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Q8T9S7 (PTEN_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:pteN
Synonyms:ptenA
ORF Names:DDB_G0286557
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Catalytic activity

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.

Subcellular location

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. Ref.4 Ref.5

Developmental stage

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. Ref.5

Disruption phenotype

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. Ref.4 Ref.5 Ref.7 Ref.8 Ref.10

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
   Biological processCell cycle
Chemotaxis
Lipid metabolism
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandLipid-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Traceable author statement PubMed 15473840. Source: dictyBase

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 17606871. Source: dictyBase

aggregation involved in sorocarp development

Traceable author statement PubMed 15473840. Source: dictyBase

cellular component movement

Inferred from mutant phenotype Ref.7. Source: dictyBase

chemotaxis

Inferred from mutant phenotype Ref.7. Source: dictyBase

chemotaxis to cAMP

Inferred from mutant phenotype PubMed 21169559. Source: dictyBase

establishment of cell polarity

Inferred from mutant phenotype PubMed 21169559. Source: dictyBase

mitotic cytokinesis

Inferred from mutant phenotype PubMed 21169559. Source: dictyBase

negative chemotaxis

Inferred from mutant phenotype PubMed 17517960. Source: dictyBase

negative regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 21169559. Source: dictyBase

phosphatidylinositol dephosphorylation

Traceable author statement PubMed 15473840. Source: dictyBase

phosphatidylinositol-mediated signaling

Traceable author statement PubMed 15366706. Source: dictyBase

positive regulation of cellular component movement

Traceable author statement PubMed 15473840. Source: dictyBase

protein localization to trailing edge

Inferred from direct assay PubMed 21169559. Source: dictyBase

regulation of adenylate cyclase activity

Inferred from genetic interaction PubMed 16267269. Source: dictyBase

regulation of cell morphogenesis

Inferred from mutant phenotype Ref.10. Source: dictyBase

regulation of pseudopodium assembly

Inferred from mutant phenotype Ref.10. Source: dictyBase

   Cellular_componentcell cortex of cell tip

Inferred from direct assay Ref.7. Source: dictyBase

cell trailing edge

Inferred from direct assay PubMed 16900100Ref.10. Source: dictyBase

cytosol

Inferred from direct assay PubMed 23132928. Source: dictyBase

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity

Traceable author statement PubMed 15473840. Source: dictyBase

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
PRO_0000376825

Regions

Domain14 – 185172Phosphatase tensin-type
Domain271 – 406136C2 tensin-type
Compositional bias237 – 2404Poly-Lys
Compositional bias266 – 2727Poly-Gln
Compositional bias455 – 4639Poly-Asn
Compositional bias471 – 4755Poly-Thr

Sites

Active site1241Phosphocysteine intermediate Potential

Experimental info

Sequence conflict5151I → N in AAL99958. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8T9S7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 9922F7887D6F9F6A

FASTA53359,831
        10         20         30         40         50         60 
MSNLLRVAVS KQKRRYQKNG YDLDLAYITD NIVAMGFPSE KVEGVFRNPM KDVQRFLDQY 

        70         80         90        100        110        120 
HKDHFKVYNL CSERVYDHSK FYGRVGYYPF DDHNAPQFEM IDAFCRDVDA WMKEDSKNIA 

       130        140        150        160        170        180 
VIHCKAGKGR TGLMICCWLM YCGMWKNTED SLRFYAALRT YNQKGVTIPS QIRYVGYFGR 

       190        200        210        220        230        240 
SIRESIKYVP RNVTLKKIVL RPLPKEINLS EVQFNISVGK NCVFNSKEHN MNVVISKKKK 

       250        260        270        280        290        300 
TVVDKNKKDP KKKLTKENSE KNIDSQQQQQ SQSSLSQSQQ GQSSPNMQSL SASGTISSGS 

       310        320        330        340        350        360 
NVGTVNGNTL HQLGGSQFSL SDLADGNTIG NDEYISFEIG ALSLAGDIRI EFTNKQDDRM 

       370        380        390        400        410        420 
FMFWVNTSFV QQLEIIPKSG LDKAHKDKNH KAFPEDFHVE LTFDQLDQQQ SHTTVVASAE 

       430        440        450        460        470        480 
EQTNNQHYPQ SSNNVATSSS HHDNITVVAS DAPQNNNNNN NLNSSNSNNA TTTTTKNNIS 

       490        500        510        520        530 
LASSQSNPVQ QESNPSTTTQ VSEENSAPKV EAEKIENSNA SANDSETSSN SSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF467431 mRNA. Translation: AAL75566.1.
AF483827 mRNA. Translation: AAL99958.1.
AAFI02000089 Genomic DNA. Translation: EAL64034.1.

3D structure databases

ProteinModelPortalQ8T9S7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191093; DDB0191093; DDB_G0286557.
KEGGddi:DDB_G0286557.

Organism-specific databases

dictyBaseDDB_G0286557. pten.

Phylogenomic databases

eggNOGCOG2453.
InParanoidQ8T9S7.
KOK01110.
OMAWKNTEDS.
PhylomeDBQ8T9S7.

Family and domain databases

InterProIPR000008. C2_dom.
IPR014020. Tensin_C2-dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF10409. PTEN_C2. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTEN_DICDI
AccessionPrimary (citable) accession number: Q8T9S7
Secondary accession number(s): Q54LI5, Q8T658
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase