ID   A0A6B0QTZ0_9CETA        Unreviewed;       351 AA.
AC   A0A6B0QTZ0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-NOV-2024, entry version 20.
DE   RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN {ECO:0000256|ARBA:ARBA00034338, ECO:0000256|PIRNR:PIRNR038025};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081, ECO:0000256|PIRNR:PIRNR038025};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR038025};
DE            EC=3.1.3.67 {ECO:0000256|PIRNR:PIRNR038025};
DE   AltName: Full=Phosphatase and tensin homolog {ECO:0000256|PIRNR:PIRNR038025};
GN   ORFNames=E5288_WYG009068 {ECO:0000313|EMBL:MXQ80540.1};
OS   Bos mutus (wild yak).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=72004 {ECO:0000313|EMBL:MXQ80540.1, ECO:0000313|Proteomes:UP000322234};
RN   [1] {ECO:0000313|EMBL:MXQ80540.1, ECO:0000313|Proteomes:UP000322234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WY2019 {ECO:0000313|EMBL:MXQ80540.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:MXQ80540.1};
RA   Liu Y.;
RT   "The sequence and de novo assembly of the wild yak genome.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual-specificity protein phosphatase, dephosphorylating
CC       tyrosine-, serine- and threonine-phosphorylated proteins. Also
CC       functions as a lipid phosphatase, removing the phosphate in the D3
CC       position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol
CC       3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate
CC       and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for
CC       PtdIns(3,4,5)P3. {ECO:0000256|PIRNR:PIRNR038025}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-
CC         3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate;
CC         Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83420, ChEBI:CHEBI:83423;
CC         Evidence={ECO:0000256|ARBA:ARBA00034256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43561;
CC         Evidence={ECO:0000256|ARBA:ARBA00034256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC         trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC         ChEBI:CHEBI:83419; Evidence={ECO:0000256|ARBA:ARBA00034268};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43553;
CC         Evidence={ECO:0000256|ARBA:ARBA00034268};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627,
CC         ChEBI:CHEBI:57733; Evidence={ECO:0000256|ARBA:ARBA00043762};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144;
CC         Evidence={ECO:0000256|ARBA:ARBA00043762};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77155,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC         ChEBI:CHEBI:203600; Evidence={ECO:0000256|ARBA:ARBA00043734};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77156;
CC         Evidence={ECO:0000256|ARBA:ARBA00043734};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00036558};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC         Evidence={ECO:0000256|ARBA:ARBA00036558};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00036676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC         Evidence={ECO:0000256|ARBA:ARBA00036676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00033632};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000256|ARBA:ARBA00033632};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC         trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC         ChEBI:CHEBI:58456; EC=3.1.3.67;
CC         Evidence={ECO:0000256|ARBA:ARBA00043760};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25018;
CC         Evidence={ECO:0000256|ARBA:ARBA00043760};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm
CC       {ECO:0000256|PIRNR:PIRNR038025}. Nucleus
CC       {ECO:0000256|PIRNR:PIRNR038025}. Nucleus, PML body
CC       {ECO:0000256|PIRNR:PIRNR038025}. Postsynaptic density
CC       {ECO:0000256|ARBA:ARBA00034105}.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000256|ARBA:ARBA00007881, ECO:0000256|PIRNR:PIRNR038025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MXQ80540.1}.
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DR   EMBL; VBQZ03000005; MXQ80540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6B0QTZ0; -.
DR   Proteomes; UP000322234; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0048870; P:cell motility; IEA:TreeGrafter.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:UniProtKB-UniRule.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:TreeGrafter.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:TreeGrafter.
DR   FunFam; 2.60.40.1110:FF:000003; Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR051281; Dual-spec_lipid-protein_phosph.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF81; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF22785; Tc-R-P; 1.
DR   PIRSF; PIRSF038025; PTEN; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038025};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038025};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR038025};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW   ECO:0000256|PIRNR:PIRNR038025}; Nucleus {ECO:0000256|PIRNR:PIRNR038025};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR038025};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          1..133
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          50..121
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          138..298
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   REGION          302..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        72
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038025-50"
SQ   SEQUENCE   351 AA;  40893 MW;  0584C813AC80C862 CRC64;
     MHKLTVVPGI AWHIKCWLCA ERHYDTAKFN CRVAQYPFED HNPPQLELIK PFCEDLDQWL
     SEDDNHVAAI HCKAGKGRTG VMICAYLLHR GKFLKAQEAL DFYGEVRTRD KKGVTIPSQR
     RYVYYYSYLL KNHLDYRPVA LLFHKMMFET IPMFSGGTCN PQFVVCQLKV KIYSSNSGPT
     RREDKFMYFE FPQPLPVCGD IKVEFFHKQN KMLKKDKMFH FWVNTFFIPG PEETSEKVEN
     GSLCDQEIDS ICSIERADND KEYLVLTLTK NDLDKANKDK ANRYFSPNFK VKLYFTKTVE
     ESSNPEASSS TSVTPDVSDN EPDHYRYSDT TDSDPENEPF DEDQHTQITK V
//