LPP1_YEAST
ID LPP1_YEAST Reviewed; 274 AA.
AC Q04396; D6VTC5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Lipid phosphate phosphatase 1;
DE EC=3.1.3.81 {ECO:0000269|PubMed:9603941};
DE AltName: Full=Lysophosphatidate phosphatase;
DE EC=3.1.3.106;
DE AltName: Full=Phosphatidate phosphatase {ECO:0000303|PubMed:9603941};
DE EC=3.1.3.4 {ECO:0000269|PubMed:9603941};
GN Name=LPP1; OrderedLocusNames=YDR503C; ORFNames=D9719.9;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9603941; DOI=10.1074/jbc.273.23.14331;
RA Toke D.A., Bennett W.L., Oshiro J., Wu W.I., Voelker D.R., Carman G.M.;
RT "Isolation and characterization of the Saccharomyces cerevisiae LPP1 gene
RT encoding a Mg2+-independent phosphatidate phosphatase.";
RL J. Biol. Chem. 273:14331-14338(1998).
RN [5]
RP FUNCTION.
RX PubMed=10329682; DOI=10.1074/jbc.274.21.14831;
RA Faulkner A., Chen X., Rush J., Horazdovsky B., Waechter C.J., Carman G.M.,
RA Sternweis P.C.;
RT "The LPP1 and DPP1 gene products account for most of the isoprenoid
RT phosphate phosphatase activities in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:14831-14837(1999).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10685032; DOI=10.1016/s1388-1981(99)00202-4;
RA Furneisen J.M., Carman G.M.;
RT "Enzymological properties of the LPP1-encoded lipid phosphatase from
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1484:71-82(2000).
RN [7]
RP TOPOLOGY.
RX PubMed=12786943; DOI=10.1046/j.1365-2443.2003.00653.x;
RA Kihara A., Sano T., Iwaki S., Igarashi Y.;
RT "Transmembrane topology of sphingoid long-chain base-1-phosphate
RT phosphatase, Lcb3p.";
RL Genes Cells 8:525-535(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate
CC (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA
CC to diacylglycerol (DAG). Together with DPP1, regulates intracellular
CC DGPP and PA levels which are phospholipid molecules believed to play a
CC signaling role in stress response. Can also use lysophosphatidic acid
CC (LPA) as a substrate. Substrate preference is PA > DGPP > LPA.
CC {ECO:0000269|PubMed:10329682, ECO:0000269|PubMed:10685032,
CC ECO:0000269|PubMed:9603941}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC Evidence={ECO:0000269|PubMed:10685032, ECO:0000269|PubMed:9603941};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC Evidence={ECO:0000305|PubMed:10685032, ECO:0000305|PubMed:9603941};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000269|PubMed:10685032, ECO:0000269|PubMed:9603941};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:10685032, ECO:0000305|PubMed:9603941};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC EC=3.1.3.106; Evidence={ECO:0000269|PubMed:10685032,
CC ECO:0000269|PubMed:9603941};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC Evidence={ECO:0000305|PubMed:10685032, ECO:0000305|PubMed:9603941};
CC -!- ACTIVITY REGULATION: PA phosphatase activity is magnesium ion-
CC independent and potently inhibited by N-ethylmaleimide. Also inhibited
CC by phenylglyoxal and propranolol. {ECO:0000269|PubMed:10685032}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The phosphatase sequence motif I (including Arg-143) and II
CC (including His-189) are part of the cytoplasmic loop 2 and phosphatase
CC sequence motif III (including His-235) is part of the cytoplasmic loop
CC 3.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; U33057; AAB64945.1; -; Genomic_DNA.
DR EMBL; AY693191; AAT93210.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12335.1; -; Genomic_DNA.
DR PIR; S69561; S69561.
DR RefSeq; NP_010791.3; NM_001180811.3.
DR AlphaFoldDB; Q04396; -.
DR BioGRID; 32554; 75.
DR DIP; DIP-1415N; -.
DR IntAct; Q04396; 6.
DR MINT; Q04396; -.
DR STRING; 4932.YDR503C; -.
DR SwissLipids; SLP:000000058; -.
DR MaxQB; Q04396; -.
DR PaxDb; Q04396; -.
DR PRIDE; Q04396; -.
DR DNASU; 852114; -.
DR EnsemblFungi; YDR503C_mRNA; YDR503C; YDR503C.
DR GeneID; 852114; -.
DR KEGG; sce:YDR503C; -.
DR SGD; S000002911; LPP1.
DR VEuPathDB; FungiDB:YDR503C; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_4_0_1; -.
DR InParanoid; Q04396; -.
DR OMA; YGLDICQ; -.
DR BioCyc; MetaCyc:YDR503C-MON; -.
DR BioCyc; YEAST:YDR503C-MON; -.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SCE-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q04396; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04396; protein.
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:0016020; C:membrane; IDA:SGD.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:SGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..274
FT /note="Lipid phosphate phosphatase 1"
FT /id="PRO_0000220919"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..117
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..214
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..274
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 136..144
FT /note="Phosphatase sequence motif I"
FT REGION 186..189
FT /note="Phosphatase sequence motif II"
FT REGION 228..239
FT /note="Phosphatase sequence motif III"
SQ SEQUENCE 274 AA; 31586 MW; 2311DB0BC841D2DA CRC64;
MISVMADEKH KEYFKLYYFQ YMIIGLCTIL FLYSEISLVP RGQNIEFSLD DPSISKRYVP
NELVGPLECL ILSVGLSNMV VFWTCMFDKD LLKKNRVKRL RERPDGISND FHFMHTSILC
LMLIISINAA LTGALKLIIG NLRPDFVDRC IPDLQKMSDS DSLVFGLDIC KQTNKWILYE
GLKSTPSGHS SFIVSTMGFT YLWQRVFTTR NTRSCIWCPL LALVVMVSRV IDHRHHWYDV
VSGAVLAFLV IYCCWKWTFT NLAKRDILPS PVSV
