LYPLA3 (gene)

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Lysophospholipase 3 (lysosomal phospholipase A2)
Identifiers
Symbol(s) LYPLA3; ACS; DKFZp564A0122; LLPL; LPLA2
External IDs OMIM: 609362 MGI2178076 HomoloGene8200
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 23659 192654
Ensembl ENSG00000103066 ENSMUSG00000031903
Uniprot Q8NCC3 Q3U303
Refseq NM_012320 (mRNA)
NP_036452 (protein)
NM_133792 (mRNA)
NP_598553 (protein)
Location Chr 16: 66.84 - 66.85 Mb Chr 8: 109.04 - 109.05 Mb
Pubmed search [1] [2]

Lysophospholipase 3 (lysosomal phospholipase A2), also known as LYPLA3, is a human gene.[1]

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine to glycerophosphorylcholine and a free fatty acid. This enzyme is present in the plasma and thought to be associated with high-density lipoprotein. A later paper contradicts the function of this gene. It demonstrates that this gene encodes a lysosomal enzyme instead of a lysophospholipase and has both calcium-independent phospholipase A2 and transacylase activities.[1]

[edit] References

[edit] Further reading

  • Wang A, Dennis EA (1999). "Mammalian lysophospholipases.". Biochim. Biophys. Acta 1439 (1): 1-16. PMID 10395961. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149. 
  • Taniyama Y, Shibata S, Kita S, et al. (1999). "Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase.". Biochem. Biophys. Res. Commun. 257 (1): 50-6. doi:10.1006/bbrc.1999.0411. PMID 10092508. 
  • Ohta T, Michel JJ, Schottelius AJ, Xiong Y (1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity.". Mol. Cell 3 (4): 535-41. PMID 10230407. 
  • Hiraoka M, Abe A, Shayman JA (2002). "Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase.". J. Biol. Chem. 277 (12): 10090-9. doi:10.1074/jbc.M111977200. PMID 11790796. 
  • 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. 
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265-70. doi:10.1101/gr.1293003. PMID 12975309. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Abe A, Poucher HK, Hiraoka M, Shayman JA (2004). "Induction of lysosomal phospholipase A2 through the retinoid X receptor in THP-1 cells.". J. Lipid Res. 45 (4): 667-73. doi:10.1194/jlr.M300342-JLR200. PMID 14754907. 
  • Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites.". Protein Sci. 13 (10): 2819-24. doi:10.1110/ps.04682504. PMID 15340161. 
  • 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. 
  • Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117-26. doi:10.1093/dnares/12.2.117. PMID 16303743.