TEP1_YEAST
ID TEP1_YEAST Reviewed; 434 AA.
AC P53916; D6W155;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Probable phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TEP1;
DE EC=3.1.3.67;
GN Name=TEP1; OrderedLocusNames=YNL128W; ORFNames=N1220, N1872;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=11070083; DOI=10.1073/pnas.97.23.12672;
RA Heymont J., Berenfeld L., Collins J., Kaganovich A., Maynes B., Moulin A.,
RA Ratskovskaya I., Poon P.P., Johnston G.C., Kamenetsky M., DeSilva J.,
RA Sun H., Petsko G.A., Engebrecht J.;
RT "TEP1, the yeast homolog of the human tumor suppressor gene
RT PTEN/MMAC1/TEP1, is linked to the phosphatidylinositol pathway and plays a
RT role in the developmental process of sporulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12672-12677(2000).
CC -!- FUNCTION: May act as a phosphoinositide 3-phosphatase by regulating
CC PtdIns(3,4,5)P3 levels. {ECO:0000269|PubMed:11070083}.
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;
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DR EMBL; Z46843; CAA86897.1; -; Genomic_DNA.
DR EMBL; Z71404; CAA96010.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10421.1; -; Genomic_DNA.
DR PIR; S55155; S55155.
DR RefSeq; NP_014271.3; NM_001182966.4.
DR AlphaFoldDB; P53916; -.
DR SMR; P53916; -.
DR BioGRID; 35699; 120.
DR DIP; DIP-4928N; -.
DR IntAct; P53916; 12.
DR MINT; P53916; -.
DR STRING; 4932.YNL128W; -.
DR iPTMnet; P53916; -.
DR PaxDb; P53916; -.
DR PRIDE; P53916; -.
DR EnsemblFungi; YNL128W_mRNA; YNL128W; YNL128W.
DR GeneID; 855595; -.
DR KEGG; sce:YNL128W; -.
DR SGD; S000005072; TEP1.
DR VEuPathDB; FungiDB:YNL128W; -.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000154335; -.
DR HOGENOM; CLU_020105_0_0_1; -.
DR InParanoid; P53916; -.
DR OMA; CWLNLYW; -.
DR BioCyc; YEAST:G3O-33149-MON; -.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-SCE-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-SCE-202424; Downstream TCR signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-8948747; Regulation of PTEN localization.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P53916; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53916; protein.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
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: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; IPR000340; Dual-sp_phosphatase_cat-dom.
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 Pfam; PF00782; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 4: Predicted;
KW Hydrolase; Reference proteome.
FT CHAIN 1..434
FT /note="Probable phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase TEP1"
FT /id="PRO_0000215906"
FT DOMAIN 33..255
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT ACT_SITE 193
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
SQ SEQUENCE 434 AA; 50152 MW; E56739475D1FA898 CRC64;
MREEGSELEM EKGFLKWKPV NLMKKILSLP MKKTKNDIGL RLDISYILVN LIVCSYPVNT
YPKLLYRNSL DDLILFLTVY HGKGNFRIFN FRGEKEDSDY KDNDLIGIAA KFESKDFEIQ
ELRSTLINDG KIPISPIDLE TRTLVEEETN NVICERIGWL DHFPPPFELL EEIVDGIENY
LSVSKNRVAV LHCRMGKGRS GMITVAYLMK YLQCPLGEAR LIFMQARFKY GMTNGVTIPS
QLRYLRYHEF FITHEKAAQE GISNEAVKFK FKFRLAKMTF LRPSSLITSE SAIVTTKIQH
YNDDRNALLT RKVVYSDIMA HECGGNMTFI FGRDYLTLEN DCRIEFTLGT SKSKAASSII
SWTSCASCWL NIYLETLMHI IKDDSSPDYF QVERLKRDEM LGTTISWQEL DGFGELSTHG
LKLFQALKLE WEII
