.
    PIRiS25532.
    S31089.
    RefSeqiNP_190266.1. NM_114549.3.
    UniGeneiAt.311.

    Genome annotation databases

    EnsemblPlantsiAT3G46820.1; AT3G46820.1; AT3G46820.
    GeneIDi823835.
    KEGGiath:AT3G46820.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93412 mRNA. Translation: AAA32840.1 .
    AL096859 Genomic DNA. Translation: CAB51183.1 .
    CP002686 Genomic DNA. Translation: AEE78208.1 .
    BT024715 mRNA. Translation: ABD59053.1 .
    AK220755 mRNA. Translation: BAD93940.1 .
    AK227072 mRNA. Translation: BAE99129.1 .
    Z12162 mRNA. Translation: CAA78152.1 .
    PIRi S25532.
    S31089.
    RefSeqi NP_190266.1. NM_114549.3.
    UniGenei At.311.

    3D structure databases

    ProteinModelPortali P48485.
    SMRi P48485. Positions 14-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-8060796.

    Proteomic databases

    PaxDbi P48485.
    PRIDEi P48485.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G46820.1 ; AT3G46820.1 ; AT3G46820 .
    GeneIDi 823835.
    KEGGi ath:AT3G46820.

    Organism-specific databases

    TAIRi AT3G46820.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    InParanoidi P48485.
    KOi K06269.
    OMAi QIKNIER.
    PhylomeDBi P48485.

    Enzyme and pathway databases

    BioCyci ARA:AT3G46820-MONOMER.

    Gene expression databases

    Genevestigatori P48485.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana."
      Smith R.D., Walker J.C.
      Plant Mol. Biol. 21:307-316(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [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. "Arabidopsis ORF clones."
      Shinn P., Chen H., Kim C.J., Ecker J.R.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      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 (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "A protein phosphatase 1 from Arabidopsis thaliana restores temperature sensitivity of a Schizosaccharomyces pombe cdc25ts/wee1-double mutant."
      Ferreira P.C.G., Hemerly A.S., van Montagu M., Inze D.
      Plant J. 4:81-87(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-312.
    7. "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.
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP15_ARATH
    AccessioniPrimary (citable) accession number: P48485
    Secondary accession number(s): Q29Q41, Q570F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 106 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