ID A0A267EU38_9PLAT Unreviewed; 453 AA.
AC A0A267EU38;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOX15_Mlig013990g1 {ECO:0000313|EMBL:PAA65018.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA65018.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA65018.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA65018.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA65018.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA65018.1}.
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DR EMBL; NIVC01001693; PAA65018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267EU38; -.
DR STRING; 282301.A0A267EU38; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IEA:UniProt.
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; 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:SF81; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN; 1.
DR Pfam; PF10409; PTEN_C2; 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:UP000215902}.
FT DOMAIN 14..194
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 79..168
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 199..373
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 314..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 51031 MW; 8449E87CC5D24FC6 CRC64;
MSINLRQLVS RKKKRFEDGE FNLDLSYITP QIIAMGFPAE TLERIYRNDI SEVSRFLETY
HADRYRVYNL CAERSYNHAK FKDRVEQFAM QDHNPPLIHT IPYFCTSVYK WLQTGTDYVA
AIHCKAGKGR TGVMIACYLL YESFKGIHDS PPTYLSADAV LDLYDRQRTH NGKGVTIPSQ
RRYVYYYAHT LRKSLSVESC PLVLKSVTLE GGQPVFPPSN SCSLYFRCKK LVRDCHQDNR
STHRPIGDSE VCEVRGGQQT AILVQPTSPI PVNGDVKIVF YHRSSNRLAR YDKIFHFWLN
TFFVVNQPGD TPGARWRQER GLDDGGPASA ASGDGGLRGR DIFLTLTKAE LDKACKDRLL
PDTFSATLRF SVPEYHSDDD DASGPYRSFA YTPQQAAAAP PAGLSDDAGS NQQHHQSSSS
SCSSQTDDDE DPEKAFGQQQ QQQQEQGSDQ GGQ
//
