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Database: UniProt
Entry: F0Z675_DICPU
LinkDB: F0Z675_DICPU
Original site: F0Z675_DICPU 
ID   F0Z675_DICPU            Unreviewed;       860 AA.
AC   F0Z675;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DICPUDRAFT_25009 {ECO:0000313|EMBL:EGC40549.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC40549.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
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DR   EMBL; GL870941; EGC40549.1; -; Genomic_DNA.
DR   RefSeq; XP_003282885.1; XM_003282837.1.
DR   AlphaFoldDB; F0Z675; -.
DR   STRING; 5786.F0Z675; -.
DR   EnsemblProtists; EGC40549; EGC40549; DICPUDRAFT_25009.
DR   GeneID; 10503345; -.
DR   KEGG; dpp:DICPUDRAFT_25009; -.
DR   eggNOG; KOG0248; Eukaryota.
DR   eggNOG; KOG2283; Eukaryota.
DR   InParanoid; F0Z675; -.
DR   OMA; NFHTGMF; -.
DR   OrthoDB; 9895at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   CDD; cd14497; PTP_PTEN-like; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF100; PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE 3-PHOSPHATASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00233; PH; 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   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT   DOMAIN          18..189
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          103..177
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          194..330
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          403..502
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          493..624
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          758..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  97533 MW;  C404035AAF4114D1 CRC64;
     MYNSIVKAVR KTISADKNRF ENEEYDLDLT YITERVIAMS FPADGVESAY RNSIYDVSKM
     LNENHKNNYL IYNLSERKYD YSLFNKSVVD WCGFPDHHAP PLGLLFKIVK TIYDWLGKDP
     LNVVIVHCMA GKGRTGTVIS CLLQYGGLFD SASDAMRYFA VKRSNNNYGI TGPSQIRYTQ
     YFSELYLGGK DLNPSPVFLK SISMVTIPKF FLGPLKQGIC PVLNIYSATQ KGVRIFTSAP
     IEGDTKETRT YQSGNATIIF EVRKIVRGDI LLVFSHITPF YRVEQICRAN FHTGMFSMPT
     LILTKSDLDG ADGDKRFSND FNLKLEFQEV VNNNSNGSQS PLIEASTSQS ILEYQKEIKK
     EIKWIRHEAI KKDPKNGSVF FLPKNNSEKI KQAKDIASKQ GTFGVHSGFL LKKGHNFKSW
     RRRWFVLKDN LLSYYKSPKD TTPAGVIPVN EILDISIKCE ISQQEGHDYC FEIITHKASY
     LISAENEKDL EDWTEILNSA IKMIQSTGRL FIEILEAKYE PNVILQSLTD PSAIIDINDH
     PIDIITYLTI HLGKKRDTTS HKSMLFNPIF QYAGDFAIYN EPCDLVVSLW VRSSVQNIKD
     TLAAEFVLNH KQLMSSYNTE WREFNRIKSN LLTNMSLKFG SVYRCESDLS LHENALGSLQ
     SPNQFSNSPG SFNSNENRKS IIHQSVSFNH SLYQQTPNNN NNNIDNSKII SNNGGLSNSL
     NFNSISNNNN NNNLSTNVST SAPSTNYIFL AKSREENHRA NSMNSNNNSN NNKSLNNSNE
     TNSNKNNNSS SLDKTTAMNS YGFSFDGDDE DKLIKALENQ LNDTQDDDEL ISDLQSKLDY
     FEDIAPNEDD SLSEFKIINK
//
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