PPAP2B

Phosphatidic acid phosphatase type 2B
Identifiers
Symbols	PPAP2B ; Dri42; LPP3; PAP2B; VCIP
External IDs	OMIM: 607125 MGI: 1915166 HomoloGene: 15410 GeneCards: PPAP2B Gene
EC number	3.1.3.4
Gene ontology Molecular function • phosphoprotein phosphatase activity • integrin binding • protein binding • phosphatidate phosphatase activity • sphingosine-1-phosphate phosphatase activity • lipid phosphatase activity Cellular component • endoplasmic reticulum membrane • Golgi apparatus • plasma membrane • adherens junction • membrane • integral component of membrane • extracellular exosome Biological process • blood vessel development • gastrulation with mouth forming second • negative regulation of protein phosphorylation • protein dephosphorylation • lipid metabolic process • phospholipid metabolic process • sphingolipid metabolic process • germ cell migration • regulation of Wnt signaling pathway • sphingolipid biosynthetic process • homotypic cell-cell adhesion • small molecule metabolic process • canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration • canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion • canonical Wnt signaling pathway involved in positive regulation of wound healing • positive regulation of peptidyl-tyrosine phosphorylation • protein stabilization • positive regulation of sequence-specific DNA binding transcription factor activity • Bergmann glial cell differentiation • regulation of sphingolipid mediated signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8613	67916
Ensembl	ENSG00000162407	ENSMUSG00000028517
UniProt	O14495	Q99JY8
RefSeq (mRNA)	NM_003713	NM_080555
RefSeq (protein)	NP_003704	NP_542122
Location (UCSC)	Chr 1: 56.49 – 56.65 Mb	Chr 4: 105.16 – 105.23 Mb
PubMed search

Lipid phosphate phosphohydrolase 3 is an enzyme that in humans is encoded by the PPAP2B gene.^[1][2]

Function

The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is a membrane glycoprotein localized at the cell plasma membrane. It has been shown to actively hydrolyze extracellular lysophosphatidic acid and short-chain phosphatidic acid. The expression of this gene is found to be enhanced by epidermal growth factor in Hela cells. Alternatively spliced transcript variants encoding the same protein have been described.^[2]

References

1. Kai M, Wada I, Imai Si, Sakane F, Kanoh H (Sep 1997). "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase". The Journal of Biological Chemistry 272 (39): 24572–8. doi:10.1074/jbc.272.39.24572. PMID 9305923.
2. "Entrez Gene: PPAP2B phosphatidic acid phosphatase type 2B".

Further reading

• Nanjundan M, Possmayer F (Jan 2003). "Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase". American Journal of Physiology. Lung Cellular and Molecular Physiology 284 (1): L1–23. doi:10.1152/ajplung.00029.2002. PMID 12471011.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Roberts R, Sciorra VA, Morris AJ (Aug 1998). "Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform". The Journal of Biological Chemistry 273 (34): 22059–67. doi:10.1074/jbc.273.34.22059. PMID 9705349.
• Sciorra VA, Morris AJ (Nov 1999). "Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cells". Molecular Biology of the Cell 10 (11): 3863–76. doi:10.1091/mbc.10.11.3863. PMC 25685. PMID 10564277.
• Ishikawa T, Kai M, Wada I, Kanoh H (Apr 2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". Journal of Biochemistry 127 (4): 645–51. doi:10.1093/oxfordjournals.jbchem.a022652. PMID 10739957.
• Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK (Apr 2003). "Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP". The EMBO Journal 22 (7): 1539–54. doi:10.1093/emboj/cdg165. PMC 152909. PMID 12660161.
• Burnett C, Howard K (Aug 2003). "Fly and mammalian lipid phosphate phosphatase isoforms differ in activity both in vitro and in vivo". EMBO Reports 4 (8): 793–9. doi:10.1038/sj.embor.embor900. PMC 1326340. PMID 12856002.
• Burnett C, Makridou P, Hewlett L, Howard K (Jan 2004). "Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity". BMC Biochemistry 5: 2. doi:10.1186/1471-2091-5-2. PMC 319698. PMID 14725715.
• Kai M, Sakane F, Jia YJ, Imai S, Yasuda S, Kanoh H (Nov 2006). "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts". Journal of Biochemistry 140 (5): 677–86. doi:10.1093/jb/mvj195. PMID 17005594.
• Mechtcheriakova D, Wlachos A, Sobanov J, Bornancin F, Zlabinger G, Baumruker T, Billich A (Jun 2007). "FTY720-phosphate is dephosphorylated by lipid phosphate phosphatase 3". FEBS Letters 581 (16): 3063–8. doi:10.1016/j.febslet.2007.05.069. PMID 17555747.