ID   TPTE2_MACFA             Reviewed;         566 AA.
AC   Q4R6N0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2;
DE            EC=3.1.3.67 {ECO:0000250|UniProtKB:Q6XPS3};
GN   Name=TPTE2; ORFNames=QtsA-17567;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a lipid phosphatase, removing the phosphate in the D3
CC       position of the inositol ring from phosphatidylinositol 3,4,5-
CC       trisphosphate. {ECO:0000250|UniProtKB:Q6XPS3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC         trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC         ChEBI:CHEBI:58456; EC=3.1.3.67;
CC         Evidence={ECO:0000250|UniProtKB:Q6XPS3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25018;
CC         Evidence={ECO:0000250|UniProtKB:Q6XPS3};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6XPS3}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6XPS3};
CC       Multi-pass membrane protein {ECO:0000255}.
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DR   EMBL; AB169152; BAE01245.1; -; mRNA.
DR   AlphaFoldDB; Q4R6N0; -.
DR   SMR; Q4R6N0; -.
DR   PRIDE; Q4R6N0; -.
DR   Ensembl; ENSMFAT00000031690; ENSMFAP00000023555; ENSMFAG00000043402.
DR   GeneTree; ENSGT00940000154335; -.
DR   Proteomes; UP000233100; Chromosome 17.
DR   Bgee; ENSMFAG00000043402; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd14510; PTP_VSP_TPTE; 1.
DR   Gene3D; 1.20.120.350; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR045102; PTP_VSP_TPTE.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Golgi apparatus; Hydrolase; Lipid metabolism;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..566
FT                   /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT                   phosphatase TPTE2"
FT                   /id="PRO_0000224188"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          272..448
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT   DOMAIN          455..566
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT   ACT_SITE        382
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
SQ   SEQUENCE   566 AA;  65234 MW;  ADD94DEBBA51F5AB CRC64;
     MCRVMKASFS RKVKLELCLL SDCALLSSSS APTNELSGTN LEAHINESPD PNALVGVIIE
     RSPSDSTQTN EFKGATKETL TIETPHSSEC KGAGLLSPVS KSMLERLSKF EVEDAENVAS
     YDTKIKKIVR SIVSSFAFGI FGVFLVLLDV TLLLADLIFN DSKLYIPLVY RSISLAIALF
     FLMDVLLRVF VEGRQHYFSD LLNVLDTAII VTPLLVDVVY IFFDIKFLRN IPRWIHLVRL
     LRLIILIRIF HLIHQKRELE KLMRRLVSEN KRRYTRDGFD LDLTYVTERI IAMSFPSSGR
     QSFYRNPIEE VVRFLDKKHP NHYRVYNLCS ERAYDPKYFH NRVSRIMIDD HNVPTLHEMV
     VFTKEVNEWM AQDPANIVAI HCKGGKGRTG TMICAFLIAS EIFLTAEESL YYFGERRTDK
     TNSSKFQGVE TPSQNRYVGY FAQVKHLYNW NLPPRRILFI KRFIIYSIRG VGTGGVCDLK
     VRIVMEKKVV FSSTSLGNCS ILHDIETDRV LIDVFSGPPL YDDVKVQFFS SNLPKYYDNC
     PFFFWFNTSF IQSNRHILHS FRLVFT