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Database: UniProt
Entry: W2R251_PHYPN
LinkDB: W2R251_PHYPN
Original site: W2R251_PHYPN 
ID   W2R251_PHYPN            Unreviewed;       513 AA.
AC   W2R251;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PPTG_04810 {ECO:0000313|EMBL:ETN19522.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN19522.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN19522.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN19522.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI669565; ETN19522.1; -; Genomic_DNA.
DR   RefSeq; XP_008895357.1; XM_008897109.1.
DR   AlphaFoldDB; W2R251; -.
DR   STRING; 761204.W2R251; -.
DR   EnsemblProtists; ETN19522; ETN19522; PPTG_04810.
DR   GeneID; 20174881; -.
DR   VEuPathDB; FungiDB:PPTG_04810; -.
DR   OMA; LGHFWFH; -.
DR   OrthoDB; 5477362at2759; -.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
DR   GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 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; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF60; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE TPTE2-RELATED; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   SMART; SM01326; PTEN_C2; 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   4: Predicted;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817}.
FT   DOMAIN          123..295
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          212..283
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          358..503
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  58125 MW;  BD36749335E57D70 CRC64;
     MQRMLSITRV KHIGQSDRSL HKGKDNKSGP LDQTPTSPVS TVDSISPPSP LEAWGTFESP
     PAPPPSPVIR AASHSPSSIR PTLKIDAEQT SPMPSPSSSP TSSRRYTGGL TYRLKHLVSK
     EKRRFSSDGF DLDLTYVTQR LVALGYPAEM IEGIYRNHYR DVFRFFEQRH PGRYRVYNLC
     VERRYAPDEK FHGRVAEYGF EDHCPPPLSL LLPFCRDVHV WLTTNPENIV AVHCKAGKGR
     TGVMLCAYML YARIWRSAHG ALEYFAAARS KKLQGVTIRS QRRFVGYFSE LCRRSESADD
     LEELGSYEDE EARERAMTLA DYHTQWLQET QALLEATSPR ETIGSKLRPH AEPVLPARVN
     LVLVAVVLCG VTGHKKTNAS AAEWRVRVEC GALRPRTAVY DLIGSFQRQL RPCIDGDNGK
     EVLELEMRCN PVLVWDEVRV ELRRRSGSAL GHFWFHTAFI PQVDGHFELM LEKSEIDKIA
     KDAKHGHKKF APEFAVRLRF ELAKEQVVAK SDT
//
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