ID   A0A6B0QTZ0_9CETA        Unreviewed;       351 AA.
AC   A0A6B0QTZ0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 10.
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|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}.
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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: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-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004725; F:protein tyrosine 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   GO; GO:0006470; P:protein dephosphorylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
DR   InterPro; IPR035892; C2_domain_sf.
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   Pfam; PF10409; PTEN_C2; 1.
DR   PIRSF; PIRSF038025; PTEN; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF49562; SSF49562; 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.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 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          50..121
FT                   /note="TYR_PHOSPHATASE_2"
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
//