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Protein

Dual specificity phosphatase Cdc25

Gene

CDC25

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

Functioni

Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.
Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Enzyme regulationi

Inhibited by NSC95397.1 Publication

Kineticsi

  1. KM=50 mM for para-nitrophenyl phosphate2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Zinc2 Publications
    Active sitei86 – 861Phosphocysteine intermediateCurated
    Metal bindingi134 – 1341Zinc2 Publications
    Metal bindingi136 – 1361Zinc2 Publications
    Metal bindingi141 – 1411Zinc2 Publications

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • oxidoreductase activity Source: UniProtKB-KW
    • protein tyrosine phosphatase activity Source: TAIR

    GO - Biological processi

    • cell division Source: UniProtKB-KW
    • mitotic nuclear division Source: UniProtKB-KW
    • peptidyl-tyrosine dephosphorylation Source: GOC
    • protein phosphorylation Source: TAIR
    • response to arsenic-containing substance Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT5G03455-MONOMER.
    SABIO-RKQ8GY31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity phosphatase Cdc25 (EC:3.1.3.48)
    Alternative name(s):
    Arath;CDC25
    Arsenate reductase 2 (EC:1.20.4.-)
    Sulfurtransferase 5
    Short name:
    AtStr5
    Gene namesi
    Name:CDC25
    Synonyms:ACR2, STR5
    Ordered Locus Names:At5g03455
    ORF Names:F12E4_220
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G03455.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth conditions, but plants show reduced root size when grown in presence of hydroxyurea.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861C → S: Loss of phosphatase activity. 1 Publication
    Mutagenesisi145 – 1451C → S: No major structural changes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 146146Dual specificity phosphatase Cdc25PRO_0000198663Add
    BLAST

    Proteomic databases

    PaxDbiQ8GY31.
    PRIDEiQ8GY31.

    Expressioni

    Tissue specificityi

    Expressed in roots and at lower levels in shoots (at protein level). Expressed in leaves, stems and flowers.2 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi17108. 3 interactions.
    IntActiQ8GY31. 3 interactions.
    STRINGi3702.AT5G03455.1.

    Structurei

    Secondary structure

    1
    146
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 246Combined sources
    Turni26 – 316Combined sources
    Beta strandi38 – 447Combined sources
    Helixi47 – 504Combined sources
    Beta strandi56 – 605Combined sources
    Beta strandi63 – 664Combined sources
    Helixi69 – 746Combined sources
    Beta strandi81 – 877Combined sources
    Beta strandi90 – 923Combined sources
    Helixi93 – 10614Combined sources
    Beta strandi107 – 1093Combined sources
    Beta strandi113 – 1219Combined sources
    Helixi124 – 1296Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T3KNMR-A15-146[»]
    ProteinModelPortaliQ8GY31.
    SMRiQ8GY31. Positions 15-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GY31.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 135102RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate-binding
    Regioni68 – 714Substrate-binding
    Regioni90 – 923Substrate-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 144Poly-Lys

    Sequence similaritiesi

    Belongs to the MPI phosphatase family.Curated
    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG294009.
    HOGENOMiHOG000162894.
    InParanoidiQ8GY31.
    KOiK18065.
    OMAiNIMILER.
    PhylomeDBiQ8GY31.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8GY31-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY
    60 70 80 90 100
    DGHIAGSLHY ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL
    110 120 130 140
    VNYLDEKKED TGIKNIMILE RGFNGWEASG KPVCRCAEVP CKGDCA
    Length:146
    Mass (Da):16,450
    Last modified:March 1, 2003 - v1
    Checksum:iEA2DD0E79784D538
    GO

    Sequence cautioni

    The sequence AAM63780.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAB83305.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL162751 Genomic DNA. Translation: CAB83305.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED90607.1.
    AK117898 mRNA. Translation: BAC42537.1.
    BT003658 mRNA. Translation: AAO39886.1.
    AY086729 mRNA. Translation: AAM63780.1. Different initiation.
    PIRiT48370.
    RefSeqiNP_568119.1. NM_120425.2.
    UniGeneiAt.43043.

    Genome annotation databases

    EnsemblPlantsiAT5G03455.1; AT5G03455.1; AT5G03455.
    GeneIDi831832.
    KEGGiath:AT5G03455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL162751 Genomic DNA. Translation: CAB83305.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED90607.1.
    AK117898 mRNA. Translation: BAC42537.1.
    BT003658 mRNA. Translation: AAO39886.1.
    AY086729 mRNA. Translation: AAM63780.1. Different initiation.
    PIRiT48370.
    RefSeqiNP_568119.1. NM_120425.2.
    UniGeneiAt.43043.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T3KNMR-A15-146[»]
    ProteinModelPortaliQ8GY31.
    SMRiQ8GY31. Positions 15-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi17108. 3 interactions.
    IntActiQ8GY31. 3 interactions.
    STRINGi3702.AT5G03455.1.

    Proteomic databases

    PaxDbiQ8GY31.
    PRIDEiQ8GY31.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G03455.1; AT5G03455.1; AT5G03455.
    GeneIDi831832.
    KEGGiath:AT5G03455.

    Organism-specific databases

    TAIRiAT5G03455.

    Phylogenomic databases

    eggNOGiNOG294009.
    HOGENOMiHOG000162894.
    InParanoidiQ8GY31.
    KOiK18065.
    OMAiNIMILER.
    PhylomeDBiQ8GY31.

    Enzyme and pathway databases

    BioCyciARA:AT5G03455-MONOMER.
    SABIO-RKQ8GY31.

    Miscellaneous databases

    EvolutionaryTraceiQ8GY31.
    PROiQ8GY31.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      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. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The Arabidopsis CDC25 induces a short cell length when overexpressed in fission yeast: evidence for cell cycle function."
      Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.
      New Phytol. 165:425-428(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2)."
      Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.
      Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Differential expression of Arabidopsis sulfurtransferases under various growth conditions."
      Bartels A., Mock H.P., Papenbrock J.
      Plant Physiol. Biochem. 45:178-187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    9. "Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to hydroxyurea but not to zeocin or salt stress."
      Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E., Rogers H.J., Francis D.
      Ann. Bot. 107:1183-1192(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase."
      Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D., de Veylder L., Lippens G.
      Biochem. Biophys. Res. Commun. 322:734-739(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-145.
    11. Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-86.

    Entry informationi

    Entry nameiCDC25_ARATH
    AccessioniPrimary (citable) accession number: Q8GY31
    Secondary accession number(s): Q8LC90, Q9LZE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 1, 2003
    Last modified: July 22, 2015
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds 1 zinc ion which is not required for enzyme activity (PubMed:15329414). Plants silencing ACR2 show increased sensitivity to arsenate but not arsenite (PubMed:16567632).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.