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Protein

Lipid phosphate phosphatase 1

Gene

LPP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation of diacylglycerol phosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with DPP1, regulates intracellular DGPP and PA levels which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) as a substrate. Substrate preference is PA > DGPP > LPA.2 Publications

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.1 Publication
Diacylglycerol pyrophosphate + H2O = phosphatidate + phosphate.1 Publication

Enzyme regulationi

PA phosphatase activity is magnesium ion-independent and potently inhibited by N-ethylmaleimide. Also inhibited by phenylglyoxal and propranolol.1 Publication

GO - Molecular functioni

  • phosphatidate phosphatase activity Source: SGD

GO - Biological processi

  • dephosphorylation Source: GOC
  • phospholipid metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15446.
YEAST:YDR503C-MONOMER.

Chemistry

SwissLipidsiSLP:000000058.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid phosphate phosphatase 1 (EC:3.1.3.-)
Alternative name(s):
Phosphatidate phosphatase (EC:3.1.3.4)
Gene namesi
Name:LPP1
Ordered Locus Names:YDR503C
ORF Names:D9719.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR503C.
SGDiS000002911. LPP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515LumenalSequence analysisAdd
BLAST
Transmembranei16 – 3318Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini34 – 6936CytoplasmicSequence analysisAdd
BLAST
Transmembranei70 – 8718Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini88 – 11730LumenalSequence analysisAdd
BLAST
Transmembranei118 – 13922Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini140 – 18950CytoplasmicSequence analysisAdd
BLAST
Transmembranei190 – 20314Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini204 – 21411LumenalSequence analysisAdd
BLAST
Transmembranei215 – 23117Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini232 – 2376CytoplasmicSequence analysis
Transmembranei238 – 25518Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini256 – 27419LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Lipid phosphate phosphatase 1PRO_0000220919Add
BLAST

Proteomic databases

MaxQBiQ04396.

Interactioni

Protein-protein interaction databases

BioGridi32554. 32 interactions.
DIPiDIP-1415N.
IntActiQ04396. 5 interactions.
MINTiMINT-400466.

Structurei

3D structure databases

ProteinModelPortaliQ04396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 1449Phosphatase sequence motif I
Regioni186 – 1894Phosphatase sequence motif II
Regioni228 – 23912Phosphatase sequence motif IIIAdd
BLAST

Domaini

The phosphatase sequence motif I (including Arg-143) and II (including His-189) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-235) is part of the cytoplasmic loop 3.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000057102.
InParanoidiQ04396.
OMAiDHRHHWY.
OrthoDBiEOG7QNVXN.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q04396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISVMADEKH KEYFKLYYFQ YMIIGLCTIL FLYSEISLVP RGQNIEFSLD
60 70 80 90 100
DPSISKRYVP NELVGPLECL ILSVGLSNMV VFWTCMFDKD LLKKNRVKRL
110 120 130 140 150
RERPDGISND FHFMHTSILC LMLIISINAA LTGALKLIIG NLRPDFVDRC
160 170 180 190 200
IPDLQKMSDS DSLVFGLDIC KQTNKWILYE GLKSTPSGHS SFIVSTMGFT
210 220 230 240 250
YLWQRVFTTR NTRSCIWCPL LALVVMVSRV IDHRHHWYDV VSGAVLAFLV
260 270
IYCCWKWTFT NLAKRDILPS PVSV
Length:274
Mass (Da):31,586
Last modified:November 1, 1996 - v1
Checksum:i2311DB0BC841D2DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64945.1.
AY693191 Genomic DNA. Translation: AAT93210.1.
BK006938 Genomic DNA. Translation: DAA12335.1.
PIRiS69561.
RefSeqiNP_010791.3. NM_001180811.3.

Genome annotation databases

EnsemblFungiiYDR503C; YDR503C; YDR503C.
GeneIDi852114.
KEGGisce:YDR503C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64945.1.
AY693191 Genomic DNA. Translation: AAT93210.1.
BK006938 Genomic DNA. Translation: DAA12335.1.
PIRiS69561.
RefSeqiNP_010791.3. NM_001180811.3.

3D structure databases

ProteinModelPortaliQ04396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32554. 32 interactions.
DIPiDIP-1415N.
IntActiQ04396. 5 interactions.
MINTiMINT-400466.

Chemistry

SwissLipidsiSLP:000000058.

Proteomic databases

MaxQBiQ04396.

Protocols and materials databases

DNASUi852114.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR503C; YDR503C; YDR503C.
GeneIDi852114.
KEGGisce:YDR503C.

Organism-specific databases

EuPathDBiFungiDB:YDR503C.
SGDiS000002911. LPP1.

Phylogenomic databases

HOGENOMiHOG000057102.
InParanoidiQ04396.
OMAiDHRHHWY.
OrthoDBiEOG7QNVXN.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15446.
YEAST:YDR503C-MONOMER.

Miscellaneous databases

NextBioi970484.
PROiQ04396.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Isolation and characterization of the Saccharomyces cerevisiae LPP1 gene encoding a Mg2+-independent phosphatidate phosphatase."
    Toke D.A., Bennett W.L., Oshiro J., Wu W.I., Voelker D.R., Carman G.M.
    J. Biol. Chem. 273:14331-14338(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  5. "Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae."
    Furneisen J.M., Carman G.M.
    Biochim. Biophys. Acta 1484:71-82(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  6. "Transmembrane topology of sphingoid long-chain base-1-phosphate phosphatase, Lcb3p."
    Kihara A., Sano T., Iwaki S., Igarashi Y.
    Genes Cells 8:525-535(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLPP1_YEAST
AccessioniPrimary (citable) accession number: Q04396
Secondary accession number(s): D6VTC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.