ID   A0A3B3C5P2_ORYME        Unreviewed;       659 AA.
AC   A0A3B3C5P2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE            EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE   AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000013135.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000013135.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC         phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC         Evidence={ECO:0000256|ARBA:ARBA00001291};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   AlphaFoldDB; A0A3B3C5P2; -.
DR   Ensembl; ENSOMET00000020678.1; ENSOMEP00000013135.1; ENSOMEG00000014588.1.
DR   GeneTree; ENSGT00940000158055; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF34; MYOTUBULARIN-RELATED PROTEIN 6; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE   3: Inferred from homology;
FT   DOMAIN          129..505
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          551..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        341
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         278..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         341..347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   659 AA;  75685 MW;  85358272F6E40389 CRC64;
     MEHIRTPKVE QVRLLDRFSN KSTNGTLYLT ATHLIFVESS SNNSTSAGQE IWILHHHIAS
     VEKLSLTTTG CPLVIQCRNF RVVHFVVQRE RDCHDVYSSL LRLLRPVCYE ELYAFSYNPK
     QNDQQREEGW QLIDLGAEFE RMGVPCDQWQ LTDVNRDYKV CETYPRDLYV PITASKPIII
     GSSKFRSKGR FPVLTYFYQE KKAAVCRCSQ PLSGFSARCL EDESMLQAIS RANHNSRFIY
     VMDTRPKLNA MANRAAGKGY ENEDNYSNIR FQFVGIENIH VMRTSLQKLL EVVGSRSLTM
     SDYLVGLENS GWLRHIKAVT DAAIFLAKAV TVEGASVLVH CSDGWDRTAQ VCSLGALLMD
     PYYRTIKGFM VLIEKDWISF GHKFADRCDQ LDGDPKEVSP IFTQFLECVW QLTEQFPQAF
     EFSEWFLLQI HEHVHSCQYG NFLGNNQRQR EELQLRERTH SLWAFLMSER QNYLNPFYSP
     AYSEAHPVLQ PSTLPYHFKF WRNMYHQFDR SMHPRQSILK TILTLKEKTC KAEGTLHALE
     NRLQQLGVAP MVTSDTPAPP PTRDQRSNPL PPRPDSLILG APVNHKEAER KQEEEEDEQG
     EVGQEALEST YSERTVEGSS GTESRKQSYG ELEGKHNEER AKEEPSVVCS VYARCSAVG
//