LYPLA3

LYPLA3, also known as Group XV phospholipase A2, is an enzyme that in humans is encoded by the PLA2G15 gene.

PLA2G15
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4X90, 4X91, 4X92, 4X93, 4X94, 4X95, 4X97
Identifiers
Aliases	PLA2G15, ACS, GXVPLA2, LLPL, LPLA2, LYPLA3, phospholipase A2 group XV
External IDs	OMIM: 609362; MGI: 2178076; HomoloGene: 8200; GeneCards: PLA2G15; OMA:PLA2G15 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16q22.1 Start 68,245,304 bp End 68,261,058 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 D3 Start 106,877,031 bp End 106,891,347 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle apex of heart muscle of thigh left ventricle right auricle right hemisphere of cerebellum stromal cell of endometrium glutes right lobe of liver monocyte Top expressed in stroma of bone marrow secondary oocyte primary oocyte blastocyst blastocyst zygote calvaria morula lumbar spinal ganglion spleen More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity O-acyltransferase activity lysophospholipase activity acyltransferase activity hydrolase activity phospholipid binding calcium-independent phospholipase A2 activity Cellular component membrane mitochondrion lysosome extracellular exosome extracellular space nucleoplasm intracellular membrane-bounded organelle extracellular region Biological process fatty acid catabolic process phosphatidylcholine catabolic process ceramide metabolic process lipid metabolism fatty acid metabolic process lipid catabolic process phosphatidylethanolamine catabolic process glycerophospholipid metabolic process phosphatidylcholine metabolic process phospholipid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23659 192654 Ensembl ENSG00000103066 ENSMUSG00000031903 UniProt Q8NCC3 Q8VEB4 RefSeq (mRNA) NM_012320 NM_001363551 NM_133792 NM_001357319 RefSeq (protein) NP_036452 NP_001350480 NP_598553 NP_001344248 Location (UCSC) Chr 16: 68.25 – 68.26 Mb Chr 8: 106.88 – 106.89 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Further reading

• Wang A, Dennis EA (1999). "Mammalian lysophospholipases". Biochim. Biophys. Acta. 1439 (1): 1–16. doi:10.1016/s1388-1981(99)00063-3. 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407. S2CID 19371828.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 403697. 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. PMC 2286551. 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. PMC 528928. 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.