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Database: UniProt
Entry: A0A0L8GN43_OCTBM
LinkDB: A0A0L8GN43_OCTBM
Original site: A0A0L8GN43_OCTBM 
ID   A0A0L8GN43_OCTBM        Unreviewed;       727 AA.
AC   A0A0L8GN43;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=OCBIM_22031022mg {ECO:0000313|EMBL:KOF78274.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF78274.1};
RN   [1] {ECO:0000313|EMBL:KOF78274.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF78274.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF78274.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KQ421144; KOF78274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L8GN43; -.
DR   EnsemblMetazoa; Ocbimv22031024m; Ocbimv22031024m.p; Ocbimv22031022m.g.
DR   EnsemblMetazoa; XM_014924131.1; XP_014779617.1; LOC106875841.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14533; PTP-MTMR3-like; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
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:SF75; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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;
FT   DOMAIN          1..279
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          85..129
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          509..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         29..32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         54..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         116..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   727 AA;  80598 MW;  99211E5284F7CF9F CRC64;
     MTMGIRENST NALGMLIIDA RSYSAAIANR AKGGGCECAE YYPNCEIQFM NLANIHSIRK
     SFCALRTLCG SSPDQTNWLS GLENTKWLHH IANLLKAACV VASAIHKEGR PVLVHCSDGW
     DRTPQIVALA ELLLDPYYRT SYGFYVLVER EWLQFGHKFA DRCGHDVNNG DSNERCPVFL
     QWLDCVHQIY RQFPCAFEFS EAFLIKLVQH TYSRLFGTFL CNNANERKKA KLKTKTASVW
     SLLLPGNKRF TNSLYNPSTD QVLYPSCHVL NLTLWTHVFL SNNSFSTSSD DIVGTNASDH
     FLDEQHKVDH NNLGKTRSYD DLVGVEHPAY FSRRLSDPNI AVDNHEQAMF PAKECSNSVY
     SLINVNSNHL LEETSASPPQ ELFNGNHCAS TPDSEPADNI EEGNTEMEYQ IKFGEELLNG
     DILTNLTNSE VNGNSSLPSF ITSVSSKSHR TLNKSSQVSV NETFSNSIAP IVDEPLNKLT
     NFRNTCTAKT SSSSSSSTAN LPANVYMNGN IEHQNSSSSS NSSSSSSSSS SSSEEDDYSA
     KCNAERTLQI YSSISTSTSD ISDSRIDANG GDSSSSSAVP PAVSPAETEY RSIPRSSLKF
     NYLFESKMNI SKTKSCPSTP NIPMAQCLKR ALTPVTPAAE SKVQPLLKQC STAQNQTSFN
     VTRHLDPDGL TTHPDTVQQR VNEIRSDYHQ TIEIQKRHLE QLATLYQASA FNGTVRQISD
     KDELKLW
//
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