ID A0A3Q2DPX0_CYPVA Unreviewed; 657 AA.
AC A0A3Q2DPX0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
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};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000021663.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000021663.1}
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 -!- 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 RefSeq; XP_015244706.1; XM_015389220.1.
DR AlphaFoldDB; A0A3Q2DPX0; -.
DR STRING; 28743.ENSCVAP00000021663; -.
DR Ensembl; ENSCVAT00000011229.1; ENSCVAP00000021663.1; ENSCVAG00000003857.1.
DR GeneID; 107093894; -.
DR KEGG; cvg:107093894; -.
DR CTD; 9107; -.
DR GeneTree; ENSGT00940000158055; -.
DR OMA; QWQHTDV; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000265020; Unplaced.
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 GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd13210; PH-GRAM_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 InterPro; IPR000387; Tyr_Pase_dom.
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.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT DOMAIN 129..505
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 310..354
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 550..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 278..279
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 341..347
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 657 AA; 75393 MW; 5213BFDCA31239BF CRC64;
MEHIRTPKVE QVRLVDRFSN KSTNGTLYLT ATHLIFVESS SNNSSSAGQE IWILHHHIAS
VEKQSLTTTG CPLVIHCRNF RVVHFVLQRE RDCHDIYSSL LRLLRPVYYE ELYAFSYNPK
QNDQQREEGW QLIDLGAEFE RMGVPNDQWQ HTDVNREYKV CETYPRDLYV PITASKPIIV
GSSKFRSKGR FPVLTYFYQE KKAAVCRCSQ PLSGFSARCL EDESMLQAIS KANHNSRFVY
VMDTRPKLNA LANRAAGKGY ENEDNYSNIR FQFVGIENIH VMRSSLQKLL EVTGTRSLTM
SDYLGGLESS GWLRHIKAVV DAAVFLTKAV TVEGASVLVH CSDGWDRTAQ VCALGSLLMD
PYYRTIKGFM VLIEKDWISF GHKFADRCDQ LDGDPKEVSP IFTQFLECVW QLTEQFPQAF
EYSEWFLLQI HEHVHSCQYG NFLGNNQRQR EELQLRERTH SLWAFLMSEK QNYLNPFYRP
SYSEAHPVLE PSTLPYHFKF WRNMYHQFDR SMHPRQSILK TILTLKENTR SAESTLQALQ
TRLQQLGVTP IATSDPPAPP PTRDQCTNPL PPRPDSLILG APINHKEVQR REVEDDQDEV
GEEAMESTDT ERTVEGSSGT ESRKQSYGEL EGTCNGELAK EEPAVVSLEL GVARMTC
//
