ID A0A3B3BRI0_ORYME Unreviewed; 1184 AA.
AC A0A3B3BRI0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN Name=MTMR4 {ECO:0000313|Ensembl:ENSOMEP00000008080.1};
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:ENSOMEP00000008080.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000008080.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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-
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 Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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; A0A3B3BRI0; -.
DR Ensembl; ENSOMET00000003033.1; ENSOMEP00000008080.1; ENSOMEG00000009297.1.
DR GeneTree; ENSGT00940000158976; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine 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; cd15733; FYVE_MTMR4; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046978; MTMR4_FYVE.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
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 InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF64; MYOTUBULARIN-RELATED PROTEIN 4; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 169..584
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 390..434
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1103..1163
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 278..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 334..337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 359..360
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 421..427
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1184 AA; 131432 MW; EC769893C8879711 CRC64;
MSVAGRVSCS MLNCFGEEGP PSLEYIKAKD LFPQKELVKE DDNLQVPFPV LQGEGVEYLG
HANEAIIAIS NYRFHIKFKE SVVNVPLRLI EGVESRDMFQ LHIICKDSKV VRCHFSTFKQ
CQEWAKRLNQ AIAHPSRLED LFALAYHAWC LGGSADDEDQ HVHLCRPGDH VRHRMEMEVK
RMGFDTQNVW RVSDINSNYK LCSSYPQKLL VPIWITDKEL ESVASFRSWK RIPVVVYRHQ
KNGAVIARCS QPEISWWGWR NTDDEYLVTS IAKACQTDSG AKGAPANRQR GEAPDSSDSD
FDSSLTGASG CDDNTVPHKL LILDARSYTA AVANRAKGGG CECEEYYPNC EVMFMGMANI
HAIRNSFQAL RAVCSQIPDP GNWLSALEST RWLQHLSVML KASTLVCSAM EREGRPVLVH
CSDGWDRTPQ IVALAKILLD PYYRTLEGFQ VLVETEWLDF GHKFGDRCGH QESSDDVSEQ
CPVFLQWLDC IHQLLKQFPC LFEFNEAFLV KLVQHTYSCL YGTFLCNNAR EREAKNIYKR
TCSVWSLLRT GNKNFQNFLY IPSHDTVLQP VCHTRALQLW TAVYLPTSSP CTAVDESVEL
YLPPCIAGDE LTSRSLDRLP KTRSMDNLLS AFENGAPLTR TSSDPNLNKH CQDDRGAAEA
SSASSANDSD DPEDGQSDHQ SPTQSVPWAE DPEDGRAEPC LTTQPLPSPP LPSVTTDSPS
STPVLHQALT HATDLPLPPP VEAESPCRTA DGAVPPTLDS EPCLPLPCKN SPPAAVAPTP
LLNGHSDGVA DSALKQPTPL PMEDSTETIT GEAEGPPTNP PPILPSTAPL VLPQEEPLKL
QTQVYPHRQT EEVRGRGADG AQPMVRPLLS ESPLSELSLL GSHWDSVHGL VQSACSHPGV
SRALQPNTYQ CRRLATKLLR AHGLTVGGGS QCLRREAPCC PSSPLQAGWP SVARSYNGLC
IPAMAALSSY SLAAHQFQLA SFSSASSSPP PPQAPAYLDD DGLPVPLDAV QQRLRQIEAG
YKQEVEVLRQ QVRQLQMRLE SKQYGTPPSE PDVDYEDDIT CLRESDNSNE EDSLSTHSED
RLSEGSWDRV ERKDAEVTRW VPDHMASHCF SCDSEFWMAK RRHHCRNCGN VFCKDCCHLK
LPIPDQQLYD PVLVCNSCHD LLLESRTREI RSQQLKKAIA TASS
//
