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Database: UniProt
Entry: G3UAC2_LOXAF
LinkDB: G3UAC2_LOXAF
Original site: G3UAC2_LOXAF 
ID   G3UAC2_LOXAF            Unreviewed;       540 AA.
AC   G3UAC2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=MTMR6 {ECO:0000313|Ensembl:ENSLAFP00000024780.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000024780.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000024780.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000024780.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000024780.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000024780.1};
RG   Ensembl;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   AlphaFoldDB; G3UAC2; -.
DR   Ensembl; ENSLAFT00000029261.1; ENSLAFP00000024780.1; ENSLAFG00000008869.3.
DR   GeneTree; ENSGT00940000158055; -.
DR   HOGENOM; CLU_001839_3_2_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF34; MYOTUBULARIN-RELATED PROTEIN 6; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT   DOMAIN          124..505
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   ACT_SITE        339
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         276..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         339..345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   540 AA;  62724 MW;  E2683C3BA85C40EA CRC64;
     VVHVVSKKVE QVKALDRFST SNKSLTGTLY LTATHLLFID SHQKETWILH HHIASVEKLA
     LTTSGCPLVI QCKNFRIVHF IVPRERDCHD IYNSLLQLSK QAKYEDLYAF SYNPKQNDAE
     RLQGWQLIDL AEEYERMGVP NSHWQLSDAN REYKICETYP RELYVPQVAS KPIIVGSSKF
     RSKGRFPVLS YYHQDKEKTQ AAICRCSQPL SGFSARCLED EHLLQAISKA NPVNRYMYVM
     DTRPKLNAMA NRAAGKGYEN EDNYSNIRFQ FVGIENIHVM RSSLQKLLEV NGTKGLSVND
     FYSGMESSGW LRHVKAVMDA AIFLAKAIMV ENASVLVHCS DGWDRTSQVC SLGSLLLDSY
     YRTIKGFMVL IEKDWISFGH KFSERGARCG HLDGDPKEIS PVFIQFLECV WHLTEQFPQA
     FEFNEAFLLQ IHEHIHSCQF GNFLGNCQKE REELKLKEKT YSLWPFLLDD RKKYLNPLYS
     SKAQRFTVLE PSTVSFSFKF WRNMYHQFDR TLHPRQSVFN IIMNMNEQNK QLEKEIKDLE
//
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