ID A0A2K5UD42_MACFA Unreviewed; 660 AA.
AC A0A2K5UD42;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
GN Name=MTMR7 {ECO:0000313|Ensembl:ENSMFAP00000010267.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000010267.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000010267.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000010267.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001291};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR AlphaFoldDB; A0A2K5UD42; -.
DR STRING; 9541.ENSMFAP00000010267; -.
DR Ensembl; ENSMFAT00000039848.2; ENSMFAP00000010267.2; ENSMFAG00000006049.2.
DR VEuPathDB; HostDB:ENSMFAG00000006049; -.
DR GeneTree; ENSGT00940000155777; -.
DR Proteomes; UP000233100; Chromosome 8.
DR Bgee; ENSMFAG00000006049; Expressed in temporal lobe and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IEA:UniProt.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:UniProt.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR CDD; cd13344; PH-GRAM_MTMR7; 1.
DR CDD; cd14583; PTP-MTMR7; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036003; MTMR7_PH-GRAM.
DR InterPro; IPR030572; MTMR7_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:SF35; MYOTUBULARIN-RELATED PROTEIN 7; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF21098; PH-GRAM_MTMR6-like; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 126..504
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 307..351
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 554..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..551
FT /evidence="ECO:0000256|SAM:Coils"
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:0000256|PIRSR:PIRSR630564-1"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 338..344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 660 AA; 75794 MW; B2CB571D38F0F7B0 CRC64;
MEHIRTPKVE NVRLVDRVSP KKAALGTLYL TATHVIFVEN SPDTRKETWI LHSQISTIEK
QATTATGCPL LIRCKNFQII QLIIPQERDC HDVYISLIRL ARPVKYEELY CFSFNPMLDK
EEREQGWVLI DLSEEYKRMG LPNHHWQLSD VNRDYRVCDS YPTELYVPKS ATAHIIVGSS
KFRSRRRFPV LSYYYKDNHA SICRSSQPLS GFSARCLEDE QMLQAIRKAN PGSDFVYVVD
TRPKLNAMAN RAAGKGYENE DNYSNIKFQF IGIENIHVMR NSLQKMLEVC ELKSPSMSDF
LWGLENSGWL RHIKAIMDAG IFIAKAVSEE GASVLVHCSD GWDRTAQVCS VASLLLDPHY
RTLKGFMVLI EKDWISFGHK FNHRYGNLDG DPKEVSPVID QFIECVWQLM EQFPCAFEFN
ERFLIHIQHH IYSCQFGNFL CNSQKERREL KIQERTYSLW AHLWKNRADY LNPLFRADHS
QTQGTLHLPT APCNFMYKFW SGMYNRFEKG MQPRQSVTDY LMAVKEETQQ LEEELEALEE
RLEKIQKVQL NCTKVKSKQS EPSKHSGFST SDNSIANTPQ DYSGNMKSFP SRSPSQGDED
SALILTQDNL KSSDPDLSAN SDQESGVEDL SCRSPSGGEH APSEDSGKDR DSDEAVFLTA
//
