ID A0A2D0QYH2_ICTPU Unreviewed; 1162 AA.
AC A0A2D0QYH2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 27-MAR-2024, entry version 30.
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};
GN Name=mtmr3 {ECO:0000313|RefSeq:XP_017323453.2};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017323453.2};
RN [1] {ECO:0000313|RefSeq:XP_017323453.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017323453.2};
RG RefSeq;
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 RefSeq; XP_017323453.2; XM_017467964.3.
DR STRING; 7998.ENSIPUP00000036622; -.
DR KEGG; ipu:108265535; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 101..521
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1067..1136
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 869..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 271..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 296..297
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 358..364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1162 AA; 130959 MW; 25AA6257C973E043 CRC64;
MSSYRLHVNF KESIVNVPLR LIENVECRDM LQLHITCKDC KVIRCQFSTF EQCQEWLKRL
SLVTRPPSHL EELFSFAFHA WCMDSYCGEK EQHTELCRPG EHVISRFHSE VERMGFDTHN
AWRVSEINNK YKLCSSYPQL LVVPSWITDK ELENVAAFRS WKRFPSVVYR HQSTGAVIAR
CGQPEVSWWG WRNADDEHLV QSIARACTMD SSLSKTFINR SFSRDYLNGT DLSDVGFDSS
MTNSSEVESL ASQPHKLLIL DARSYAAAVA NRAKGGGCEC PEYYPNCEVL FMGIANIHSI
RKSFQSLRFL CAQMPDPANW LSALENTKWL QNLSLLLKAA LLVVNAVDRD HRPVLVHCSD
GWDRTPQIVA LSKLLLDPYY RTIEGFQVLV EMEWLDFGHK FADRCGHGEN AEDLNERCPV
FLQWLDCVHQ LQRQFPCSFE FNEAFLVKLV QHTYSCLFGT FLCNNGKERE DQHIQERTCS
VWSLLRPANR SFRNMLYSSL SETVLHPVCH VRNLMLWIAV YLPSSSPTTP YDESCVSFSL
SGMSPEVQPL VRCPKTRSFD NLPSACVVGN SLPSNRRSSD PSLNEKWQEH HRPLELNIVA
GPDGTILQDK EGWPNGQLMA GLNIATLDRE TEDWECSQDI NCVRLPLGEG VETELSVDIA
MGQIENILQE APAVSQKDSK AEYTNNPDIS SGTENKNGTN TYLTVDEKNA IANSFEVPQD
VYVEGDSVES PDESKFSNVQ CQSSVLNKKS CDSVIHLVHA PDGVKATENQ ESVQIVEEVL
DKCTTAVAQN LHSSFNTTYS PSTANRIFNN GYGEEVNKEH KVLCPVPETT RPVTELAEKH
LSILESSTET LTEDLGIRSE TLVPMTVSTQ PKTKHTCLNH SPESDTEPQS APRMLNSTCK
QQTLSGFPLT FASAKPLHTM CNSDSSNPDP STPQQSLLSR QLSLASCSCS IQRCTHSGHS
HLDDDGLTLH TDVVQQRLRQ IEAGHQLEVE ALKRQVQELW SRLQNQYATT AQRCLSGDLG
DEMISIADSD FNLDPNCLSR CSTELFSETS WEQVDRQDTE VTRWYPDHLA VQCYGCERGF
WLVTRKHHCR SKECVEEAWN CGNVFCDSCC DQKIPVPSQQ LFEPSRVCNA CYNSLQSSAP
THGQLQLTSS QYVASTCTAA EG
//
