MTMR7_HUMAN
ID MTMR7_HUMAN Reviewed; 660 AA.
AC Q9Y216; A1L4K9; B4DG87; Q68DX4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Myotubularin-related protein 7;
DE AltName: Full=Inositol 1,3-bisphosphate phosphatase {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9Z2C9};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305};
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q9Z2C9};
GN Name=MTMR7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-44 AND
RP HIS-559.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-44.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-44.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-577 (ISOFORM 2), AND TISSUE SPECIFICITY.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16787938; DOI=10.1242/jcs.03040;
RA Lorenzo O., Urbe S., Clague M.J.;
RT "Systematic analysis of myotubularins: heteromeric interactions,
RT subcellular localisation and endosome related functions.";
RL J. Cell Sci. 119:2953-2959(2006).
CC -!- FUNCTION: Phosphatase that specifically dephosphorylates
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) and inositol 1,3-
CC bisphosphate (Ins(1,3)P2). {ECO:0000250|UniProtKB:Q9Z2C9}.
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:0000250|UniProtKB:Q9Z2C9};
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:0000250|UniProtKB:Q9Z2C9};
CC -!- ACTIVITY REGULATION: Interaction with MTMR9 increases phosphatase
CC activity. {ECO:0000250|UniProtKB:Q9Z2C9}.
CC -!- SUBUNIT: Heterodimer (via C-terminus) with MTMR9 (via coiled coil
CC domain); the interaction enhances MTMR7 catalytic activity (By
CC similarity). Does not homodimerize (By similarity). Interacts with
CC RAB1B (in GDP-bound form) (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z2C9}.
CC -!- INTERACTION:
CC Q9Y216; P51946: CCNH; NbExp=6; IntAct=EBI-10293003, EBI-741406;
CC Q9Y216; Q96QG7: MTMR9; NbExp=14; IntAct=EBI-10293003, EBI-744593;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16787938}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q9Z2C9}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9Z2C9}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z2C9}. Note=May partially localize to
CC endosomes and/or the Golgi apparatus. {ECO:0000250|UniProtKB:Q9Z2C9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y216-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y216-2; Sequence=VSP_017000, VSP_017001;
CC -!- TISSUE SPECIFICITY: Expressed specifically in brain.
CC {ECO:0000269|PubMed:9736772}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; AK294468; BAG57698.1; -; mRNA.
DR EMBL; CR749240; CAH18096.1; -; mRNA.
DR EMBL; AC124074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130577; AAI30578.1; -; mRNA.
DR EMBL; BC130579; AAI30580.1; -; mRNA.
DR EMBL; AF073482; AAC77820.1; -; mRNA.
DR CCDS; CCDS34851.1; -. [Q9Y216-1]
DR RefSeq; NP_004677.3; NM_004686.4. [Q9Y216-1]
DR AlphaFoldDB; Q9Y216; -.
DR SMR; Q9Y216; -.
DR BioGRID; 114559; 65.
DR IntAct; Q9Y216; 12.
DR MINT; Q9Y216; -.
DR STRING; 9606.ENSP00000180173; -.
DR DEPOD; MTMR7; -.
DR iPTMnet; Q9Y216; -.
DR PhosphoSitePlus; Q9Y216; -.
DR BioMuta; MTMR7; -.
DR DMDM; 296439297; -.
DR EPD; Q9Y216; -.
DR jPOST; Q9Y216; -.
DR MassIVE; Q9Y216; -.
DR MaxQB; Q9Y216; -.
DR PaxDb; Q9Y216; -.
DR PeptideAtlas; Q9Y216; -.
DR PRIDE; Q9Y216; -.
DR ProteomicsDB; 85591; -. [Q9Y216-1]
DR ProteomicsDB; 85592; -. [Q9Y216-2]
DR Antibodypedia; 1473; 72 antibodies from 17 providers.
DR DNASU; 9108; -.
DR Ensembl; ENST00000180173.10; ENSP00000180173.4; ENSG00000003987.14. [Q9Y216-1]
DR Ensembl; ENST00000521857.5; ENSP00000429733.1; ENSG00000003987.14. [Q9Y216-2]
DR GeneID; 9108; -.
DR KEGG; hsa:9108; -.
DR MANE-Select; ENST00000180173.10; ENSP00000180173.4; NM_004686.5; NP_004677.3.
DR UCSC; uc003wxm.4; human. [Q9Y216-1]
DR CTD; 9108; -.
DR DisGeNET; 9108; -.
DR GeneCards; MTMR7; -.
DR HGNC; HGNC:7454; MTMR7.
DR HPA; ENSG00000003987; Tissue enhanced (brain, retina).
DR MIM; 603562; gene.
DR neXtProt; NX_Q9Y216; -.
DR OpenTargets; ENSG00000003987; -.
DR PharmGKB; PA31257; -.
DR VEuPathDB; HostDB:ENSG00000003987; -.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000155777; -.
DR HOGENOM; CLU_001839_3_2_1; -.
DR InParanoid; Q9Y216; -.
DR OMA; GSDFMYV; -.
DR PhylomeDB; Q9Y216; -.
DR TreeFam; TF315197; -.
DR PathwayCommons; Q9Y216; -.
DR Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SignaLink; Q9Y216; -.
DR BioGRID-ORCS; 9108; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; MTMR7; human.
DR GenomeRNAi; 9108; -.
DR Pharos; Q9Y216; Tbio.
DR PRO; PR:Q9Y216; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y216; protein.
DR Bgee; ENSG00000003987; Expressed in islet of Langerhans and 101 other tissues.
DR ExpressionAtlas; Q9Y216; baseline and differential.
DR Genevisible; Q9Y216; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IEA:RHEA.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; TAS:Reactome.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:Ensembl.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
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 Alternative splicing; Coiled coil; Cytoplasm; Hydrolase; Lipid metabolism;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..660
FT /note="Myotubularin-related protein 7"
FT /id="PRO_0000094940"
FT DOMAIN 126..504
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 554..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..551
FT /evidence="ECO:0000255"
FT COMPBIAS 554..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:0000250|UniProtKB:Q9Z2C9"
FT VAR_SEQ 541..577
FT /note="RLEKIQKVQLNCTKVKSKQSEPSKHSGFSTSDNSIAN -> VRHTCFVNLFS
FT VLIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9736772"
FT /id="VSP_017000"
FT VAR_SEQ 578..660
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9736772"
FT /id="VSP_017001"
FT VARIANT 44
FT /note="P -> A (in dbSNP:rs7388581)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_059779"
FT VARIANT 559
FT /note="Q -> H (in dbSNP:rs3764796)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057144"
FT CONFLICT 241
FT /note="T -> A (in Ref. 2; CAH18096)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="Y -> N (in Ref. 4; AAC77820)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="P -> L (in Ref. 4; AAC77820)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="L -> F (in Ref. 4; AAC77820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75833 MW; 05374B19BB500580 CRC64;
MEHIRTPKVE NVRLVDRVSP KKAALGTLYL TATHVIFVEN SPDPRKETWI LHSQISTIEK
QATTATGCPL LIRCKNFQII QLIIPQERDC HDVYISLIRL ARPVKYEELY CFSFNPMLDK
EEREQGWVLI DLSEEYTRMG LPNHYWQLSD VNRDYRVCDS YPTELYVPKS ATAHIIVGSS
KFRSRRRFPV LSYYYKDNHA SICRSSQPLS GFSARCLEDE QMLQAIRKAN PGSDFVYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIKFQF IGIENIHVMR NSLQKMLEVC ELKSPSMSDF
LWGLENSGWL RHIKAIMDAG IFIAKAVSEE GASVLVHCSD GWDRTAQVCS VASLLLDPHY
RTLKGFMVLI EKDWISFGHK FNHRYGNLDG DPKEISPVID QFIECVWQLM EQFPCAFEFN
ERFLIHIQHH IYSCQFGNFL CNSQKERREL KIQERTYSLW AHLWKNRADY LNPLFRADHS
QTQGTLHLPT TPCNFMYKFW SGMYNRFEKG MQPRQSVTDY LMAVKEETQQ LEEELEALEE
RLEKIQKVQL NCTKVKSKQS EPSKHSGFST SDNSIANTPQ DYSGNMKSFP SRSPSQGDED
SALILTQDNL KSSDPDLSAN SDQESGVEDL SCRSPSGGEH APSEDSGKDR DSDEAVFLTA
