ID A0A3P9AB92_ESOLU Unreviewed; 591 AA.
AC A0A3P9AB92;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
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 Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000037904.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000037904.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000037904.2}
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 -!- 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_019899367.1; XM_020043808.1.
DR AlphaFoldDB; A0A3P9AB92; -.
DR STRING; 8010.ENSELUP00000037904; -.
DR Ensembl; ENSELUT00000027872.2; ENSELUP00000037904.2; ENSELUG00000017650.2.
DR GeneTree; ENSGT00940000155777; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000265140; LG25.
DR Bgee; ENSELUG00000017650; Expressed in liver and 15 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:UP000265140}.
FT DOMAIN 141..517
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 542..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 290..291
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 353..359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 591 AA; 68089 MW; 4D5EF0F409A473C7 CRC64;
MRITFRRVCD IFGTRKTNRT QPMVENVRLI DRTVSRKATV GTLYLSATHT IFVENNPETR
KETWVLHSLV ASVERPPTTP SGSHLVIRTK NFQVLELLVP QERDATDIHA SLARLSRPEK
YSELYCLSIN PTANKEEREE SWSFLDLHAD YRRMGVPNNL WVGTPANSEY RVCDTYPSEL
FVPKSATPPV IVGSSKFRSR GRFPVLTYFH QDTLASICRC SQPLSGFSAR SQEDEQMMQA
IMKANPGSEY IYVVDTRPKL NAMANRAAGK GYENEDHYTN IKLQFIGIEN IHVMRNSQQK
IIDMGEVKTP SMGDFLWGLE SSGWLKHIKA VLDAGVFIAK AVAEEGVSVV VHCSDGWDRT
AQACSLASVL LDPYYRTMKG LMLLIERDWV SFGHKFSHRY NHLDGDPKEV SPVIDQFVEC
VWQLSEQFPC AFEFNERFLI QLRRHVYSCQ YGNFLGNSQK ERRDMRLRER TYSLWPQLWK
DRAQYVNPLY RADHTQTQGM LRPNTTPYCF KMWKGMYNRL EKSAPPRHSP ADLLTAVREE
TQQLEQELTN HQEVAPRGTA HSGTKQEDSS PDEEEADEQQ QRRSEDDERN V
//
