ID G5BJU1_HETGA Unreviewed; 1195 AA.
AC G5BJU1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE Flags: Fragment;
GN ORFNames=GW7_05220 {ECO:0000313|EMBL:EHB09552.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB09552.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB09552.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH170667; EHB09552.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BJU1; -.
DR STRING; 10181.G5BJU1; -.
DR eggNOG; KOG4471; Eukaryota.
DR InParanoid; G5BJU1; -.
DR Proteomes; UP000006813; 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: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 CDD; cd15733; FYVE_MTMR4; 1.
DR CDD; cd13342; PH-GRAM_MTMR4; 1.
DR CDD; cd14587; PTP-MTMR4; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046978; MTMR4_FYVE.
DR InterPro; IPR035997; MTMR4_PH-GRAM.
DR InterPro; IPR030590; MTMR4_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; IPR000387; Tyr_Pase_dom.
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:SF64; MYOTUBULARIN-RELATED PROTEIN 4; 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 SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
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:UP000006813};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 153..569
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 375..419
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1114..1174
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 319..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 344..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 406..412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT NON_TER 1195
FT /evidence="ECO:0000313|EMBL:EHB09552.1"
SQ SEQUENCE 1195 AA; 133615 MW; FA571CC453D98CCD CRC64;
QGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRAAD ALIAISNYRL
HIKFKDSVIN VPLRMIDSVE SRDMFQLHIS CKDSKVVRCH FPTFKQCQEW LSRLSRATAR
PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELLRMGFDL QNVWRVSHIN
SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW
WGWRNADDEY LVTSIAKACA LDPGTRATGG SLGTGNDANE ACDADFDSSL TACSGVESAA
APQKLLILDA RSYTAAVANR AKGGGCECEE YYPNCEVVFM GMANIHAIRN SFQYLRAVCS
QMPDPSNWLS ALESTKWLQH LSVMLKAAVL VANTVDREGR PVLVHCSDGW DRTPQIVALA
KILLDPYYRT LEGFQVLVES DWLDFGHKFG DRCGHQENVE DQNEQCPVFL QWLDSVHQLL
KQFPCLFEFN EAFLVKLVQH TYSCLYGTFL ANNPCEREKH NIYKRTCSVW ALLRAGNKNF
HNFLYMPGSD MVLHPVCHVR ALHLWTAVYL PASSPCTLGE ENMDLYLSPV AQSQEFSGRS
LDRLPKTRSM DDLLSTCDTS SPLTRTSSDP NLNNHCQEVR VGLEPWHSNP EGSETIFMDP
GVGGAQQTMG EMGPPSPLPS SQKDYLSNKP FKTHKSCSLS YKLLNTAVPQ EMKSNTSDPE
IKVLGQAMTP APDPSAQDEL GRTFDGPGEL PEHHPETEAA RALSKVVSSK CDGIGDLPES
SQDSLMGALQ QAQLDSVLGV PPKCALDCSL DTLCNPPTAA CQIPLVPSPD FLSQDPPGCM
ASVSHQERPR SVLNLIHREE DTGKKGINRN GQLLENPRFG KMPLELARKP ISQSQISEFS
FLGSNWDSFQ GMVTSFPSGE NTPRRLLSYG CCSKWSSSKQ IRATGPCFGG QWAQREGVKS
SVCSNHSNGY CTGPGGKKNR MWLSGHPKQV SSTKPVPLIC PSPVPPLYLD DDGLPFPTDV
IQHRLRQIEA GYKQEVDQLR RQVRELQMRL DIRHCCAPPA EPPMDYEDDF TCLKESDGSD
TEDFGSDHSE DCLSEASWEP VDKKETEVTR WVPDHMASHC YNCDCEFWLA KRRHHCRNCG
NVFCAGCCHL KLPIPDQQLY DPVLVCNSCY EHIQVSRARE LMSQHLKKPI ATASS
//
