ID A0A1B0FDL8_GLOMM Unreviewed; 610 AA.
AC A0A1B0FDL8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000256|ARBA:ARBA00032571};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.95 {ECO:0000256|ARBA:ARBA00012903};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY001688-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY001688-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY001688-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:57923; EC=3.1.3.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001669};
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 EMBL; CCAG010007366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0FDL8; -.
DR STRING; 37546.A0A1B0FDL8; -.
DR EnsemblMetazoa; GMOY001688-RA; GMOY001688-PA; GMOY001688.
DR VEuPathDB; VectorBase:GMOY001688; -.
DR PhylomeDB; A0A1B0FDL8; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProt.
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; IPR004182; GRAM.
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:SF130; PHOSPHATIDYLINOSITOL-3,5-BISPHOSPHATE 3-PHOSPHATASE; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 188..567
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 313..316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 400..406
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 610 AA; 69550 MW; 18F7BDF27F6BC085 CRC64;
MDGKDSLLVV TVLQEKAASK NASTNSLDTD SKSSSTGSKH DAELNSSRDT LFAYLDGEED
QDQKNDVTYV CPYRGPTYGA LTITNYRLYF RSLPLRDHEP PPVILDVPLG VIARVEKIGG
ATSRGENSYG IEIFCKDMRN LRFAHKQQNH SRRTVFEKLQ SYAFPLSYSG RLFAFAHAVN
STQAGENGWA VYEPLAELRR LGVPNDMWRA TKINENYAVC DSYPAVWAVP KVASDDFLRR
VALFRSRCRL PVLSWIHQKS QAAITRCSQP LVGVGGKRSA DDELFLNYIM EANAQSDKLA
IMDARPSANA IANKAKGGGY ESEEAYKSVE IHFLDIHNIH VMRESLRKVK EVCYPTIDDS
KWLSSIDNSL WLKHIKCIVA GAVRIVDKVE TMSTSVVVHC SDGWDRTAQL TALAMLLLDP
YYRTFRGFEV LIEKEWSSFG HKFQQRIGHG DNRHSDADRS PVFLQFIDSV WQVSQQFPNA
FEFNEHLLIT IIDHLYSCRF GTFLCNTEAE RVAEDMKHKT ISLWTFINSS MDQYLNPLYP
SFTQGAHQTV LRPIASMRII KLWKGLYCRW NPSMRPQNKI YNRTRELLVL QEQLVKQVSE
KRMKANIRQA
//
