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-JUN-2021, entry version 6. DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN {ECO:0000256|PIRNR:PIRNR038025}; DE EC=3.1.3.16 {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: Tumor suppressor. Acts as a dual-specificity protein CC phosphatase, dephosphorylating tyrosine-, serine- and threonine- CC phosphorylated proteins. Also acts as a lipid phosphatase. CC {ECO:0000256|PIRNR:PIRNR038025}. 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|PIRNR:PIRNR038025}; 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|PIRNR:PIRNR038025}; 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|PIRNR:PIRNR038025}; 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:ARBA00000536, CC ECO:0000256|PIRNR:PIRNR038025}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038025}. CC Nucleus {ECO:0000256|PIRNR:PIRNR038025}. Nucleus, PML body CC {ECO:0000256|PIRNR:PIRNR038025}. 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 Proteomes; UP000322234; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; IEA:UniProtKB-UniRule. 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-phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0106306; F:protein serine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0106307; F:protein threonine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:UniProtKB-UniRule. 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; 3.90.190.10; -; 1. DR InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN. 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 Pfam; PF10409; PTEN_C2; 1. DR PIRSF; PIRSF038025; PTEN; 1. DR SMART; SM01326; PTEN_C2; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR PROSITE; PS51182; C2_TENSIN; 1. DR PROSITE; PS51181; PPASE_TENSIN; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038025}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR038025}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR038025}; KW Neurogenesis {ECO:0000256|PIRNR:PIRNR038025}; KW Nucleus {ECO:0000256|PIRNR:PIRNR038025}; KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR038025}. FT DOMAIN 1..133 FT /note="Phosphatase tensin-type" FT /evidence="ECO:0000259|PROSITE:PS51181" 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 //