MTM1_XENTR
ID MTM1_XENTR Reviewed; 602 AA.
AC Q5EB32;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myotubularin;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13496};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q13496};
GN Name=mtm1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol
CC 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate
CC (PI(3,5)P2). {ECO:0000250|UniProtKB:Q13496}.
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:0000250|UniProtKB:Q13496};
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:0000250|UniProtKB:Q13496};
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:0000250|UniProtKB:Q13496};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13496};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994,
CC ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:Q13496};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13496}. Cell
CC membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q13496}.
CC Late endosome {ECO:0000250|UniProtKB:Q13496}. Cytoplasm, myofibril,
CC sarcomere {ECO:0000250|UniProtKB:Q9Z2C5}.
CC -!- DOMAIN: The GRAM domain mediates binding to PI(3,5)P2 and, with lower
CC affinity, to other phosphoinositides. {ECO:0000250|UniProtKB:Q13496}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; BC090112; AAH90112.1; -; mRNA.
DR RefSeq; NP_001015828.1; NM_001015828.1.
DR RefSeq; XP_017951735.1; XM_018096246.1.
DR AlphaFoldDB; Q5EB32; -.
DR SMR; Q5EB32; -.
DR STRING; 8364.ENSXETP00000016895; -.
DR PaxDb; Q5EB32; -.
DR DNASU; 548545; -.
DR Ensembl; ENSXETT00000016895; ENSXETP00000016895; ENSXETG00000017786.
DR GeneID; 548545; -.
DR KEGG; xtr:548545; -.
DR CTD; 4534; -.
DR eggNOG; KOG4471; Eukaryota.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; Q5EB32; -.
DR OMA; NSPKMNS; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q5EB32; -.
DR TreeFam; TF315197; -.
DR Reactome; R-XTR-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-XTR-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-XTR-1660517; Synthesis of PIPs at the late endosome membrane.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017786; Expressed in skeletal muscle tissue and 15 other tissues.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:InterPro.
DR GO; GO:0045109; P:intermediate filament organization; IEA:InterPro.
DR GO; GO:0048311; P:mitochondrion distribution; IEA:InterPro.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:InterPro.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0044088; P:regulation of vacuole organization; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030561; Myotubularin.
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; PTHR10807; 1.
DR PANTHER; PTHR10807:SF69; PTHR10807:SF69; 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; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Endosome; Hydrolase;
KW Lipid metabolism; Membrane; Protein phosphatase; Reference proteome.
FT CHAIN 1..602
FT /note="Myotubularin"
FT /id="PRO_0000328659"
FT DOMAIN 28..96
FT /note="GRAM"
FT DOMAIN 162..537
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
SQ SEQUENCE 602 AA; 69459 MW; F595F2001127315F CRC64;
MASNSTPKYN SNSLENSLRR SPGDGMNHEQ NDEIPCLPGE ALITDKDVIY MCPFYGPVKG
RIHVTNYKLY FKGEEMEPLI SFSVPLGVIA RIEKMGGASS RGENSYGLDI TCKDMRNLRF
ALKQEVHSRK QIFEDLTKYA FPLSHGLLLF AFQNEEKFPE NGWAVYDAMT EFRRQGLPNG
QWRITFINKN YELCDTYPPL LVVPYSASEE DLKKVAAFRS RNRIPVLSWL HPENQSAIMR
CSQPLVGMSG KRNKDDERYL DIIRDTNGQT SKLTIYDARP NVNAVANKAT GGGYESEDAY
PNAELVFLDI HNIHVMRESL KKLKDIVYPN VEESHWLSSL ESTHWLEHIK LVLTGAIQVA
DKVASGKSSV VVHCSDGWDR TAQLTSLAML MLDSYYRTIV GFEVLVQKEW ISFGHKFSSR
IGHGDKNHAD ADRSPIFLQF IDCVWQMSKQ FPTAFEFNEH FLITVLDHLY SCRFGTFLYN
CENIRDKEKV REKTQSLWSL ISSEKSKYTN PFYTKELNRV LYPVASMRHL ELWVNYYIRW
NPRIRQQQPN PVEQRYMELL ALRDDYVRRL EELQITNSPK MNSSTTSPSS PSQIMPQVHT
PF
