Q8T9S7 (PTEN_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	pteN
Synonyms:	ptenA
ORF Names:	DDB_G0286557

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + phosphate. Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cytoplasm › cell 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 process	Cell cycle Chemotaxis Lipid metabolism
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Lipid-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 to cAMP Inferred from mutant phenotype PubMed 21169559. Source: dictyBase cytokinesis after mitosis Inferred from mutant phenotype PubMed 21169559. Source: dictyBase establishment of cell polarity 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 peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC 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_component	cell cortex of cell tip Inferred from direct assay Ref.7. Source: dictyBase plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trailing edge Inferred from direct assay PubMed 16900100Ref.10. Source: dictyBase
Molecular_function	lipid 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 533	533	Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN		PRO_0000376825
Regions
	Domain	14 – 185	172	Phosphatase tensin-type
	Domain	271 – 406	136	C2 tensin-type
	Compositional bias	237 – 240	4	Poly-Lys
	Compositional bias	266 – 272	7	Poly-Gln
	Compositional bias	455 – 463	9	Poly-Asn
	Compositional bias	471 – 475	5	Poly-Thr
Sites
	Active site	124	1	Phosphocysteine intermediate Potential
Experimental info
	Sequence conflict	515	1	I → N in AAL99958. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8T9S7 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 9922F7887D6F9F6A	FASTA	533	59,831
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_637576.1. XM_632484.1.
3D structure databases
HSSP	HSSP built from PDB template 1D5R based on UniProtKB P60484.
ProteinModelPortal	Q8T9S7.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0191093.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191093; DDB0191093; DDB_G0286557.
GeneID	8625716.
KEGG	ddi:DDB_G0286557.
Organism-specific databases
dictyBase	DDB_G0286557. pten.
Phylogenomic databases
eggNOG	COG2453.
InParanoid	Q8T9S7.
KO	K01110.
OMA	WKNTEDS.
Family and domain databases
InterPro	IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR014019. Phosphatase_tensin-typ. IPR014020. Tensin_phosphatase_C2-dom. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF10409. PTEN_C2. 1 hit. PF00102. Y_phosphatase. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS51182. C2_TENSIN. 1 hit. PS51181. PPASE_TENSIN. 1 hit. PS00383. TYR_PHOSPHATASE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTEN_DICDI

Accession

Primary (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:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)