MTMR7_MOUSE
ID MTMR7_MOUSE Reviewed; 660 AA.
AC Q9Z2C9; Q8C4J6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Myotubularin-related protein 7;
DE AltName: Full=Inositol 1,3-bisphosphate phosphatase {ECO:0000305};
DE EC=3.1.3.- {ECO:0000269|PubMed:12890864};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305};
DE EC=3.1.3.64 {ECO:0000269|PubMed:12890864};
GN Name=Mtmr7;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 291-602.
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INTERACTION WITH MTMR9, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12890864; DOI=10.1073/pnas.1333958100;
RA Mochizuki Y., Majerus P.W.;
RT "Characterization of myotubularin-related protein 7 and its binding
RT partner, myotubularin-related protein 9.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9768-9773(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-578, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
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).
RN [5]
RP INTERACTION WITH RAB1B.
RX PubMed=23188820; DOI=10.1074/jbc.m112.395087;
RA Mochizuki Y., Ohashi R., Kawamura T., Iwanari H., Kodama T., Naito M.,
RA Hamakubo T.;
RT "Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6)
RT is regulated by small GTPase Rab1B in the early secretory and autophagic
RT pathways.";
RL J. Biol. Chem. 288:1009-1021(2013).
CC -!- FUNCTION: Phosphatase that specifically dephosphorylates
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) and inositol 1,3-
CC bisphosphate (Ins(1,3)P2). {ECO:0000269|PubMed:12890864}.
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:12890864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3-bisphosphate + H2O = 1D-myo-inositol 1-
CC phosphate + phosphate; Xref=Rhea:RHEA:57840, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58433, ChEBI:CHEBI:83242;
CC Evidence={ECO:0000269|PubMed:12890864};
CC -!- ACTIVITY REGULATION: Interaction with MTMR9 increases phosphatase
CC activity. {ECO:0000269|PubMed:12890864}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57 uM for inositol 1,3-bisphosphate (at pH 6 and in presence of
CC MTMR9) {ECO:0000269|PubMed:12890864};
CC Vmax=7.2 umol/min/mg enzyme (at pH 6 and in presence of MTMR9)
CC {ECO:0000269|PubMed:12890864};
CC -!- SUBUNIT: Heterodimer (via C-terminus) with MTMR9 (via coiled coil
CC domain); the interaction enhances MTMR7 catalytic activity
CC (PubMed:12890864). Does not homodimerize (PubMed:12890864). Interacts
CC with RAB1B (in GDP-bound form) (PubMed:23188820).
CC {ECO:0000269|PubMed:12890864, ECO:0000269|PubMed:23188820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12890864}.
CC Endomembrane system {ECO:0000269|PubMed:12890864}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12890864}; Cytoplasmic side
CC {ECO:0000269|PubMed:12890864}. Note=May partially localize to endosomes
CC and/or the Golgi apparatus. {ECO:0000269|PubMed:12890864}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
CC Expressed at low levels in liver, kidney and testis.
CC {ECO:0000269|PubMed:12890864}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AK081973; BAC38383.1; -; mRNA.
DR EMBL; AF073882; AAC80004.1; -; mRNA.
DR CCDS; CCDS40324.1; -.
DR RefSeq; NP_001035789.1; NM_001040699.1.
DR AlphaFoldDB; Q9Z2C9; -.
DR SMR; Q9Z2C9; -.
DR BioGRID; 207637; 3.
DR STRING; 10090.ENSMUSP00000043851; -.
DR iPTMnet; Q9Z2C9; -.
DR PhosphoSitePlus; Q9Z2C9; -.
DR MaxQB; Q9Z2C9; -.
DR PaxDb; Q9Z2C9; -.
DR PeptideAtlas; Q9Z2C9; -.
DR PRIDE; Q9Z2C9; -.
DR ProteomicsDB; 290112; -.
DR Antibodypedia; 1473; 72 antibodies from 17 providers.
DR DNASU; 54384; -.
DR Ensembl; ENSMUST00000048898; ENSMUSP00000043851; ENSMUSG00000039431.
DR GeneID; 54384; -.
DR KEGG; mmu:54384; -.
DR UCSC; uc009lmz.1; mouse.
DR CTD; 9108; -.
DR MGI; MGI:1891693; Mtmr7.
DR VEuPathDB; HostDB:ENSMUSG00000039431; -.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000155777; -.
DR InParanoid; Q9Z2C9; -.
DR OMA; GSDFMYV; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q9Z2C9; -.
DR TreeFam; TF315197; -.
DR Reactome; R-MMU-1660517; Synthesis of PIPs at the late endosome membrane.
DR BioGRID-ORCS; 54384; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Mtmr7; mouse.
DR PRO; PR:Q9Z2C9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z2C9; protein.
DR Bgee; ENSMUSG00000039431; Expressed in epithelium of lens and 214 other tissues.
DR ExpressionAtlas; Q9Z2C9; baseline and differential.
DR Genevisible; Q9Z2C9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; EXP:Reactome.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:MGI.
DR CDD; cd13344; PH-GRAM_MTMR7; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030572; MTMR7.
DR InterPro; IPR036003; MTMR7_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:SF35; PTHR10807:SF35; 1.
DR Pfam; PF06602; Myotub-related; 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 Coiled coil; Cytoplasm; Hydrolase; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..660
FT /note="Myotubularin-related protein 7"
FT /id="PRO_0000094941"
FT DOMAIN 126..504
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 550..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..548
FT /evidence="ECO:0000255"
FT COMPBIAS 562..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 338..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 579..602
FT /note="PQDYSGNSKSFPSRSPSQGDEDSA -> LRITVGTASPSHPGARPRVMKILL
FT (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75608 MW; 57CA1A447192A52B CRC64;
MEHIRTPKVE NVRLVDRVSC KKAALGTLYL TATHVIFVEN APDTRKETWI LHSQISTIEK
QATTATGCPL LIRCKNFQIV QLVIPQERDC HDVYISLIRL ARPVKYEELY CFSFNPKLDK
EEREQGWLLV DLSEEYKRMG LPDNYWQLSD VNRDYRVCDS YPTELYVPRS ATAHIIVGSS
KFRSRRRFPA LSYYCKDSHA SICRSSQPLS GFSARCLEDE QMLQAIRKAN PGSDFIYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIKFQF IGIENIHVMR NSLQKMLEVC ELKSPSMSDF
LWGLENSGWL RHIKAIMDAG IFIAKAVSEE GASVLVHCSD GWDRTAQVCS VASLLLDPYY
RTLKGFMVLI EKDWISFGHK FNHRYGNLDG DPKEISPVID QFIECVWQLT EQFPCAFEFN
ERFLTHIQHH VYSCQFGNFL CNSQKERREL KIQERTYSLW SNLWKNRADY LNPLFRADHS
QTQGSLHLPT APCNFTYKFW NGMYNRFEKG LQPRQSVTDY LMAVKEESQQ LEEELESLEE
RLEKIQKVHL HGTKVKSKQS EPSKHSGFST SDHSTANTPQ DYSGNSKSFP SRSPSQGDED
SALILTQDNL KSSDPDLSVN SDQESGVEDL SCRSPSGGEH APSEDSGKDR DSDEAVFLTA
