LYPLA3 (gene)
From Wikipedia, the free encyclopedia
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Lysophospholipase 3 (lysosomal phospholipase A2)
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| Identifiers | ||||||||||||||
| Symbol(s) | LYPLA3; ACS; DKFZp564A0122; LLPL; LPLA2 | |||||||||||||
| External IDs | OMIM: 609362 MGI: 2178076 HomoloGene: 8200 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| 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) |
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| 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. PMID 16303743.

