Reviewed, UniProtKB/Swiss-Prot Q04396 (LPP1_YEAST)

Names and origin

Protein names

Recommended name:
    Lipid phosphate phosphatase 1
    EC=3.1.3.-
Alternative name(s):
    Phosphatidate phosphatase
    EC=3.1.3.4

Gene names

Name:	LPP1
Ordered Locus Names:	YDR503C
ORF Names:	D9719.9

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.3 Ref.4
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate. Ref.3 Diacylglycerol pyrophosphate + H2O = phosphatidate + phosphate. Ref.3
Enzyme regulation	PA phosphatase activity is magnesium ion-independent and potently inhibited by N-ethylmaleimide. Also inhibited by phenylglyoxal and propranolol. Ref.4
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein. Ref.6
Domain	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.
Miscellaneous	Present with 300 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct phosphatidate phosphatase activity Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-35436,EBI-35436
	P25361	1	EBI-35436,EBI-21909
RBD2	Q12270	1	EBI-35436,EBI-31471
SAC1	P32368	1	EBI-35436,EBI-16210
VRG4	P40107	1	EBI-35436,EBI-7764

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 274	274	Lipid phosphate phosphatase 1		PRO_0000220919
Regions
	Topological domain	1 – 15	15	Lumenal Potential
	Transmembrane	16 – 33	18	1 Potential
	Topological domain	34 – 69	36	Cytoplasmic Potential
	Transmembrane	70 – 87	18	2 Potential
	Topological domain	88 – 117	30	Lumenal Potential
	Transmembrane	118 – 139	22	3 Potential
	Topological domain	140 – 189	50	Cytoplasmic Potential
	Transmembrane	190 – 203	14	4 Potential
	Topological domain	204 – 214	11	Lumenal Potential
	Transmembrane	215 – 231	17	5 Potential
	Topological domain	232 – 237	6	Cytoplasmic Potential
	Transmembrane	238 – 255	18	6 Potential
	Topological domain	256 – 274	19	Lumenal Potential
	Region	136 – 144	9	Phosphatase sequence motif I
	Region	186 – 189	4	Phosphatase sequence motif II
	Region	228 – 239	12	Phosphatase sequence motif III

Sequences

	Sequence		Length	Mass (Da)
	Q04396-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 2311DB0BC841D2DA	FASTA	274	31,586
	10 20 30 40 50 60 MISVMADEKH KEYFKLYYFQ YMIIGLCTIL FLYSEISLVP RGQNIEFSLD DPSISKRYVP 70 80 90 100 110 120 NELVGPLECL ILSVGLSNMV VFWTCMFDKD LLKKNRVKRL RERPDGISND FHFMHTSILC 130 140 150 160 170 180 LMLIISINAA LTGALKLIIG NLRPDFVDRC IPDLQKMSDS DSLVFGLDIC KQTNKWILYE 190 200 210 220 230 240 GLKSTPSGHS SFIVSTMGFT YLWQRVFTTR NTRSCIWCPL LALVVMVSRV IDHRHHWYDV 250 260 270 VSGAVLAFLV IYCCWKWTFT NLAKRDILPS PVSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 9603941] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[4]	"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: 10685032] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[5]	"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: 12786943] [Abstract] Cited for: TOPOLOGY.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U33057 Genomic DNA. Translation: AAB64945.1. AY693191 Genomic DNA. Translation: AAT93210.1.
PIR	S69561.
RefSeq	NP_010791.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1415N.
IntAct	Q04396. 14 interactions.
Genome annotation databases
Ensembl	YDR503C. Saccharomyces cerevisiae. [Contig view]
GeneID	852114.
GenomeReviews	Gene locus YDR503C in contig Z71256_GR.
KEGG	sce:YDR503C.
NMPDR	fig|4932.3.peg.1564.
Organism-specific databases
CYGD	YDR503c.
SGD	S000002911. LPP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q04396.
OMA	Q04396. DHRHHWY.
Enzyme and pathway databases
BRENDA	3.1.3.4. 250.
Gene expression databases
GermOnline	YDR503C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970484.

Entry information

Entry name

LPP1_YEAST

Accession

Primary (citable) accession number: Q04396

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)