ID A0A3Q3VVL3_MOLML Unreviewed; 1191 AA.
AC A0A3Q3VVL3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000006946.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000006946.1}
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; A0A3Q3VVL3; -.
DR STRING; 94237.ENSMMOP00000006946; -.
DR Ensembl; ENSMMOT00000007076.1; ENSMMOP00000006946.1; ENSMMOG00000005400.1.
DR OMA; TRWLQHM; -.
DR Proteomes; UP000261620; 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; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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:UP000261620};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 148..559
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 365..409
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1110..1170
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 612..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 309..312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 334..335
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 396..402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1191 AA; 133453 MW; CAAD25B46AD558E9 CRC64;
ILEYIKAKDL FPQKELVKED ESLQVPFPVL QGEGVEYLGH ADEAIIAISN YRLHIKFKDS
VINVPLRLIE SAECRDMFQL QIICKDSKIV RCHFATFKQC QEWAKRLNRA IAHPSRLEDL
FALAYHAWCL GGSADDEDQH VNLCRPGDHV RQRMEMEVKR MGFDTQNAWR LSDINCNYKL
CSSYPQKLLV PIWITDKELE SVASFRSWKR IPVVVYRYQK NGAVIARCSQ PEISWWGWRN
KDDEYLVTSI AKACQMGTKG ACRQRGEAPD SCDSDFDSFL TGGSGCDDST VPQKLLILDA
RSYTAAVANR AKGGGCECEE YYPNCEVMFM GMANIHAIRN SFQALRTVCS QIPDPGNWLS
ALESTRWLQH LSVMLKAATL VCSAVEREGR PVLVHCSDGW DRTPQIVALA KILLDPYYRT
LEGFQVLVEI DWLDYGHKFG DRCGHQENTD DVSEQCPVFL QWLDCVHQLL KQFPCLFEFN
EAFLVKMVQH TYSCLYGTFL CNNACEREAR NIYNRTCSVW SLLRSGNKNF QNFLYIPSHD
MVLQPVCHTR ALQLWTAVYL PTSSPCTAVD DSVELYFPPS VTGDELTSRS LDRLPKTRSM
DNLLSAFENG LPLTRTSSDP NLNKHCQEGR LASEPSPATE EATAEISDVM PDAVLDSSEG
EPQHQSSANT QQDSLGAQSC EVTQEDSCLT TQPLPSLPFP PVPLREEDVS AHTPDLQQAF
PQVIKTALPP PPLSESPCMT AKNTNAPSHN AVPCLPLPCN GMHPAAHIPA TSLNGHSYKQ
ADGLPESADL LALQLSPLLP MEDSTETLTG EGEPSPVLPP TATKDLTYNP NDEEQPEVQP
QVQPQKERLR TEIVKEREHV IPVAPVDCTQ GAVRHLYSQS QLSDLSLLGF HWESVQGLVQ
SASSAASHSG VSRALQPNTC QSRRLATKLL RFQGLAVANG LQCCRKEALC CPSRSQQPGL
LCAARSGTTA SINSYSQQGH QLLLGSYSSP STSSSPPPLQ APAYLDDDGL PVPMDAVQQR
LRQIEAGYKQ EVEVLRQQVR QLQMRLESKQ YSTPPSEPDI DYEDDITCLR ESDNSNEEDS
LSTHSEDRMS EGSWDRVERR DTEVTRWVPD HMASHCFNCD CEFWIAKRRH HCRNCGNVFC
KDCCHLKLPI PDQQLYDPVL VCNTCYDLLL ESRTREIRSQ QLKKAIATAS S
//
