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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) (Pten 3-phosphoinositide phosphatase alpha)

 PTEN_DICDI              Reviewed;         533 AA.
Q8T9S7; Q54LI5; Q8T658;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=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;
AltName: Full=Pten 3-phosphoinositide phosphatase alpha;
Name=pteN; Synonyms=ptenA; ORFNames=DDB_G0286557;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AX3;
Meili R., Firtel R.A.;
"Spatial and temporal regulation of Dictyostelium discoideum
chemotaxis by PTEN.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-515.
Iijima M., Devreotes P.N.;
"Dictyostelium discoideum PI3 phosphatase PTEN homolog.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
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.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[4]
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=12062103; DOI=10.1016/S0092-8674(02)00745-6;
Iijima M., Devreotes P.;
"Tumor suppressor PTEN mediates sensing of chemoattractant
gradients.";
Cell 109:599-610(2002).
[5]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=12062104; DOI=10.1016/S0092-8674(02)00755-9;
Funamoto S., Meili R., Lee S., Parry L., Firtel R.A.;
"Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase
and PTEN mediates chemotaxis.";
Cell 109:611-623(2002).
[6]
FUNCTION.
PubMed=17419997; DOI=10.1016/j.devcel.2007.03.005;
Chen L., Iijima M., Tang M., Landree M.A., Huang Y.E., Xiong Y.,
Iglesias P.A., Devreotes P.N.;
"PLA2 and PI3K/PTEN pathways act in parallel to mediate chemotaxis.";
Dev. Cell 12:603-614(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17623773; DOI=10.1242/jcs.010876;
Wessels D., Lusche D.F., Kuhl S., Heid P., Soll D.R.;
"PTEN plays a role in the suppression of lateral pseudopod formation
during Dictyostelium motility and chemotaxis.";
J. Cell Sci. 120:2517-2531(2007).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18657484; DOI=10.1016/j.arr.2008.04.003;
McMains V.C., Liao X.-H., Kimmel A.R.;
"Oscillatory signaling and network responses during the development of
Dictyostelium discoideum.";
Ageing Res. Rev. 7:234-248(2008).
[9]
FUNCTION.
PubMed=18676656; DOI=10.1529/biophysj.108.130179;
Gruver J.S., Wikswo J.P., Chung C.Y.;
"3'-phosphoinositides regulate the coordination of speed and accuracy
during chemotaxis.";
Biophys. J. 95:4057-4067(2008).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19011688; DOI=10.1371/journal.pone.0003734;
Maeda Y.T., Inose J., Matsuo M.Y., Iwaya S., Sano M.;
"Ordered patterns of cell shape and orientational correlation during
spontaneous cell migration.";
PLoS ONE 3:E3734-E3734(2008).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:12062103,
ECO:0000269|PubMed:12062104, ECO:0000269|PubMed:17419997,
ECO:0000269|PubMed:17623773, ECO:0000269|PubMed:18657484,
ECO:0000269|PubMed:18676656, ECO:0000269|PubMed:19011688}.
-!- CATALYTIC ACTIVITY: Phosphatidylinositol 3,4,5-trisphosphate +
H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- 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.
-!- 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.
{ECO:0000269|PubMed:12062104}.
-!- 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. {ECO:0000269|PubMed:12062103,
ECO:0000269|PubMed:12062104, ECO:0000269|PubMed:17623773,
ECO:0000269|PubMed:18657484, ECO:0000269|PubMed:19011688}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF467431; AAL75566.1; -; mRNA.
EMBL; AF483827; AAL99958.1; -; mRNA.
EMBL; AAFI02000089; EAL64034.1; -; Genomic_DNA.
RefSeq; XP_637576.1; XM_632484.1.
ProteinModelPortal; Q8T9S7; -.
BioGrid; 1250719; 3.
STRING; 44689.DDB0191093; -.
PaxDb; Q8T9S7; -.
EnsemblProtists; EAL64034; EAL64034; DDB_G0286557.
GeneID; 8625716; -.
KEGG; ddi:DDB_G0286557; -.
dictyBase; DDB_G0286557; pten.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
InParanoid; Q8T9S7; -.
KO; K01110; -.
OMA; MWKNTED; -.
PhylomeDB; Q8T9S7; -.
Reactome; R-DDI-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-DDI-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-DDI-202424; Downstream TCR signaling.
Reactome; R-DDI-5689880; Ub-specific processing proteases.
Reactome; R-DDI-5689896; Ovarian tumor domain proteases.
Reactome; R-DDI-8948747; Regulation of PTEN localization.
Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
PRO; PR:Q8T9S7; -.
Proteomes; UP000002195; Chromosome 4.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0051285; C:cell cortex of cell tip; IDA:dictyBase.
GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
GO; GO:0031257; C:cell trailing edge membrane; IDA:dictyBase.
GO; GO:0005829; C:cytosol; IDA:dictyBase.
GO; GO:1990753; C:equatorial cell cortex; IDA:dictyBase.
GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
GO; GO:0001931; C:uropod; IDA:dictyBase.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:dictyBase.
GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; IDA:dictyBase.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0030041; P:actin filament polymerization; IMP:dictyBase.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:dictyBase.
GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0048870; P:cell motility; IMP:dictyBase.
GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
GO; GO:0030010; P:establishment of cell polarity; IMP:dictyBase.
GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
GO; GO:0050919; P:negative chemotaxis; IMP:dictyBase.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:dictyBase.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:dictyBase.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; TAS:dictyBase.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:dictyBase.
GO; GO:0051272; P:positive regulation of cellular component movement; TAS:dictyBase.
GO; GO:0036051; P:protein localization to trailing edge; IDA:dictyBase.
GO; GO:0036052; P:protein localization to uropod; IMP:dictyBase.
GO; GO:0031269; P:pseudopodium assembly; IMP:dictyBase.
GO; GO:0045761; P:regulation of adenylate cyclase activity; IGI:dictyBase.
GO; GO:0022604; P:regulation of cell morphogenesis; IMP:dictyBase.
GO; GO:0031272; P:regulation of pseudopodium assembly; IMP:dictyBase.
GO; GO:0034461; P:uropod retraction; IMP:dictyBase.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR014020; Tensin_C2-dom.
InterPro; IPR029023; Tensin_phosphatase.
InterPro; IPR016130; Tyr_Pase_AS.
Pfam; PF00782; DSPc; 1.
Pfam; PF10409; PTEN_C2; 1.
SMART; SM01326; PTEN_C2; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
2: Evidence at transcript level;
Cell cycle; Cell membrane; Chemotaxis; Complete proteome; Cytoplasm;
Hydrolase; Lipid metabolism; Lipid-binding; Membrane;
Protein phosphatase; Reference proteome.
CHAIN 1 533 Phosphatidylinositol 3,4,5-trisphosphate
3-phosphatase and dual-specificity
protein phosphatase PTEN.
/FTId=PRO_0000376825.
DOMAIN 14 185 Phosphatase tensin-type.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
DOMAIN 271 406 C2 tensin-type. {ECO:0000255|PROSITE-
ProRule:PRU00589}.
COMPBIAS 237 240 Poly-Lys.
COMPBIAS 266 272 Poly-Gln.
COMPBIAS 455 463 Poly-Asn.
COMPBIAS 471 475 Poly-Thr.
ACT_SITE 124 124 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00590,
ECO:0000255|PROSITE-ProRule:PRU10044}.
CONFLICT 515 515 I -> N (in Ref. 2; AAL99958).
{ECO:0000305}.
SEQUENCE 533 AA; 59831 MW; 9922F7887D6F9F6A CRC64;
MSNLLRVAVS KQKRRYQKNG YDLDLAYITD NIVAMGFPSE KVEGVFRNPM KDVQRFLDQY
HKDHFKVYNL CSERVYDHSK FYGRVGYYPF DDHNAPQFEM IDAFCRDVDA WMKEDSKNIA
VIHCKAGKGR TGLMICCWLM YCGMWKNTED SLRFYAALRT YNQKGVTIPS QIRYVGYFGR
SIRESIKYVP RNVTLKKIVL RPLPKEINLS EVQFNISVGK NCVFNSKEHN MNVVISKKKK
TVVDKNKKDP KKKLTKENSE KNIDSQQQQQ SQSSLSQSQQ GQSSPNMQSL SASGTISSGS
NVGTVNGNTL HQLGGSQFSL SDLADGNTIG NDEYISFEIG ALSLAGDIRI EFTNKQDDRM
FMFWVNTSFV QQLEIIPKSG LDKAHKDKNH KAFPEDFHVE LTFDQLDQQQ SHTTVVASAE
EQTNNQHYPQ SSNNVATSSS HHDNITVVAS DAPQNNNNNN NLNSSNSNNA TTTTTKNNIS
LASSQSNPVQ QESNPSTTTQ VSEENSAPKV EAEKIENSNA SANDSETSSN SSS


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