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Database: UniProt
Entry: A6QLT4
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Original site: A6QLT4 
ID   MTM1_BOVIN              Reviewed;         603 AA.
AC   A6QLT4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-SEP-2014, entry version 59.
DE   RecName: Full=Myotubularin;
DE            EC=3.1.3.64;
GN   Name=MTM1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC       phosphatidylinositol 3-monophosphate (PI3P) and
CC       phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been
CC       shown to dephosphorylate phosphotyrosine- and phosphoserine-
CC       containing peptides. Negatively regulates EGFR degradation through
CC       regulation of EGFR trafficking from the late endosome to the
CC       lysosome. Plays a role in vacuolar formation and morphology.
CC       Regulates desmin intermediate filament assembly and architecture.
CC       Plays a role in mitochondrial morphology and positioning. Required
CC       for skeletal muscle maintenance but not for myogenesis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3-phosphate +
CC       H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate.
CC   -!- ENZYME REGULATION: Allosterically activated by
CC       phosphatidylinositol 5-phosphate (PI5P) (By similarity).
CC   -!- SUBUNIT: Interacts with MTMR12; the interaction modulates MTM1
CC       intracellular localization. Interacts with KMT2A/MLL1 (via SET
CC       domain). Interacts with DES in skeletal muscle but not in cardiac
CC       muscle (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity). Cell projection,
CC       filopodium (By similarity). Cell projection, ruffle (By
CC       similarity). Late endosome (By similarity). Note=Localizes as a
CC       dense cytoplasmic network. Also localizes to the plasma membrane,
CC       including plasma membrane extensions such as filopodia and
CC       ruffles. Predominantly located in the cytoplasm following
CC       interaction with MTMR12. Recruited to the late endosome following
CC       EGF stimulation (By similarity).
CC   -!- DOMAIN: The GRAM domain mediates binding to PI(3,5)P2 and, with
CC       lower affinity, to other phosphoinositides (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI48079.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; BC148078; AAI48079.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001193354.1; NM_001206425.2.
DR   ProteinModelPortal; A6QLT4; -.
DR   SMR; A6QLT4; 33-544.
DR   STRING; 9913.ENSBTAP00000018789; -.
DR   PRIDE; A6QLT4; -.
DR   Ensembl; ENSBTAT00000018789; ENSBTAP00000018789; ENSBTAG00000014138.
DR   GeneID; 533622; -.
DR   KEGG; bta:533622; -.
DR   CTD; 4534; -.
DR   eggNOG; NOG322789; -.
DR   GeneTree; ENSGT00670000097670; -.
DR   HOGENOM; HOG000210598; -.
DR   HOVERGEN; HBG000220; -.
DR   InParanoid; A6QLT4; -.
DR   KO; K01108; -.
DR   OMA; QGLPNHH; -.
DR   OrthoDB; EOG7XDBF9; -.
DR   TreeFam; TF315197; -.
DR   Reactome; REACT_214431; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; REACT_221945; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; REACT_227888; Synthesis of PIPs at the plasma membrane.
DR   NextBio; 20876095; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR   GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR   GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0044088; P:regulation of vacuole organization; ISS:UniProtKB.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00568; GRAM; 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; Complete proteome; Cytoplasm;
KW   Endosome; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN         1    603       Myotubularin.
FT                                /FTId=PRO_0000328655.
FT   DOMAIN       29     97       GRAM.
FT   DOMAIN      163    538       Myotubularin phosphatase.
FT   ACT_SITE    375    375       Phosphocysteine intermediate (By
FT                                similarity).
FT   MOD_RES     495    495       Phosphothreonine (By similarity).
FT   MOD_RES     588    588       Phosphoserine (By similarity).
SQ   SEQUENCE   603 AA;  70020 MW;  7A7E7929C26FF8F9 CRC64;
     MASAPTSKYN SHSLENESIK RTSRDGVNRD VGETLPRLPG EIRITDKEVI YICPFNGPIK
     GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDLRNLR
     FALKQEGHSR RDMFEILTRY AFPLAHSLPI FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN
     HHWRITFINK CYKLCDTYPA LLVVPYRASD EDLRRVATFR SRNRIPVLSW IHPENKTVIV
     RCSQPLVGMS GKRNKEDERY LDVIRETNRQ VNKLTIYDAR PNVNAVANKA TGGGYESDDV
     YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV
     ADRVSSGKSS VVVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS
     RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE RFLITILDHL YSCRFGTFLY
     NCESAREKQK VTERTVSLWS LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR
     WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LDELQLANSA KLSDPSASPS SPSQMMPHVQ
     THF
//
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