ID   A0A2Y9QDJ5_TRIMA        Unreviewed;       508 AA.
AC   A0A2Y9QDJ5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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};
GN   Name=LOC101358818 {ECO:0000313|RefSeq:XP_023581275.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023581275.1};
RN   [1] {ECO:0000313|RefSeq:XP_023581275.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   RefSeq; XP_023581275.1; XM_023725507.1.
DR   AlphaFoldDB; A0A2Y9QDJ5; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd14591; PTP-MTM1; 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   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR10807:SF69; MYOTUBULARIN; 1.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   Pfam; PF06602; Myotub-related; 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.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT   DOMAIN          68..443
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          249..311
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          483..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        280
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         218..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         280..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   508 AA;  59282 MW;  C722AEC95B97B558 CRC64;
     MGGATSRGEN SYGLDITCKD MRNLRFALKQ EGHSRRDMFE ILTRYAFPLA HSLPLFAFLN
     EEKFNVDGWT VYNPVEEYRR QGLPNHDWRV TFINKCYELC DTYPALLVVP YRASDDDLRR
     VATFRSRNRI PVLSWIHPEN KTVIVRCSQP LVGMSGKRNK DDEKYLDVIR ETNRQISKLT
     IYDARPNVNA VANKATGGGY ESDDAYHNAE LFFLDIHNIH VMRESLKKVK DIVYPNVEES
     HWLSSLESTH WLEHIKLVLT GAIQVADKVS SGKSSVLVHC SDGWDRTAQL TSLAMLMLDS
     FYRSIEGFEI LVQKEWISFG HKFASRIGHG DKNHADADRS PIFLQFIDCV WQMSKQFPTA
     FEFNEQFLIT ILDHLYSCRF GTFLYNCESA RERQKVTERT VSLWSLINSN KEKFKNPFYT
     KEINRVLYPV ASMRHLELWV NYYIRWNPRI KQQQPNPVEQ RYMELLALRD EYIKRLEELQ
     INNSAKISDP PTSPASPSQM MPHVQTHF
//