ID A0A6B0QTZ0_9CETA Unreviewed; 351 AA. AC A0A6B0QTZ0; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 02-OCT-2024, entry version 19. 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=H2O + O-phospho-L-seryl-[protein] = 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=H2O + O-phospho-L-threonyl-[protein] = 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=H2O + O-phospho-L-tyrosyl-[protein] = 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VBQZ03000005; MXQ80540.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6B0QTZ0; -. DR Proteomes; UP000322234; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. 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: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 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 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 //