ID A0A3B4ZDI4_SERLL Unreviewed; 451 AA.
AC A0A3B4ZDI4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000033204.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000033204.1}
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; A0A3B4ZDI4; -.
DR STRING; 1841481.ENSSLDP00000033204; -.
DR Ensembl; ENSSLDT00000034131.1; ENSSLDP00000033204.1; ENSSLDG00000025420.1.
DR GeneTree; ENSGT00940000163053; -.
DR OrthoDB; 5477362at2759; -.
DR Proteomes; UP000261360; 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; IPR000242; PTP_cat.
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 Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF038025; PTEN; 2.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM01301; PTPlike_phytase; 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..185
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 102..173
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 190..398
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 308..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038025-50"
SQ SEQUENCE 451 AA; 52489 MW; E21A8643501E947C CRC64;
MAAIIKEMVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL CAERHYDAAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA
AIHCKAGKGR TGVMICAYLL HRGKFLEAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY
LLKNQLEYKP VALLFHKMVF ETLPMFSGGT CRDSTVKNRT EPTPQGFKKG NWHWDPQFVV
YQLKVKIHTS HPAHTRREDK HMFFEFPQPL PVCGDIKVEF FHKQNKMMKK DKMFHFWVNT
FFIPGPEESG EKMENGAVNN AESQQGGPGP GQGQPQSQPQ PQLQTQPQRA ESRDSCRDSD
RDYLILTLTK NDLDKANKDK ANRYFSPNFK VKLYFTKAVE EPSNSEASTS TSVTPDVSDN
EPDHYRYSDT TDSDPENEPF DEEQHTQITK V
//
