ID A0A1S3EZR3_DIPOR Unreviewed; 1163 AA.
AC A0A1S3EZR3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
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_012869881.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012869881.1};
RN [1] {ECO:0000313|RefSeq:XP_012869881.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012869881.1};
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_012869881.1; XM_013014427.1.
DR AlphaFoldDB; A0A1S3EZR3; -.
DR GeneID; 105984295; -.
DR CTD; 8897; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000081671; Unplaced.
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 CDD; cd13341; PH-GRAM_MTMR3; 1.
DR CDD; cd14586; PTP-MTMR3; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035888; MTMR3_PH-GRAM.
DR InterPro; IPR046352; MTMR3_PTP.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000081671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 155..576
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1084..1144
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 265..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1037..1064
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 265..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 326..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 413..419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1163 AA; 129512 MW; DEB3BE30CF1BE6CF CRC64;
MDEETGHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEYVGRAED AIIALSNYRL
HIKFKESLVN VPLQLIETVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQDW LKRLNNAIRP
PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN
INEKYKLCGS YPQELIVPAW ITDKELESVA SFRSWKRIPA VVYRHQNNGA VIARCGQPEV
SWWGWRNADD EHLVQSVAKA CASDSRSSGS KLSTRNSSRD FPNGADLSDV EFDSSLSNAS
GAENLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ
SLRLLCTQMP DPGNWLSALE GTKWLHHLSV LLKSALLVVH AVDRDQRPVL VHCSDGWDRT
PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL
DCVHQLQRQF PCSFEFSEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL
RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPSTPVDESC APYPAPGTSP
DEPPLSRLPK TRSFDNLTTA CDSTMPLASR RSSDPSLNEK WQEHRRSLEL SSLAGPGEEL
PTHAADSLGK PSRMPGGAEL SVAAGVAEGQ MENILQEATK EESGAEEPPH RGGVEIPEVK
EETLLAKESR RMSAEGSLVL YQEPELEDAT PQSQPDSSMS LFSQGIPQQQ GGHSVLSSLQ
APSRGEDSQG TPGEPPRIRD ATEGREGAVP PIPVDAKVGH GTSQSSSMLP SQIPCETGGP
NVDSSVDVLI EDKVTSESGP QVHRRPLLIT SDRFSGKDMP AAELWPAERN LAERPQGESV
MHRTSPGSTL SPKRAHCALP LAECKEGLVC NGSPETENKA LEQPIGLSTI QKYPTPNGHC
TNGEAGRNKD SLSRQMSVTS CSSAHLYSRN LHHKWLHSHL GRPSATSSPD QPSRSHLDDD
GMPVYTDTIQ QRLRQIESGH QQEVETLKKQ VQELKSRLES QYLTSSLRFN GDFGDEVMTR
WLPDHLAAHC YACDSAFWLA SRKHHCRNCG NVFCSSCCNQ KVPVPSQQLF EPSRVCKSCY
NSLHPTSSSI DLELDKPIAA TSN
//
