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 27-MAR-2024, entry version 163. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7. DR IntAct; Q9Z2C4; 2. DR MINT; Q9Z2C4; -. DR STRING; 10090.ENSMUSP00000015358; -. DR GlyGen; Q9Z2C4; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9Z2C4; -. DR PhosphoSitePlus; Q9Z2C4; -. DR EPD; Q9Z2C4; -. DR MaxQB; Q9Z2C4; -. DR PaxDb; 10090-ENSMUSP00000110248; -. DR PeptideAtlas; Q9Z2C4; -. DR ProteomicsDB; 286074; -. DR Pumba; Q9Z2C4; -. DR Antibodypedia; 442; 121 antibodies from 24 providers. DR DNASU; 53332; -. DR Ensembl; ENSMUST00000015358.8; ENSMUSP00000015358.2; ENSMUSG00000015214.15. DR GeneID; 53332; -. DR KEGG; mmu:53332; -. DR UCSC; uc009tjt.1; mouse. DR AGR; MGI:1858271; -. 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; DNICVKF; -. DR OrthoDB; 5474662at2759; -. 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 80 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 234 other cell types or tissues. DR ExpressionAtlas; Q9Z2C4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. 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-phosphate 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 CDD; cd14592; PTP-MTMR1; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR004182; GRAM. DR InterPro; IPR037857; MTMR1_PH-GRAM. DR InterPro; IPR030587; MTMR1_PTP. 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; MYOTUBULARIN-RELATED; 1. DR PANTHER; PTHR10807:SF40; MYOTUBULARIN-RELATED PROTEIN 1; 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; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR Genevisible; Q9Z2C4; MM. 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 //