MTMR1_MOUSE
ID MTMR1_MOUSE Reviewed; 669 AA.
AC Q9Z2C4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Myotubularin-related protein 1;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q13613};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000269|PubMed:12217958};
GN Name=Mtmr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA Mandel J.-L.;
RT "Characterization of the myotubularin dual specificity phosphatase gene
RT family from yeast to human.";
RL Hum. Mol. Genet. 7:1703-1712(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wiehe T., Zhao W., Herman G.E., Rosenthal A., Platzer M.;
RT "Comparative sequence analysis of the mouse Mtm locus and the corresponding
RT region of human Xq28.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12217958; DOI=10.1093/hmg/11.19.2297;
RA Buj-Bello A., Furling D., Tronchere H., Laporte J., Lerouge T.,
RA Butler-Browne G.S., Mandel J.L.;
RT "Muscle-specific alternative splicing of myotubularin-related 1 gene is
RT impaired in DM1 muscle cells.";
RL Hum. Mol. Genet. 11:2297-2307(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-53, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Lipid phosphatase that has high specificity for
CC phosphatidylinositol 3-phosphate and has no activity with
CC phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-
CC bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate
CC (PubMed:12217958). Activity with phosphatidylinositol (3,5)-
CC bisphosphate is controversial; it has been shown for the human ortholog
CC (By similarity). In contrast, PubMed:12217958 find no activity with
CC this substrate. {ECO:0000250|UniProtKB:Q13613,
CC ECO:0000269|PubMed:12217958}.
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:Q13613};
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:0000269|PubMed:12217958};
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:Q13613};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q13613}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12217958};
CC Peripheral membrane protein {ECO:0000269|PubMed:12217958}; Cytoplasmic
CC side {ECO:0000269|PubMed:12217958}. Cytoplasm
CC {ECO:0000269|PubMed:12217958}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in skeletal muscle,
CC heart, lung, liver and brain. {ECO:0000269|PubMed:12217958}.
CC -!- DOMAIN: The C-terminal region is required for dimerization.
CC {ECO:0000250|UniProtKB:Q13613}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AF073997; AAC77822.1; -; mRNA.
DR EMBL; AF125314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056376; AAH56376.1; -; mRNA.
DR EMBL; BC057337; AAH57337.1; -; mRNA.
DR CCDS; CCDS30178.1; -.
DR RefSeq; NP_001300631.1; NM_001313702.1.
DR RefSeq; NP_001300632.1; NM_001313703.1.
DR RefSeq; NP_001300633.1; NM_001313704.1.
DR RefSeq; NP_001300635.1; NM_001313706.1.
DR RefSeq; NP_001300636.1; NM_001313707.1.
DR RefSeq; NP_058681.1; NM_016985.2.
DR AlphaFoldDB; Q9Z2C4; -.
DR SMR; Q9Z2C4; -.
DR BioGRID; 207292; 6.
DR IntAct; Q9Z2C4; 2.
DR MINT; Q9Z2C4; -.
DR STRING; 10090.ENSMUSP00000110248; -.
DR iPTMnet; Q9Z2C4; -.
DR PhosphoSitePlus; Q9Z2C4; -.
DR EPD; Q9Z2C4; -.
DR MaxQB; Q9Z2C4; -.
DR PaxDb; Q9Z2C4; -.
DR PeptideAtlas; Q9Z2C4; -.
DR PRIDE; Q9Z2C4; -.
DR ProteomicsDB; 286074; -.
DR Antibodypedia; 442; 102 antibodies from 24 providers.
DR DNASU; 53332; -.
DR Ensembl; ENSMUST00000015358; ENSMUSP00000015358; ENSMUSG00000015214.
DR GeneID; 53332; -.
DR KEGG; mmu:53332; -.
DR UCSC; uc009tjt.1; mouse.
DR CTD; 8776; -.
DR MGI; MGI:1858271; Mtmr1.
DR VEuPathDB; HostDB:ENSMUSG00000015214; -.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000153669; -.
DR HOGENOM; CLU_001839_4_1_1; -.
DR InParanoid; Q9Z2C4; -.
DR OMA; RITRCKT; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q9Z2C4; -.
DR BRENDA; 3.1.3.64; 3474.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 53332; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Mtmr1; mouse.
DR PRO; PR:Q9Z2C4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2C4; protein.
DR Bgee; ENSMUSG00000015214; Expressed in hindlimb stylopod muscle and 231 other tissues.
DR ExpressionAtlas; Q9Z2C4; baseline and differential.
DR Genevisible; Q9Z2C4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; ISO:MGI.
DR CDD; cd13358; PH-GRAM_MTMR1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030587; MTMR1.
DR InterPro; IPR037857; MTMR1_PH-GRAM.
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:SF40; PTHR10807:SF40; 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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Hydrolase; Lipid metabolism;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..669
FT /note="Myotubularin-related protein 1"
FT /id="PRO_0000094933"
FT DOMAIN 94..165
FT /note="GRAM"
FT DOMAIN 230..605
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..669
FT /note="Required for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q13613"
FT REGION 644..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 355..358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13613"
FT BINDING 380..381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13613"
FT BINDING 442..448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13613"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13613"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 669 AA; 75313 MW; 1856792245F2D800 CRC64;
MDRPVAAAAA ASAASCEGAG GPGPGPGASW RPSRVAGGAS ASSRHPSIET LDSPTGSHVE
WCKQLIAATI SSQISGSVTS ENVSRDYKAL RDGNKLAQME EAPLFPGESI KAIVKDVIYI
CPFMGAVSGT LTVTDFKMYF KNVERDPHFV LDVPLGVISR VEKIGAQSHG DNSCGIEIVC
KDMRNLRLAY KQEEQRKLGI FENLNKHAFP LSNGQVLFAF NYKEKFPVNG WKVYDPVSEY
KRQGLPNESW KISKINSNYE FCDTYPAIIV VPTSVKDDDL SKVAAFRAKG RVPVLSWIHP
ESQATITRCS QPLVGPNDKR CKEDEKYLQT IMDANAQSHK LTIFDARQNS VADTNKAKGG
GYENESAYPN AELIFLEIHN IHVMRESLRK LKEIVYPSID ESHWLSNVDG THWLEYIRVL
LAGAVRIADK IESGKTSVVI HCSDGWDRTS QLTSLAMLML DSYYRTIKGF EALIEKEWIS
FGHRFALRVG HGDDNHADAD RSPIFLQFID CVWQMTRQFP SAFEFNELFL ITILDHLYSC
LFGTFLCNCE QQRIKEDVYT NTISLWSYIN SQLDEFSNPF FVNYENHVLY PVASMSHLEL
WVNYYVRWNP RMRPQMPIHQ NLKELLAIKA ELQKRVEDLQ REMATRTISS SSERGSSPTH
SATPVHTSV
