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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) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)

 PTEN_CANLF              Reviewed;         403 AA.
P60483; O00633; O02679;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
16-FEB-2004, sequence version 1.
25-OCT-2017, entry version 112.
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=Mutated in multiple advanced cancers 1;
AltName: Full=Phosphatase and tensin homolog;
Name=PTEN; Synonyms=MMAC1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9090379; DOI=10.1038/ng0497-356;
Steck P.A., Pershouse M.A., Jasser S.A., Lin H., Yung W.K.A.,
Ligon A.H., Langford L.A., Baumgard M.L., Hattier T., Davis T.,
Frye C., Hu R., Swedlund B., Teng D.H.-F., Tavtigian S.V.;
"Identification of a candidate tumour suppressor gene, MMAC1, at
chromosome 10q23.3 that is mutated in multiple advanced cancers.";
Nat. Genet. 15:356-363(1997).
-!- FUNCTION: Tumor suppressor. 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 with order of
substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 >
PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is
critical for its tumor suppressor function. Antagonizes the PI3K-
AKT/PKB signaling pathway by dephosphorylating phosphoinositides
and thereby modulating cell cycle progression and cell survival.
The unphosphorylated form cooperates with AIP1 to suppress AKT1
activation. Dephosphorylates tyrosine-phosphorylated focal
adhesion kinase and inhibits cell migration and integrin-mediated
cell spreading and focal adhesion formation. Plays a role as a key
modulator of the AKT-mTOR signaling pathway controlling the tempo
of the process of newborn neurons integration during adult
neurogenesis, including correct neuron positioning, dendritic
development and synapse formation. May be a negative regulator of
insulin signaling and glucose metabolism in adipose tissue. The
nuclear monoubiquitinated form possesses greater apoptotic
potential, whereas the cytoplasmic nonubiquitinated form induces
less tumor suppressive ability. In motile cells, suppresses the
formation of lateral pseudopods and thereby promotes cell
polarization and directed movement (By similarity). {ECO:0000250}.
-!- 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.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer. The unphosphorylated form interacts with the
second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro.
Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with
MAST4 nor with DLG5; interaction with MAGI2 increases protein
stability. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2;
in the presence of NEDD4 or ITCH, this interaction promotes PTEN
ubiquitination. Interacts (via C2 domain) with FRK. Interacts with
USP7; the interaction is direct (By similarity). Interacts with
ROCK1 (By similarity). Interacts with XIAP/BIRC4. Interacts with
STK11; the interaction phosphorylates PTEN. Interacts with
PPP1R16B (By similarity). Interacts with NOP53; regulates PTEN
phosphorylation and increases its stability.
{ECO:0000250|UniProtKB:O08586, ECO:0000250|UniProtKB:P60484}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P60484}.
Nucleus {ECO:0000250|UniProtKB:P60484}. Nucleus, PML body
{ECO:0000250|UniProtKB:P60484}. Note=Monoubiquitinated form is
nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with
PML and USP7 in PML nuclear bodies. XIAP/BIRC4 promotes its
nuclear localization. {ECO:0000250|UniProtKB:P60484}.
-!- PTM: Constitutively phosphorylated by CK2 under normal conditions.
Phosphorylation results in an inhibited activity towards PIP3.
Phosphorylation can both inhibit or promote PDZ-binding.
Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from
ubiquitin-mediated degradation probably by inhibiting its binding
to NEDD4. Phosphorylation by ROCK1 is essential for its stability
and activity. Phosphorylation by PLK3 promotes its stability and
prevents its degradation by the proteasome (By similarity).
{ECO:0000250}.
-!- PTM: Monoubiquitinated; monoubiquitination is increased in
presence of retinoic acid. Deubiquitinated by USP7; leading to its
nuclear exclusion. Monoubiquitination of one of either Lys-13 and
Lys-289 amino acid is sufficient to modulate PTEN
compartmentalization (By similarity). Ubiquitinated by XIAP/BIRC4
(By similarity). {ECO:0000250}.
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EMBL; U92435; AAC48709.1; -; mRNA.
RefSeq; NP_001003192.1; NM_001003192.1.
UniGene; Cfa.3695; -.
ProteinModelPortal; P60483; -.
SMR; P60483; -.
MINT; MINT-128368; -.
STRING; 9615.ENSCAFP00000023027; -.
PaxDb; P60483; -.
GeneID; 403832; -.
KEGG; cfa:403832; -.
CTD; 5728; -.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
HOGENOM; HOG000008008; -.
HOVERGEN; HBG000239; -.
InParanoid; P60483; -.
KO; K01110; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; ISS:UniProtKB.
GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0046855; P:inositol phosphate dephosphorylation; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
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.
InterPro; IPR003595; Tyr_Pase_cat.
Pfam; PF00782; DSPc; 1.
Pfam; PF10409; PTEN_C2; 1.
PIRSF; PIRSF038025; PTEN; 1.
SMART; SM01326; PTEN_C2; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
2: Evidence at transcript level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Isopeptide bond; Lipid metabolism; Neurogenesis; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome;
Tumor suppressor; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P60484}.
CHAIN 2 403 Phosphatidylinositol 3,4,5-trisphosphate
3-phosphatase and dual-specificity
protein phosphatase PTEN.
/FTId=PRO_0000215903.
DOMAIN 14 185 Phosphatase tensin-type.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
DOMAIN 190 350 C2 tensin-type. {ECO:0000255|PROSITE-
ProRule:PRU00589}.
REGION 338 348 Required for interaction with NOP53.
{ECO:0000250|UniProtKB:P60484}.
REGION 401 403 PDZ domain-binding. {ECO:0000250}.
ACT_SITE 124 124 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:O08586}.
MOD_RES 336 336 Phosphotyrosine; by FRK.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 366 366 Phosphothreonine; by GSK3-beta and PLK3.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 370 370 Phosphoserine; by CK2 and PLK3.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 380 380 Phosphoserine; by ROCK1.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 382 382 Phosphothreonine; by ROCK1.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 383 383 Phosphothreonine; by ROCK1.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 385 385 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000250|UniProtKB:P60484}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P60484}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P60484}.
SEQUENCE 403 AA; 47166 MW; 75F97C3DD6802BA9 CRC64;
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA
AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY
LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY
FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS
SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV


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