PTEN_SCHPO
ID PTEN_SCHPO Reviewed; 348 AA.
AC O94526;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1;
DE EC=3.1.3.67 {ECO:0000269|PubMed:15249580};
GN Name=ptn1; ORFNames=SPBC609.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=15249580; DOI=10.1083/jcb.200404150;
RA Mitra P., Zhang Y., Rameh L.E., Ivshina M.P., McCollum D., Nunnari J.J.,
RA Hendricks G.M., Kerr M.L., Field S.J., Cantley L.C., Ross A.H.;
RT "A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast.";
RL J. Cell Biol. 166:205-211(2004).
CC -!- FUNCTION: Acts as a phosphoinositide 3-phosphatase and regulates
CC PtdIns(3,4,5)P3 levels. {ECO:0000269|PubMed:15249580}.
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:0000269|PubMed:15249580};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-
CC (1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420,
CC ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15249580}.
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DR EMBL; CU329671; CAA22831.1; -; Genomic_DNA.
DR PIR; T40573; T40573.
DR RefSeq; NP_596312.1; NM_001022234.2.
DR AlphaFoldDB; O94526; -.
DR SMR; O94526; -.
DR BioGRID; 277616; 30.
DR STRING; 4896.SPBC609.02.1; -.
DR PaxDb; O94526; -.
DR EnsemblFungi; SPBC609.02.1; SPBC609.02.1:pep; SPBC609.02.
DR GeneID; 2541101; -.
DR KEGG; spo:SPBC609.02; -.
DR PomBase; SPBC609.02; ptn1.
DR VEuPathDB; FungiDB:SPBC609.02; -.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_020105_4_1_1; -.
DR InParanoid; O94526; -.
DR OMA; FWFHTQL; -.
DR PhylomeDB; O94526; -.
DR Reactome; R-SPO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SPO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-SPO-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-SPO-202424; Downstream TCR signaling.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-8948747; Regulation of PTEN localization.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:O94526; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005770; C:late endosome; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IDA:PomBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; EXP:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..348
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase ptn1"
FT /id="PRO_0000353823"
FT DOMAIN 18..189
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT ACT_SITE 129
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
SQ SEQUENCE 348 AA; 40157 MW; ABF91D58CB93C492 CRC64;
MNILRSVVSR GRKGLKQEKV NRSFAYLDMV YITSKVIAMS TPAAGIHKLY RNDELDVFKY
LTTQLKDNWI LLNLCAEETV YHLELFKPNV INYGFQDHNP PPLLFLWAIV MNMDALFQTQ
PLLTLVVHCK AGKGRTGTVI CSYLVAFGGL TAKQSLELYT EKRMVRGHGL TISSQIRYVY
YIEILKQFPN YLKAVEFNTG TTFFKSFKCL NIKKNSSLIL SLHAFSKGRN INPVALWKSS
DISSHNVSIK EGKRIWGIQC NLETSEKDLL LRVERKGQFY FPSSVQCWFH THFQPMLVEY
TNGINFQQGI NSFLQGQQSI SFSWSEMDNS RRSDPFFEQL TIVYENVF
