ID S7MEN6_MYOBR Unreviewed; 1639 AA.
AC S7MEN6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Myotubularin-related protein 4 {ECO:0000313|EMBL:EPQ02789.1};
GN ORFNames=D623_10005404 {ECO:0000313|EMBL:EPQ02789.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ02789.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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; KE161260; EPQ02789.1; -; Genomic_DNA.
DR eggNOG; KOG4471; Eukaryota.
DR Proteomes; UP000052978; 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:InterPro.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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; 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; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 171..588
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 394..438
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 338..341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 363..364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 425..431
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1639 AA; 182802 MW; 1A00295A41D17C6D CRC64;
MRPKGPSGAG DLGLRPSPQG EEGPPSLEYI HAKDLFPPKE LVKEEENLQV PFTVLQGEGV
EFLGRAADAL IAISNYRLHI KFKDSVINVP LRMIDSVESR DMFQLHIACK DSKVVRCHFS
TFKQCQEWLS RLSRATARPA KPEDLFAFAY HAWCLGLTEE DQHTHLCQPG EHIRCRQEAE
LVRMGFDLQN VWRVSHINSN YKLCPSYPQK LLVPVWITDK ELENVASFRS WKRIPVVVYR
HLRNGAAIAR CSQPEISWWG WRNADDEYLV TSIAKACALD PGTRATGGSL GTGNSDASEA
CDTDFDSSLT ACSGVESTAA PQKLLILDAR SYTAAVANRA KGGGCECEEY YPNCEVVFMG
MANIHAIRNS FQYLRAVCSQ MPDPSNWLSA LESTKWLQHL SVMLKAAVLV ANTVDREGRP
VLVHCSDGWD RTPQIVALAK ILLDPYYRTL EGFQVLVESD WLDFGHKFGD RCGHQENAED
QNEQCPVFLQ WLDSVHQLLK QFPCLFEFNE AFLVKLVQHT YSCLYGTFLA NNPCEREKRN
IYKRTCSVWA LLRAGNKNFH NFLYTPGSDM VLHPVCHVRA LHLWTAVYLP ASSPCTLGEE
NMDLYLSPVA QSQEFSGRSL DRLPKTRSMD DLLSACDTSS PLTRTSSDPN LNNHCQETRA
GLEPWHSNPE GSETAFVESG VGGPQQTVGE MGLPSPLPSS QKDYLSNKPF KSHKSCSPSY
KLLSATVPQE MKSNSSDPEI KVLEETKASA PDPPAQEVLC RTLDGTEEPP EHFPEKEAVS
ALSKVISNKC DRICDFPESS QDSLTGAPQQ AQLGSVLGVP SRSAPDHSLG ILCNPPSATC
QTPPDPSTDF LNQDPPESVA SISHQEQPSS VPDLIDGEED TDKKGNNRNG QLLENPRFGK
VPLDLARKPI SQSQISEFSF LGSNWDSFQG MVTSFPSGET TPRRLLSYGC CSKRSSSKQM
RPIGPCFGGQ WVQREGVKSP LCSSHSNGHC TGPGGKNRIW LSGHPKQVSN TKPVPLSCPS
PVPPLYLDDD GLPFPTDVIQ HRLRQIEAVY KQEVEQLRRQ VRELQMRLDI RHCCAPPAEP
PMDYEDDFTC LKESDGSDTE DFGSDHSEDC LSEASWEPVD KKETEVTRWV PDHMASHCYN
CDCEFWLAKR RHHCRLEGRI CFWYSFEGSL VWLMKSEFKD TILRNPWYHE TGAEEFQFDR
RSSTTGPVAV GQFHRSFRRD SLSPYSYVST SSHNHSTFPL KGLDRTPIPP RTWQNSLGMH
PGQVETSPTF SDKGVPFPVL QRFPTEVTYT LQPSATSVHV QQGPQTMVNS SQKYSNYTPS
AQYSQAYYPT AVLQCCSPST HMDALSSCVT PTASTYAHCN YFQNPPMPSS YPVEFLPSNW
PCGTTDENKK TEVNLEAVFR ILDELHSSPK LEMVKVEPVE NQCPTSQSNR GQHILANSSN
NNPSSTSQAS QLEPLTPVGS DITSFVVGTE QAITCSLPQS PEYMYTIHTA QPVENTTMQE
SAAIQQAHVK LKEHLSHNPS PPSVVFVQEG LPFSPHQVDA SIKCQTNPPE NILPSEQMGF
LISEMGPASK PSKDTDLSTP VRYRERRSSS QQGKSPDYDL ETFVNKAEPA LAQQAKHFSA
LQLEEQASKQ IGSKKWPQW
//
