MTM1_XENLA
ID MTM1_XENLA Reviewed; 602 AA.
AC Q52KU6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-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; BC094184; AAH94184.1; -; mRNA.
DR RefSeq; NP_001089410.1; NM_001095941.1.
DR RefSeq; XP_018087605.1; XM_018232116.1.
DR RefSeq; XP_018087606.1; XM_018232117.1.
DR RefSeq; XP_018087607.1; XM_018232118.1.
DR RefSeq; XP_018087608.1; XM_018232119.1.
DR AlphaFoldDB; Q52KU6; -.
DR SMR; Q52KU6; -.
DR BioGRID; 592241; 1.
DR IntAct; Q52KU6; 1.
DR DNASU; 734460; -.
DR GeneID; 734460; -.
DR KEGG; xla:734460; -.
DR CTD; 734460; -.
DR OMA; DDAYHNT; -.
DR OrthoDB; 824298at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 734460; Expressed in gastrula and 19 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_0000328658"
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..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..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 ACT_SITE 374
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
SQ SEQUENCE 602 AA; 69730 MW; 045A0EFF24F1F8AB CRC64;
MATSSTPKYN SNSLENSVRR SPGDGINHEQ NDEISRLPGE TLITDKEVIY MCPFYGPVKG
RIYVTNYKLY FKGEEMEPLI TFAVPLGVIA RIEKMGGASS RGENSYGLDI TCKDMRNLRF
ALKQEVHSRK QIFEDLTKYA FPLSHGLLFF AFQNEEKFPE NGWAVYDAMT EFRRQGLPND
QWRITFINRN YELCDTYPPL LVVPYSASEE DLKRVAAFRS RNRIPVLSWL HPENQSAIMR
CSQPLVGMSG KRNKDDERYL DIIRETNGQT SKLTIYDARP NVNAVANKAT GGGYENEDAY
PNAELVFLDI HNIHVMRESL KKLKDIVYPN VEESHWLSSL ESTHWLEHIK LVLTGAIQVA
DKVASGKSSV VVHCSDGWDR TAQLTSLAML MLDSYYRTIV GFEVLVQKEW ISFGHKFSSR
IGHGDKNHAD ADRSPIFLQF IDCVWQMSKQ FPTAFEFNEH FLITILDHLY SCRFGTFLYN
CETIRDKEKV REKTPSLWSL ISSEKSKYTN PFYTKELNRV LYPVASMRHL ELWVNYYIRW
NPRIRQQQPN PVEQRYMELL ALRDDYVRRL EELQISNSPK INRSTTSPSS PSQMMPQVQT
PF
