ID G3QA25_GASAC Unreviewed; 1183 AA.
AC G3QA25;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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:ENSGACP00000026741.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000026741.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000026741.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000026741.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3QA25; -.
DR STRING; 69293.ENSGACP00000026741; -.
DR Ensembl; ENSGACT00000026793.1; ENSGACP00000026741.1; ENSGACG00000020239.1.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000158976; -.
DR InParanoid; G3QA25; -.
DR OMA; TRWLQHM; -.
DR TreeFam; TF315197; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000020239; Expressed in liver and 13 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 157..575
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 381..425
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1102..1162
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 628..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 350..351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 412..418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1183 AA; 132496 MW; 186D2CBC407BD362 CRC64;
MGEEGPPSLE YIKAKDLFPQ KELVKEDESL QVPFAVLQGE GVEYLGYADE AVIAISNYRL
HIKFKDSVIN VPLRLIENVE SRDMFQLHII CKDSKVVRCH FATFKQCQEW VKRLNRAAAH
PSRLENLFAL AYHAWCLGGN VDDEDQHIHL CRPGTGDHVR QRMEMEVKRM GFDTQNVWRV
SDLNCNFKLC SSYPQKLLVP IWITDKELES VASFRSWKRI PVVVYRHQKN GAVISRCSQP
EISWWGWRNT DDEYLVTSIA KACQMDTGGR DTCGALACRQ RGEAHDSSDS DFDSSLTGGS
GCDERTVPQK LLILDARSYT AAVANRAKGG GCECEEYYPN CEVMFMGMAN IHAIRNSFQA
LRTVCSQIPD PGNWLSALES TRWLQHLSVM LKAATLVGSA VERDGRPVLV HCSDGWDRTP
QIVALSKILL DPYYRTLEGF QVLVETEWLD YGHKFGDRCG HQENADDVSE QCPVFLQWLD
CIHQLLKQFP CLFEFNEAFL VKLVQHTYSC LYGTFLCNNA REREMRNIYK RTCSVWSLLR
NGNKNFQNFL YIPSHDMVLQ PVCHTRALQL WTAVYLPTSS PCTAVDDSME LYFPQSVTGD
ELRSLDRLPK TRSMDNLLSA FENGVALTRT SSDPNLNKHC QEGRTAPESS PTVEETSADL
SEESPSKTPE GVLGAESCED TMEEPCLTTQ PLPSLPLSPV LLGKDVALAH TPSPTPVLQH
PWPQITNPPP PLEAESPRRT GESTASPTHR SEPCLPLRCK GTEPAAAAPT SLLSGHPEGQ
EDGSPESAHL LALKPQTTLL PMEDSTETLT GDGDLPPTPP PTVSPDLTKS HLYDKEKPES
QPQVQPPEEK EDTRPDGVSG KEPVLTVAVA PFDSNQAAPR HLTSHSPFTD LSLLGSHWES
VQGLVQSACS SASHYGVSRA WQHNAYQSRR LACKLLRSQG VAAANGSQER GLQRPVRSRP
QPPSTAPPWR GISSCRRPYS SLFASSSPPP PQAPAYLDDD GLPVPMDAVQ QRLRQIEAGY
KQEVEVLRQQ VRQLQMRLES KQYSSPPSEP DIDYEDDITC LRESDNSNEE DSLSTHSEDR
LSEGSWDRVD RKDTEVTRWV PDHMASHCFN CDCEFWIAKR RHHCRNCGNV FCKDCCHLKL
PIPDQQLYDA VLVCNSCHDL LLVARTRDIR SQQLKKAIAT ASS
//
