ID H3A9V3_LATCH Unreviewed; 404 AA.
AC H3A9V3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
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};
GN Name=PTEN {ECO:0000313|Ensembl:ENSLACP00000006424.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006424.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000006424.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01212335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01212343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006009982.1; XM_006009920.2.
DR AlphaFoldDB; H3A9V3; -.
DR STRING; 7897.ENSLACP00000006424; -.
DR Ensembl; ENSLACT00000006477.1; ENSLACP00000006424.1; ENSLACG00000005701.1.
DR GeneID; 102348548; -.
DR KEGG; lcm:102348548; -.
DR CTD; 368415; -.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000154335; -.
DR HOGENOM; CLU_020105_5_2_1; -.
DR InParanoid; H3A9V3; -.
DR OMA; TXFLDSK; -.
DR OrthoDB; 5477362at2759; -.
DR TreeFam; TF324513; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000005701; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
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..351
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 354..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
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 404 AA; 47158 MW; 32A09A5BEA62C75D CRC64;
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL CAERHYDATK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDK WLSEDDNHVA
AIHCKAGKGR TGVMICAYLL HRSKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY
LLKHQLDYKP VALLFHKLAF ETIPMFSGGT CNPLFVVYQL KVKIYTSPLG PTRREEKYMH
FEFPQPLPVC GDIKVEFFHK QNKMMKKEKM FHFWINTFFI PGPEENSDKV ENGSVVGEKE
LDGIYSTERS DNDKEYLILT LAKNDLDKAN KDKANKSFSP NFKVKLFFTK TVEEPSNSEA
SSSTSVTPDV SDNEPDHYRY SDTTDSDPEN EPFDEDQHPQ ITKV
//
