MTMR7_PONAB
ID MTMR7_PONAB Reviewed; 660 AA.
AC Q5R6F6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2C9}.
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
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DR EMBL; CR860534; CAH92660.1; -; mRNA.
DR RefSeq; NP_001126555.1; NM_001133083.1.
DR AlphaFoldDB; Q5R6F6; -.
DR SMR; Q5R6F6; -.
DR STRING; 9601.ENSPPYP00000020599; -.
DR GeneID; 100173546; -.
DR KEGG; pon:100173546; -.
DR CTD; 9108; -.
DR eggNOG; KOG1089; Eukaryota.
DR InParanoid; Q5R6F6; -.
DR OrthoDB; 824298at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IEA:UniProt.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:UniProt.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
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 2: Evidence at transcript 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_0000094942"
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 514..558
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"
SQ SEQUENCE 660 AA; 75734 MW; DC25690EA650CDC2 CRC64;
MEHIRTPKVE NVRLVDRVSP KKAALGTLYL TATHVIFVEN SPGSRKETWI LHSQISTIEK
QATTATGCPL LIRCKNFQII QLIIPQERDC HDVYISLIRL ARPVKYGELY CFSFNPMLDK
EEREQGWVLI DLSEEYKRMG LPNHYWQLSD VNRDYRVCDS YPTELYVPKS ATAHIIVGSS
KFRSRRRFPV LSYYYKDNHA SICRSSQPLS GFSARCLEDE QMLQAIRKAN PGSDFVYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIKFQF IGIENIHVMR NSLQKMLEVC ELKSPSMSDF
LWGLENSGWL RHIKAIMDAG IFIAKAVSEE GTSVLVHCSD GWDRTAQVCS VASLLLDPHY
RTLKGFMVLI EKDWISFGHK FNHRYGNLDG DPKEISPVID QFIECVWQLM EQFPCAFEFN
ERFLIHIQHH IYSCQFGNFL CNSQKERQEL KIQERTYSLW AHLWKNRADY LNPLFRADHS
QTQGTLHLPT IPCNFMYKFW SGMYNRFEKG MQPRQSVTDY LMAVKEETQQ LEEELEALEE
RLEKIQKVQL NCTKVKSKQS EPSKHSGFST SDNSIANTPQ DYSGNMKSFP SRSPSQGDED
SALILTQDNL KSSDPDLSAN SDQESGVEDL SCRSPSGGEH APSEDSGKDR DSDEAVFLTA
