Reviewed, UniProtKB/Swiss-Prot P97544 (LPP3_RAT)

Names and origin

Protein names

Recommended name:
    Lipid phosphate phosphohydrolase 3
    EC=3.1.3.4
Alternative name(s):
    Phosphatidic acid phosphatase 2b
    PAP2-beta
      Short name=PAP-2b
      Short name=PAP2b
    Phosphatidate phosphohydrolase type 2b
    Differentially expressed in rat intestine 42
      Short name=Dri42

Gene names

Name:	Ppap2b
Synonyms:	Lpp3

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

General annotation (Comments)

Function	Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P) By similarity. Involved in the regulation of epithelial differentiation.
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Detected in epithelial cells of intestinal mucosa, lung, liver and brain. Ref.2 Ref.3
Developmental stage	Expression is increased during epithelial differentiation in intestinal mucosa as well as in kidney, liver and lung. Ref.2
Post-translational modification	N-glycosylated. Ref.1
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Ref.1 Inferred from direct assay. Source: RGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidate phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Lipid phosphate phosphohydrolase 3		PRO_0000220914
Regions
	Topological domain	1 – 33	33	Cytoplasmic Potential
	Transmembrane	34 – 54	21	Potential
	Topological domain	55 – 85	31	Lumenal Potential
	Transmembrane	86 – 106	21	Potential
	Topological domain	107 – 123	17	Cytoplasmic Potential
	Transmembrane	124 – 144	21	Potential
	Topological domain	145 – 194	50	Lumenal Potential
	Transmembrane	195 – 215	21	Potential
	Topological domain	216 – 226	11	Cytoplasmic Potential
	Transmembrane	227 – 247	21	Potential
	Topological domain	248 – 258	11	Lumenal Potential
	Transmembrane	259 – 279	21	Potential
	Topological domain	280 – 312	33	Cytoplasmic Potential
Amino acid modifications
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	110	1	Phosphotyrosine By similarity
	Modified residue	298	1	Phosphoserine By similarity
	Glycosylation	171	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P97544-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 9B447FD321DB0419	FASTA	312	35,318
	10 20 30 40 50 60 MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK 70 80 90 100 110 120 PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILRI ITGEFYRIYY LKEKSRSTIQ 130 140 150 160 170 180 NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY 190 200 210 220 230 240 RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF 250 260 270 280 290 300 YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTTLSLPAP AIRREILSPV 310 DIMDRSNHHN MV

References

[1]	"The Dri 42 gene, whose expression is upregulated during epithelial differentiation, encodes a novel ER resident transmembrane protein." Barila D., Plateroti M., Nobili F., Muda A.O., Xie Y., Morimoto T., Perozzi G. J. Biol. Chem. 271:29928-29936(1996) [PubMed: 8939937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TOPOLOGY, GLYCOSYLATION. Strain: Wistar. Tissue: Small intestine.
[2]	"Subtractive hybridization cloning of novel genes differentially expressed during intestinal development." Barila D., Murgia C., Nobili F., Gaetani S., Perozzi G. Eur. J. Biochem. 223:701-709(1994) [PubMed: 8055940] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]	"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: TISSUE SPECIFICITY. Strain: Sprague-Dawley.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y07783 mRNA. Translation: CAA69106.1.
IPI	IPI00205490.
UniGene	Rn.12038
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P97544.
Genome annotation databases
Ensembl	ENSRNOG00000008116. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	620454. Ppap2b.
Phylogenomic databases
HOVERGEN	P97544.
Enzyme and pathway databases
BRENDA	3.1.3.4. 248.
Gene expression databases
ArrayExpress	P97544.
GermOnline	ENSRNOG00000008116. Rattus norvegicus.
Family and domain databases
InterPro	IPR016118. P_Acid_Pase/Cl_peroxidase_N. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Gene3D	G3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LPP3_RAT

Accession

Primary (citable) accession number: P97544

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)