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Q8T9S7

- PTEN_DICDI

UniProt

Q8T9S7 - PTEN_DICDI

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MSNLLRVAVS KQKRRYQKNG YDLDLAYITD NIVAMGFPSE KVEGVFRNPM
60 70 80 90 100
KDVQRFLDQY HKDHFKVYNL CSERVYDHSK FYGRVGYYPF DDHNAPQFEM
110 120 130 140 150
IDAFCRDVDA WMKEDSKNIA VIHCKAGKGR TGLMICCWLM YCGMWKNTED
160 170 180 190 200
SLRFYAALRT YNQKGVTIPS QIRYVGYFGR SIRESIKYVP RNVTLKKIVL
210 220 230 240 250
RPLPKEINLS EVQFNISVGK NCVFNSKEHN MNVVISKKKK TVVDKNKKDP
260 270 280 290 300
KKKLTKENSE KNIDSQQQQQ SQSSLSQSQQ GQSSPNMQSL SASGTISSGS
310 320 330 340 350
NVGTVNGNTL HQLGGSQFSL SDLADGNTIG NDEYISFEIG ALSLAGDIRI
360 370 380 390 400
EFTNKQDDRM FMFWVNTSFV QQLEIIPKSG LDKAHKDKNH KAFPEDFHVE
410 420 430 440 450
LTFDQLDQQQ SHTTVVASAE EQTNNQHYPQ SSNNVATSSS HHDNITVVAS
460 470 480 490 500
DAPQNNNNNN NLNSSNSNNA TTTTTKNNIS LASSQSNPVQ QESNPSTTTQ
510 520 530
VSEENSAPKV EAEKIENSNA SANDSETSSN SSS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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 29, 2014
This is version 87 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