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-APR-2013, entry version 49.
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 MLL (via SET domain).
CC Interacts with DES in skeletal muscle but not in cardiac muscle
CC (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 IPI; IPI00713767; -.
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; TDKEVIY; -.
DR OrthoDB; EOG4B5P4S; -.
DR NextBio; 20876095; -.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; IEA:Compara.
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 homeostasis; IEA:Compara.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR GO; GO:0046856; P:phosphatidylinositol 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; Myotub-related.
DR InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR InterPro; IPR011993; PH_like_dom.
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 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
//
