ID A0A3B3XUJ7_9TELE Unreviewed; 423 AA.
AC A0A3B3XUJ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|ARBA:ARBA00013064, ECO:0000256|PIRNR:PIRNR038025};
DE EC=3.1.3.67 {ECO:0000256|ARBA:ARBA00013015, ECO:0000256|PIRNR:PIRNR038025};
DE AltName: Full=Phosphatase and tensin homolog {ECO:0000256|PIRNR:PIRNR038025};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000018598.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000018598.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3B3XUJ7; -.
DR Ensembl; ENSPMET00000027768.1; ENSPMEP00000018598.1; ENSPMEG00000022320.1.
DR Proteomes; UP000261480; Unplaced.
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 CDD; cd14509; PTP_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; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR045101; PTP_PTEN.
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 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|ARBA:ARBA00023098,
KW 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 14..180
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 97..168
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 185..370
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 372..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038025-50"
SQ SEQUENCE 423 AA; 48863 MW; 20BAA35C984BC9C2 CRC64;
MAAIIKEMVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL NFLLVLANCI AQYPFEDHNP PQLELIKPFC EDLDQWLSED DNHVAAIHCK
AGKGRTGVMI CAYLLHRGKF TEAQDALDFY GEVRTRDRKG VTIPSQRRYV YYYNYLLKNQ
LEYKPVALLF HKMVFETLPM FSGGTCNPQF VVYQLKVKIH TSNPAHTRRE DKHMIFEFPQ
PLPVCGDIKV EFFHKQNKMM KKDKMFHFWV NTFFIPGPDE SGEKMENGAV NNVESQQGAP
GLGLGLVQGQ VQSQVQGQPQ GAETRDGCRE GDRDYLILTL TKNDLDKANK DKANRYFSPN
FKVKLYFTKT VEEPSNSEAS TSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEEQHTQI
TKV
//
