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P97544 (LPP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipid phosphate phosphohydrolase 3

EC=3.1.3.4
Alternative name(s):
Differentially expressed in rat intestine 42
Short name=Dri42
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name=PAP-2b
Short name=PAP2b
Gene names
Name:Ppap2b
Synonyms:Lpp3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence 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 1,2-diacylglycerol 3-phosphate + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Lipid phosphate phosphohydrolase 3
PRO_0000220914

Regions

Topological domain1 – 3333Cytoplasmic Potential
Transmembrane34 – 5421Helical; Potential
Topological domain55 – 8531Lumenal Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 12317Cytoplasmic Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 19450Lumenal Potential
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 22611Cytoplasmic Potential
Transmembrane227 – 24721Helical; Potential
Topological domain248 – 25811Lumenal Potential
Transmembrane259 – 27921Helical; Potential
Topological domain280 – 31233Cytoplasmic Potential

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue1101Phosphotyrosine By similarity
Modified residue2981Phosphoserine By similarity
Glycosylation1711N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P97544 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 9B447FD321DB0419

FASTA31235,318
        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 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07783 mRNA. Translation: CAA69106.1.
IPIIPI00205490.
UniGeneRn.12038.

3D structure databases

ProteinModelPortalP97544.
ModBaseSearch...

Protein-protein interaction databases

STRINGP97544.

Proteomic databases

PRIDEP97544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCNM_138905. rat.

Organism-specific databases

RGD620454. Ppap2b.

Phylogenomic databases

eggNOGroNOG07493.
HOVERGENHBG002048.
InParanoidP97544.
OrthoDBEOG40CHHS.
PhylomeDBP97544.

Gene expression databases

ArrayExpressP97544.
GenevestigatorP97544.
GermOnlineENSRNOG00000008116. Rattus norvegicus.

Family and domain databases

InterProIPR016118. P_Acid_Pase/Cl_peroxidase_N.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
Gene3DG3DSA:1.20.144.10. P_Acid_Pase/Cl_peroxidase_N. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. AcPase_VanPerase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPP3_RAT
AccessionPrimary (citable) accession number: P97544
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 1997
Last modified: September 21, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families