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Database: UniProt
Entry: A0A0M0JET4_9EUKA
LinkDB: A0A0M0JET4_9EUKA
Original site: A0A0M0JET4_9EUKA 
ID   A0A0M0JET4_9EUKA        Unreviewed;       771 AA.
AC   A0A0M0JET4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   SubName: Full=Phosphatidylinositol-trisphosphate 3-phosphatase TPTe2-like protein {ECO:0000313|EMBL:KOO24753.1};
GN   ORFNames=Ctob_003434 {ECO:0000313|EMBL:KOO24753.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO24753.1, ECO:0000313|Proteomes:UP000037460};
RN   [1] {ECO:0000313|Proteomes:UP000037460}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX   PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA   Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA   Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA   Cattolico R.A.;
RT   "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT   Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT   Prymnesiales (Haptophyceae).";
RL   PLoS Genet. 11:e1005469-e1005469(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOO24753.1}.
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DR   EMBL; JWZX01003057; KOO24753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JET4; -.
DR   OrthoDB; 5477362at2759; -.
DR   Proteomes; UP000037460; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR   PANTHER; PTHR12305:SF60; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE TPTE2-RELATED; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..429
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          340..408
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          433..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  84175 MW;  61F0813B9C28153E CRC64;
     MPEVSIQIVE SRAPAPLKRF QEAGKSVMHS SSLTVVLPVS VLEDAQWPAM GPFDGRTQPP
     KDEDEEAQLE ELRRKRQEKL EAVQALGGHA AGKRMTGRQR ARWMIEGWKW QLFLLVVAII
     DIAMLFVELN AGPGAMIPVA VVTFVVLFIF VVDLIIRYYA FRNKLFSSFW FWFDFFVVAF
     SIVLFLIGLG FGSTDAEVGQ SGSTAARGGK ALRGMIVALR WLRAARLVIK LTQVKGGAST
     AARHATGENK KRYVDLEHGF DLDLAYVLPD LIAMSVPAIG WTALYRNPLP EVARFLELRH
     GKGGYTIINC CPELPYPPDK FKSGEVVRFD IQDHTPPNML QFVSFLNSMR HKPASHTLAI
     HCRGGKGRTG SMCCAWLLYS RACLDADDAL THFALERTEL SLGKKKIQGV DTPSQRRYVH
     QLDALLRAQS AYLTEPTRRR RAPASTSDAQ GEESATSLRE ESSSSSSSCW SPDGTDGSCR
     SPNGRPAGSL VRPPACPTAS MRSLDLVNWY AKAPKGALVC AVHRNGGEGE DRGKVVHWSP
     PVRDFSTAGS LISFDLAGVD VDGDVRVSVF ALDDLLKVRR KRLKKGLAAR LPFDAAPTGP
     WEDTADTPET AMRQKKSKKD DKRVIAGKES GCKFFLLFHT GFVSSTGEMP VPLKMMDKAF
     KNKGKKYRPE GVATLRFELL EKASIKPTLG AAVDQAVGAH EAELSADPSA DSSTSSATRN
     QGALARARKA SGASSSVETS AMPETTRPTG ESTALAEMMA AAEGDRSDDQ I
//
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