ID A0A287DC02_ICTTR Unreviewed; 1006 AA.
AC A0A287DC02;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=MTMR3 {ECO:0000313|Ensembl:ENSSTOP00000031073.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000031073.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000031073.1}
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 EMBL; AGTP01126883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01126884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287DC02; -.
DR STRING; 43179.ENSSTOP00000031073; -.
DR Ensembl; ENSSTOT00000042322.1; ENSSTOP00000031073.1; ENSSTOG00000032750.1.
DR GeneTree; ENSGT00940000157272; -.
DR InParanoid; A0A287DC02; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:Ensembl.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:1904562; P:phosphatidylinositol 5-phosphate metabolic process; IEA:Ensembl.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IEA:Ensembl.
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; 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 SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 34..411
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 927..987
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 425..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..870
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 267
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 192..195
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 267..273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1006 AA; 111106 MW; FA8D31FF51C79E26 CRC64;
HSLEGIQINQ IFPRKQLIRE DENLQVPSLE LHGESTEYVG RDEDAIIALL DYRLHIKFKE
ISNINEKYKL CDSYPQELIV PAWITNKELE SVASFRSWKC IPAVVYRHQS NGAVIAHCGQ
PEVNWWDWQN ADDEHLVQSV AKACVYLVFT LPPFLMSVDS SLSNASGAES LAIQLQKLLI
LDARSYAGAV ANRAKGGGCK CPDYYPNCEV VFMGMANIHS IRRSFQSLRL LCTQTPDPGN
WLSALESTKW LRHLSVLLKS RPVLVHCSDG WNRTPQIVAL AKLLLDPYYG TIEGFQVLVE
MEWLDFGHKF ADRCSHGENS NDLKECCSVF SQWLDCVKLV QHTYSCLFGT FLCNNAKERG
EKHTQERTCS VWSLLRAGNK AFKNLLYSSQ SEAVLYPVCH VRNLMLWSAV YLPCPSPSTP
VDDSCAPYPV PGTSPDDPPL SRLPKTRSFD NLTIACDSTV PLASRRSSDP SLNEKWQEHR
RSLELSNLAG PGEEPSADSL GKPSRVPGGA ELSVAAGVAE GQMENILQEA TKEESGAEEP
AHRGSVEMPQ IKEENRIATE GSAIVLYQEA ELGVAILRSH PDSSLSIFSQ GIPEEQAGPS
VLSSSLQEPY RGEDSREVPL EQPPIEDIAE NQEDAAPSIP VDVKVGYSTS LSSSLSMDML
IEDNVKSESG PQVHRKPCLV ITGRFSGKDV LPPALEPKPK PQGGFVVHRT SPGSTLNPTW
APCALPLAEC KEGFVCNGAP ETENKASEQP PALGTLQKYS TPNGHCANAE AGRSKDSLSC
QLSATSCSSV HLHLRNLHHK WLHSHAGRPS AVSSPEHPSR SHLDDDSMPV YTDTIQQRLG
QIESGHQQEV ETLKKQVQEL KSRLESQYLT GSLSFNGDFE DDVTSIPDLE SNLDQNCLSH
CSPEIFSEAS WEQVDKQDIE MTCWLPDYLA AHCYACDSAF WLASRKHHCR NCGNVFCSSC
CNQKVPVPSQ QLFEPSRVCK SCYSSLHPTS SSIDLELDKP IAATSN
//
