Reviewed, UniProtKB/Swiss-Prot O08564 (LPP1_RAT)

Names and origin

Protein names

Recommended name:
    Lipid phosphate phosphohydrolase 1
    EC=3.1.3.4
Alternative name(s):
    Phosphatidic acid phosphatase 2a
    PAP2-alpha
      Short name=PAP-2a
      Short name=PAP2a
    Phosphatidate phosphohydrolase type 2a

Gene names

Name:	Ppap2a
Synonyms:	Lpp1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), diacyl glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > C-1-P > S-1-P.
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatidate phosphatase activity Ref.2 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O08564-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O08564-2)

Also known as: LPP1a;

The sequence of this isoform differs from the canonical sequence as follows:
     21-70: GLPFIILTSR...GIVIPFCIIV → SMPMAVVNLG...LVGLGIPIFS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 282	282	Lipid phosphate phosphohydrolase 1		PRO_0000220908
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Potential
	Topological domain	28 – 53	26	Extracellular Potential
	Transmembrane	54 – 74	21	Potential
	Topological domain	75 – 88	14	Cytoplasmic Potential
	Transmembrane	89 – 109	21	Potential
	Topological domain	110 – 164	55	Extracellular Potential
	Transmembrane	165 – 185	21	Potential
	Topological domain	186 – 194	9	Cytoplasmic Potential
	Transmembrane	195 – 215	21	Potential
	Topological domain	216 – 229	14	Extracellular Potential
	Transmembrane	230 – 250	21	Potential
	Topological domain	251 – 282	32	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	142	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	21 – 70	50	GLPFI…FCIIV → SMPMAVVNLGQIYPFQRGFF CSDNSVKYPYHDSTVTTSVL VLVGLGIPIFS in isoform 2.		VSP_009653

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: A4ED3DEB33FD7943	FASTA	282	31,996
	10 20 30 40 50 60 MFDKPRLPYV VLDVICVLLA GLPFIILTSR HTPFQRGVFC TDESIKYPYR EDTIPYALLG 70 80 90 100 110 120 GIVIPFCIIV MITGETLSVY FNVLHSNSFV SNHYIATIYK AVGAFLFGAS ASQSLTDIAK 130 140 150 160 170 180 YSIGRLRPHF LAVCNPDWSK INCSDGYIEN FVCQGNEQKV REGRLSFYSG HSSFSMYCML 190 200 210 220 230 240 FVALYLQARM KGDWARLLRP MLQFGLVALS IYVGLSRVSD YKHHWSDVLI GLIQGAVVAI 250 260 270 280 LVVLYVTDFF KTTESNKERK EDSHTTLHET TNRQSYARNH EP
	Isoform 2 (LPP1a). Checksum: 3D2B45015891C873	FASTA	283	31,922
	10 20 30 40 50 60 MFDKPRLPYV VLDVICVLLA SMPMAVVNLG QIYPFQRGFF CSDNSVKYPY HDSTVTTSVL 70 80 90 100 110 120 VLVGLGIPIF SMITGETLSV YFNVLHSNSF VSNHYIATIY KAVGAFLFGA SASQSLTDIA 130 140 150 160 170 180 KYSIGRLRPH FLAVCNPDWS KINCSDGYIE NFVCQGNEQK VREGRLSFYS GHSSFSMYCM 190 200 210 220 230 240 LFVALYLQAR MKGDWARLLR PMLQFGLVAL SIYVGLSRVS DYKHHWSDVL IGLIQGAVVA 250 260 270 280 ILVVLYVTDF FKTTESNKER KEDSHTTLHE TTNRQSYARN HEP

References

[1]	"Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters." Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J., Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W., Brindley D.N. Biochem. J. 340:677-686(1999) [PubMed: 10359651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Liver.
[2]	"Molecular cloning and expression of pulmonary lipid phosphate phosphohydrolases." Nanjundan M., Possmayer F. Am. J. Physiol. 281:L1484-L1493(2001) [PubMed: 11704545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: Sprague-Dawley. Tissue: Lung.
[3]	"Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate." Waggoner D.W., Gomez-Munoz A., Dewald J., Brindley D.N. J. Biol. Chem. 271:16506-16509(1996) [PubMed: 8663293] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U90556 mRNA. Translation: AAB50246.1. AF503609 mRNA. Translation: AAM28631.1.
IPI	IPI00193763. IPI00203765.
UniGene	Rn.61687
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	O08564.
Organism-specific databases
RGD	621832. Ppap2a.
Phylogenomic databases
HOVERGEN	O08564.
Enzyme and pathway databases
BRENDA	3.1.3.4. 248.
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...

Entry information

Entry name

LPP1_RAT

Accession

Primary (citable) accession number: O08564
Secondary accession number(s): Q8K594

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)