ID G3PVV8_GASAC Unreviewed; 576 AA.
AC G3PVV8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021747.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021747.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021747.1}
RP IDENTIFICATION.
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; G3PVV8; -.
DR STRING; 69293.ENSGACP00000021747; -.
DR Ensembl; ENSGACT00000021788.1; ENSGACP00000021747.1; ENSGACG00000016465.1.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000155777; -.
DR InParanoid; G3PVV8; -.
DR OMA; ANSEYRI; -.
DR TreeFam; TF315197; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000016465; Expressed in telencephalon and 9 other cell types or tissues.
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 CDD; cd14532; PTP-MTMR6-like; 1.
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:SF124; PHOSPHATIDYLINOSITOL-3-PHOSPHATASE; 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:UP000007635}.
FT DOMAIN 127..503
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 531..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 576 AA; 65906 MW; 0FEA950F6F949404 CRC64;
MEHIRTPKVE NARLLDRSSG QRKASIGTLY LSATHTIFVE NNPETRKETW VLHSMLSSVE
RPPTIPAGSQ LILHCKDFRV FQILIPQERD CLEVHTSLLR LSRPEKYSEL YCLSFNPNVN
KVEREESWNF IDLTADFKRM GVPNNLWVAT VANSEYRVCD TYPSQLFVPK SATTALIVGS
SRFRSRGRFP VLSYFHQDTL AAVCRCSQPL SGFSGRSQDD EMMLQVMMKS NPGSDYIYVV
DTRPKLNAMA NRAAGKGYEN EDHYTNIKLQ FIGIENIHVM RSSQQKILDV GEMRSPSMTD
FLYGLENSGW LKHIKAVLDA GLFIAKAVAN EGVSVLVHCS DGWDRTAQAC SVASILLDPY
YRTIKGLMVL IERDWVSFGH KFSQRYAHLD GDPKEVSPVI DQFLECVWQL SEQFPCAFEF
NERFLIAIHT HIYSCQYGSF LGNSEKERRD MRLHERSHSL WPELWKDRAE YTNPLYKDEL
SQSQGVLRPN TTPYCFKMWK GLYNRMEKSI PPCQSAAHFL SAVKGESQQL KEELTNHQEV
PSEGTANHKP LGFRQDNNPN READLMGGNE CPDEED
//
