ID A0A3B1INC5_ASTMX Unreviewed; 1240 AA.
AC A0A3B1INC5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000031050.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000031050.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
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 Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR Ensembl; ENSAMXT00000032773.1; ENSAMXP00000048259.1; ENSAMXG00000006103.2.
DR Ensembl; ENSAMXT00000033248.1; ENSAMXP00000031050.1; ENSAMXG00000006103.2.
DR GeneTree; ENSGT00940000157272; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000006103; Expressed in camera-type eye and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine 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; cd15732; FYVE_MTMR3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF66; MYOTUBULARIN-RELATED PROTEIN 3; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 155..575
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1152..1221
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 582..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 325..328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 350..351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 412..418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1240 AA; 137759 MW; 52C694E8ABBE3E96 CRC64;
MEEEGQQSLE CIQANHFFPR KPPVLEEEDL QVPFPELHGE FTKYVGRAED AVIAMSSYRL
HIKFKESLVN VPLQIIESVE CRDMFQLHVT CKDCKVIRCQ FSTFEQCQEW LKRLSVVARP
PSQLEELFSF AFHAWCMDSC SSEKEQHGEL CRPEEHVISR FRNEVERMGF DTQNAWRISE
INNNYKLCSS YPQQLVVPAW ITDKELENVA AFRSWKRFPA VVYRHLSTGA VIARCGQPEV
SWWGWRNADD EHLVQSIARA CAVDSSSPKT LTNGSFSREY TNGADLSDVD FDSSMTNSSE
VETLAIQPHK LLILDARSYA AAVANRAKGG GCECPEYYPN CEVVFMGMAN IHSIRKSFQS
LRFLCTQMPD PANWLSALES TKWLQHLSLL LKAALLVVNA VDRDHRPVLV HCSDGWDRTP
QIVALSKLLL DPYYRTIEGF QVLVETEWLD FGHKFADRCG HGENSEDLNE RCPVFLQWLD
CVHQLQRQFP CSFEFNEAFL VKLVQHTYSC LFGTFLGNSA KEREDRHIQE RTCSVWSLLR
PANRSFKNML YSSHSETVLH PVCHVRNLML WTAVYLPSSS PTTPSDDSCA PYPASGANPE
DQPLGRRPKT RSFDNLPSAC EVGNSLPPNR RSSDPSLNEK WQDHRRSLEL NIGTGSDGAH
DSEEKANGQL PGGLNGTTLD GESEEGEGLR DANYVRLPLG EGVEAELSLG VAVGQMENIL
QEAAADSLRD VKVDSANNTA ILDGVENQNS ADADVAEIGE KVVTNGVEMQ LESNANGSNE
EFPKETKLNG LPSVAEIDKP CQSEAQLPQD LGGEQNAPES QESDELAEEV SKCTIEEALN
LPCTHNPSHS PSTALRTMTN GYGEKGNTPV PDPETARSVP ETVELAAEKR LSLLESSTET
LTEDLGLRPD TLVSAPAPVP AQPAPSIKST CLKHHVPEAE PEPQGAPRTL NGTSKRLSLS
ASSASAEPLH PVCNGDSSEP EASTPQWARV NGDRAPLSRQ VSLASCGSLT GQLHMRGSCS
HHRCLHAALL GRPPTSPPQE PPSARNHLDD DGLTLHTDAV QQRLRQIEVG HQLEVEALKR
QVQELWSRLE SQQTVGMLRL NGDMGDEVTS IADSDFNLDP NCLSRCSTEL FSEASWEQVD
TKDTEVTRWY PDHLAAQCYG CERGFWLATR KHHCRSKEHV EEAWNCGNVF CASCCDQKIP
VPSQQLFEPS RVCKACYSSL QAPAPPLELE LDKPITASSN
//
