ID   A0A3B3ZXA1_9GOBI        Unreviewed;       630 AA.
AC   A0A3B3ZXA1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000009362.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000009362.1}
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; A0A3B3ZXA1; -.
DR   STRING; 409849.ENSPMGP00000009362; -.
DR   Ensembl; ENSPMGT00000009984.1; ENSPMGP00000009362.1; ENSPMGG00000007748.1.
DR   Proteomes; UP000261520; 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   CDD; cd14532; PTP-MTMR6-like; 1.
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:SF35; MYOTUBULARIN-RELATED PROTEIN 7; 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;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          129..505
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          570..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          515..542
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        570..616
FT                   /note="Polar 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   630 AA;  71795 MW;  8E0151CDA568626A CRC64;
     MEHIRLPKVE HVKLLDRVSA RKSRVGTLYL TATHTIFVES EDGVRSETWH SSSSSSSSSS
     SSSSSSSSSG VSLMVHCKNF QLLQFMVPEE QDCQDILLSL QRLSQPESYE ELYCFAYKPN
     VAEEERQREW NFMDLRSEYK RMGLPNTNWK LSFANQDYKV SDTYPSEVFA PESATLPVIV
     GSSKFRSRGR FPTLSYYNRD NHAAVCRSSQ PLSGFSARCL EDEQMLGAVL RSNPRSEVLY
     VVDTRPKLNA IANRAAGKGY ENEDNYSNIK FQFMGIENIH VMRNSQQKML EVCEQRSPSM
     SDFLEGLENS GWLKHIKAIL DAAVFIAKAV SEEGVSVLVH CSDGWDRTSQ VCSVSSVLLD
     PYYRTLKGFM VLIEKDWIYF GHKFSHRCNH LDGDPKEVSP VIDQFLECVW QLTEQFPCSF
     EFNERFLITI HHHIYSCQFG NFIGNNQKER EHLGIHTRTH SLWSYLWTNR ADFINPLYRP
     NHSQTQGVLR PSTAPYCFKF WRGLYNRFER GVHPRQSVED CLRTIREETE QLEEQLASHK
     QVKVLGYPTA WIFTPDIRLA NTPQDYTSCF LTSSPRPAGG SPVTPQDLNQ TSSFNSNGSD
     QESGIADLSV QSPFSEDSAR DSDEAANSAA
//