PPAP2A

From Wikipedia, the free encyclopedia

Phosphatidic acid phosphatase type 2A

Identifiers

PPAP2A; LLP1a; LPP1; PAP-2a; PAP2; PAP2a2; PAP2alpha2; PAPalpha1

External IDs

OMIM: 607124 MGI: 108412 HomoloGene: 7484

Gene ontology
Molecular Function:	• phosphatidate phosphatase activity • hydrolase activity
Cellular Component:	• membrane fraction • plasma membrane • integral to plasma membrane
Biological Process:	• protein kinase C activation • negative regulation of cell proliferation • germ cell migration • regulation of lipid metabolic process • androgen receptor signaling pathway • phospholipid dephosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003711 (mRNA)
NP_003702 (protein)

NM_008247 (mRNA)
NP_032273 (protein)

Location

Chr 5: 54.76 - 54.97 Mb

Chr 13: 113.92 - 113.99 Mb

Pubmed search

[1]

[2]

Phosphatidic acid phosphatase type 2A, also known as PPAP2A, is a human gene.^[1]

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 an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.^[1]

[edit] References

^ ^a ^b Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A.

[edit] Further reading

Kanoh H, Kai M, Wada I (1999). "Molecular characterization of the type 2 phosphatidic acid phosphatase.". Chem. Phys. Lipids 98 (1-2): 119-26. PMID 10358934.
Nanjundan M, Possmayer F (2003). "Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase.". Am. J. Physiol. Lung Cell Mol. Physiol. 284 (1): L1-23. doi:10.1152/ajplung.00029.2002. PMID 12471011.
Kai M, Wada I, Imai S, et al. (1997). "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase.". J. Biol. Chem. 272 (39): 24572-8. PMID 9305923.
Ulrix W, Swinnen JV, Heyns W, Verhoeven G (1998). "Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP.". J. Biol. Chem. 273 (8): 4660-5. PMID 9468526.
Leung DW, Tompkins CK, White T (1998). "Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells.". DNA Cell Biol. 17 (4): 377-85. PMID 9570154.
Hooks SB, Ragan SP, Lynch KR (1998). "Identification of a novel human phosphatidic acid phosphatase type 2 isoform.". FEBS Lett. 427 (2): 188-92. PMID 9607309.
Roberts R, Sciorra VA, Morris AJ (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.". J. Biol. Chem. 273 (34): 22059-67. PMID 9705349.
Neumann J, Maas R, Bokník P, et al. (1999). "Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts.". J. Pharmacol. Exp. Ther. 289 (1): 188-93. PMID 10087003.
Moreno CS, Park S, Nelson K, et al. (2000). "WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A.". J. Biol. Chem. 275 (8): 5257-63. PMID 10681496.
Roberts RZ, Morris AJ (2001). "Role of phosphatidic acid phosphatase 2a in uptake of extracellular lipid phosphate mediators.". Biochim. Biophys. Acta 1487 (1): 33-49. PMID 10962286.
Woetmann A, Brockdorff J, Lovato P, et al. (2003). "Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling.". J. Biol. Chem. 278 (5): 2787-91. doi:10.1074/jbc.M210196200. PMID 12426308.
Pandey AV, Mellon SH, Miller WL (2003). "Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17.". J. Biol. Chem. 278 (5): 2837-44. doi:10.1074/jbc.M209527200. PMID 12444089.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Smyth SS, Sciorra VA, Sigal YJ, et al. (2003). "Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity.". J. Biol. Chem. 278 (44): 43214-23. doi:10.1074/jbc.M306709200. PMID 12909631.
Tanyi JL, Hasegawa Y, Lapushin R, et al. (2004). "Role of decreased levels of lipid phosphate phosphatase-1 in accumulation of lysophosphatidic acid in ovarian cancer.". Clin. Cancer Res. 9 (10 Pt 1): 3534-45. PMID 14506139.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Grkovich A, Johnson CA, Buczynski MW, Dennis EA (2006). "Lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages is phosphatidic acid phosphohydrolase-1-dependent.". J. Biol. Chem. 281 (44): 32978-87. doi:10.1074/jbc.M605935200. PMID 16950767.
Kai M, Sakane F, Jia YJ, et al. (2007). "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts.". J. Biochem. 140 (5): 677-86. doi:10.1093/jb/mvj195. PMID 17005594.