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Q8T9S7

- PTEN_DICDI

UniProt

Q8T9S7 - PTEN_DICDI

Protein

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Gene

pteN

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate By similarity. Negative regulator of PI3K chemotaxis pathways. Overexpression leads to a suppression of a PI3K-dependent activation of pkbA, and these cells exhibit chemotaxis defects consistent with a reduction in PI3K activity.By similarity7 Publications

    Catalytic activityi

    Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei124 – 1241Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity Source: dictyBase
    3. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. actin filament organization Source: dictyBase
    2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: dictyBase
    3. aggregation involved in sorocarp development Source: dictyBase
    4. cellular component movement Source: dictyBase
    5. chemotaxis Source: dictyBase
    6. chemotaxis to cAMP Source: dictyBase
    7. establishment of cell polarity Source: dictyBase
    8. mitotic cytokinesis Source: dictyBase
    9. negative chemotaxis Source: dictyBase
    10. negative regulation of protein serine/threonine kinase activity Source: dictyBase
    11. phosphatidylinositol dephosphorylation Source: dictyBase
    12. phosphatidylinositol-mediated signaling Source: dictyBase
    13. positive regulation of cellular component movement Source: dictyBase
    14. protein localization to trailing edge Source: dictyBase
    15. regulation of adenylate cyclase activity Source: dictyBase
    16. regulation of cell morphogenesis Source: dictyBase
    17. regulation of pseudopodium assembly Source: dictyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Chemotaxis, Lipid metabolism

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC:3.1.3.16, EC:3.1.3.48, EC:3.1.3.67)
    Alternative name(s):
    Pten 3-phosphoinositide phosphatase alpha
    Gene namesi
    Name:pteN
    Synonyms:ptenA
    ORF Names:DDB_G0286557
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 4, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0286557. pten.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cytoplasmcell cortex
    Note: Found uniformly on the plasma membrane in unstimulated cells. In response to chemoattractant stimulation, there is a rapid and transient release from the plasma membrane. Constitutively localized in the cortex of polarized cells.

    GO - Cellular componenti

    1. cell cortex of cell tip Source: dictyBase
    2. cell trailing edge Source: dictyBase
    3. cytosol Source: dictyBase
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Growth defect. Failure to aggregate. Slower migration. Leads to increased F-actin polymerization. Unable to suppress lateral pseudopod formation and turning. Having a direct on PI(3,4,5)P3/PI(3,4)P2 levels. Significant increase in chemoattractant-mediated activation of pkbA and a decrease in chemotaxis speed.5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENPRO_0000376825Add
    BLAST

    Expressioni

    Developmental stagei

    In chemotaxing cells, is on the plasma membrane along the lateral sides and posterior of the cell but is absent or the level is significantly reduced at the leading edge.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0191093.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8T9S7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 185172Phosphatase tensin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 406136C2 tensin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi237 – 2404Poly-Lys
    Compositional biasi266 – 2727Poly-Gln
    Compositional biasi455 – 4639Poly-Asn
    Compositional biasi471 – 4755Poly-Thr

    Sequence similaritiesi

    Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
    Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    InParanoidiQ8T9S7.
    KOiK01110.
    OMAiWKNTEDS.
    PhylomeDBiQ8T9S7.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR014020. Tensin_C2-dom.
    IPR029023. Tensin_lipid_phosphatase_dom.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF10409. PTEN_C2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS51182. C2_TENSIN. 1 hit.
    PS51181. PPASE_TENSIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8T9S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNLLRVAVS KQKRRYQKNG YDLDLAYITD NIVAMGFPSE KVEGVFRNPM    50
    KDVQRFLDQY HKDHFKVYNL CSERVYDHSK FYGRVGYYPF DDHNAPQFEM 100
    IDAFCRDVDA WMKEDSKNIA VIHCKAGKGR TGLMICCWLM YCGMWKNTED 150
    SLRFYAALRT YNQKGVTIPS QIRYVGYFGR SIRESIKYVP RNVTLKKIVL 200
    RPLPKEINLS EVQFNISVGK NCVFNSKEHN MNVVISKKKK TVVDKNKKDP 250
    KKKLTKENSE KNIDSQQQQQ SQSSLSQSQQ GQSSPNMQSL SASGTISSGS 300
    NVGTVNGNTL HQLGGSQFSL SDLADGNTIG NDEYISFEIG ALSLAGDIRI 350
    EFTNKQDDRM FMFWVNTSFV QQLEIIPKSG LDKAHKDKNH KAFPEDFHVE 400
    LTFDQLDQQQ SHTTVVASAE EQTNNQHYPQ SSNNVATSSS HHDNITVVAS 450
    DAPQNNNNNN NLNSSNSNNA TTTTTKNNIS LASSQSNPVQ QESNPSTTTQ 500
    VSEENSAPKV EAEKIENSNA SANDSETSSN SSS 533
    Length:533
    Mass (Da):59,831
    Last modified:June 1, 2002 - v1
    Checksum:i9922F7887D6F9F6A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti515 – 5151I → N in AAL99958. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF467431 mRNA. Translation: AAL75566.1.
    AF483827 mRNA. Translation: AAL99958.1.
    AAFI02000089 Genomic DNA. Translation: EAL64034.1.
    RefSeqiXP_637576.1. XM_632484.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191093; DDB0191093; DDB_G0286557.
    GeneIDi8625716.
    KEGGiddi:DDB_G0286557.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF467431 mRNA. Translation: AAL75566.1 .
    AF483827 mRNA. Translation: AAL99958.1 .
    AAFI02000089 Genomic DNA. Translation: EAL64034.1 .
    RefSeqi XP_637576.1. XM_632484.1.

    3D structure databases

    ProteinModelPortali Q8T9S7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0191093.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191093 ; DDB0191093 ; DDB_G0286557 .
    GeneIDi 8625716.
    KEGGi ddi:DDB_G0286557.

    Organism-specific databases

    dictyBasei DDB_G0286557. pten.

    Phylogenomic databases

    eggNOGi COG2453.
    InParanoidi Q8T9S7.
    KOi K01110.
    OMAi WKNTEDS.
    PhylomeDBi Q8T9S7.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR014020. Tensin_C2-dom.
    IPR029023. Tensin_lipid_phosphatase_dom.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    Pfami PF10409. PTEN_C2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS51182. C2_TENSIN. 1 hit.
    PS51181. PPASE_TENSIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Spatial and temporal regulation of Dictyostelium discoideum chemotaxis by PTEN."
      Meili R., Firtel R.A.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: AX3.
    2. "Dictyostelium discoideum PI3 phosphatase PTEN homolog."
      Iijima M., Devreotes P.N.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-515.
    3. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    4. "Tumor suppressor PTEN mediates sensing of chemoattractant gradients."
      Iijima M., Devreotes P.
      Cell 109:599-610(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION.
    5. "Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis."
      Funamoto S., Meili R., Lee S., Parry L., Firtel R.A.
      Cell 109:611-623(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    6. "PLA2 and PI3K/PTEN pathways act in parallel to mediate chemotaxis."
      Chen L., Iijima M., Tang M., Landree M.A., Huang Y.E., Xiong Y., Iglesias P.A., Devreotes P.N.
      Dev. Cell 12:603-614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis."
      Wessels D., Lusche D.F., Kuhl S., Heid P., Soll D.R.
      J. Cell Sci. 120:2517-2531(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Oscillatory signaling and network responses during the development of Dictyostelium discoideum."
      McMains V.C., Liao X.-H., Kimmel A.R.
      Ageing Res. Rev. 7:234-248(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    9. "3'-phosphoinositides regulate the coordination of speed and accuracy during chemotaxis."
      Gruver J.S., Wikswo J.P., Chung C.Y.
      Biophys. J. 95:4057-4067(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Ordered patterns of cell shape and orientational correlation during spontaneous cell migration."
      Maeda Y.T., Inose J., Matsuo M.Y., Iwaya S., Sano M.
      PLoS ONE 3:E3734-E3734(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.

    Entry informationi

    Entry nameiPTEN_DICDI
    AccessioniPrimary (citable) accession number: Q8T9S7
    Secondary accession number(s): Q54LI5, Q8T658
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2009
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3