ID L5JQT8_PTEAL Unreviewed; 1644 AA.
AC L5JQT8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=PAL_GLEAN10019787 {ECO:0000313|EMBL:ELK01720.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01720.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(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 TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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; KB031150; ELK01720.1; -; Genomic_DNA.
DR STRING; 9402.L5JQT8; -.
DR eggNOG; KOG4471; Eukaryota.
DR InParanoid; L5JQT8; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; cd01850; CDC_Septin; 1.
DR CDD; cd15733; FYVE_MTMR4; 1.
DR CDD; cd13342; PH-GRAM_MTMR4; 1.
DR CDD; cd14587; PTP-MTMR4; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016491; Septin.
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 Pfam; PF00735; Septin; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51719; G_SEPTIN; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW GTP-binding {ECO:0000256|RuleBase:RU004560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 132..405
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT DOMAIN 602..1019
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 825..869
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1563..1623
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 27..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 856
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 769..772
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 794..795
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 856..862
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1644 AA; 185153 MW; A38EE6D776EC688F CRC64;
MVRRLGPPSH NPIKRFLEDT DDTELNKFVK DFPGNESYHQ PEAKTRVSRP QVSEPRPQAP
DLNEDDLEFR TPSWPQPSDS QQYCSASAPL SPSARPRSPW GKLDPYDSSE DDKEYVGFAT
LPNQVHRKSV KKGFDFTLMV AGESGLGKST LVNSLFLTDL YRDRKLLSAE ERIMQTVEIT
KHAVDIEEKG VRLRLTIVDT PGFGDAVNNT ECWKPVAEYI DQQFEQYFRD ESGLNRKNIQ
DNRVHCCLYF ISPFGHGLRP LDVEFMKALH QRVNIVPILA KADTLTPLEV ERKKRKIREE
IELFGIKVYQ FPDCDSDEDE DFKLQDQALK ESIPFAVIGS NTVVEARGRR VRGRLYPWGI
VEVENPGHCD FVKLRTMLVR THMQDLKDVT RETHYENYRA QCIQSMTRLV VKERNRNKLT
RESGTDFPIP AVPAGTDPET ERLIREKDEE GEEGPPSLEY IQAKDLFPPK ELVKEEENLQ
VPFTVLQGEG VEFLGRAADA LIAISNYRLH IKFKDSVINV PLRMIDSVES RDMFQLHIAC
KDSKVVRCHF STFKQCQEWL SRLSRATARP AKPEDLFAFA YHAWCLGLTE EDQHTHLCQP
GEHIRCRQEA ELARMGFDLQ NVWRVSHINS NYKLCPSYPQ KLLVPVWITD KELENVASFR
SWKRIPVVVY RHLRNGAAIA RCSQPEISWW GWRNADDEYL VTSIAKACAL DPGTRATGGS
LSTGNSDSSE ACDTDFDSSL TACSGVESTA APQKLLILDA RSYTAAVANR AKGGGCECEE
YYPNCEVVFM GMANIHAIRN SFQYLRAVCS QMPDPSNWLS ALESTKWLQH LSVMLKAAVL
VANTVDREGR PVLVHCSDGW DRTPQIVALA KILLDPYYRT LEGFQVLVES DWLDFGHKFG
DRCGHQENAE DQNEQCPVFL QWLDSVHQLL KQFPCLFEFN EAFLVKLVQH TYSCLYGTFL
ANNPCEREKR NIYKRTCSVW ALLRAGNKNF HNFLYTPGSD MVLHPVCHVR ALHLWTAVYL
PASSPCTLGE ENMDLYLSPV AQSQEFSGRS LDRLPKTRSM DDLLSACDTS SPLTRTSSDP
NLNNHCQEAR VGLEPWHSNP EGSETAFVES GVEGPQQTVG EMGLPPPLSS SQKDYLSNKP
FKSHKSCSPS YKPLNATVPQ EMKSHTSDPE IKVLEETKVP ASDLPAQDEL GRTLDGTEEP
PEHFPEKAAV SVLSNVISNK CDGICDFSES SQEPPTGAPK QAQLDSGLGV SSRSAPSHSL
GTLCNPPSAT CHTPPDPTAD FLNQDPPGSV ASISHQEQPS SVPDLIHGEE DTGKRGNNRN
GQLLENLRFG KVPLELARRP ISQSQISEFS FIGSNWDSFQ GMVTSFPSGE TTPRRLLSYG
CCSKRSNSKQ MRATGPCFGQ WAQREGVKSP LCSSHSNGHC TGPGGKNNRI WVSSYPKQVS
STKPVPLSCP SPVPPLYLDD DGLPFPTDVI QHRLRQIEAG YKQEVEQLRR QVRELQMRLD
IRHCCAPPQE PPMDYEDDFT CLKESDGSDT EDFGSDHSED CLSEASWEPV DKKETEVTRW
VPDHMASHCY NCDCEFWLAK RRHHCRNCGN VFCAACCHLK LPIPDQQLYD PVLVCNSCYE
HIQVSRAREL MSQHLKKPIA TASS
//
