Description: Homo sapiens phospholipase A2, group III (PLA2G3), mRNA. RefSeq Summary (NM_015715): This gene encodes a protein that belongs to the secreted phospholipase A2 family, whose members include the bee venom enzyme. The encoded enzyme functions in lipid metabolism and catalyzes the calcium-dependent hydrolysis of the sn-2 acyl bond of phospholipids to release arachidonic acid and lysophospholipids. This enzyme acts as a negative regulator of ciliogenesis, and may play a role in cancer development by stimulating tumor cell growth and angiogenesis. This gene is associated with oxidative stress, and polymorphisms in this gene are linked to risk for Alzheimer's disease. [provided by RefSeq, Apr 2014]. Transcript (Including UTRs) Position: hg19 chr22:31,530,793-31,536,469 Size: 5,677 Total Exon Count: 7 Strand: - Coding Region Position: hg19 chr22:31,531,709-31,536,340 Size: 4,632 Coding Exon Count: 7
ID:PA2G3_HUMAN DESCRIPTION: RecName: Full=Group 3 secretory phospholipase A2; EC=3.1.1.4; AltName: Full=Group III secretory phospholipase A2; Short=GIII sPLA2; Short=sPLA2-III; AltName: Full=Phosphatidylcholine 2-acylhydrolase 3; Flags: Precursor; FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage: 1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE. Plays a role in ciliogenesis. CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1- acylglycerophosphocholine + a carboxylate. COFACTOR: Binds 1 calcium ion per subunit. ENZYME REGULATION: Arachidonic acid release is markedly increased by glypican, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan. SUBCELLULAR LOCATION: Secreted. Cell membrane. Cytoplasm, cytoskeleton, centrosome, centriole. TISSUE SPECIFICITY: Expressed in kidney, heart, liver, and skeletal muscle. Also present in placenta and peripheral blood leukocytes. Not detected in brain, colon, thymus, spleen and small intestine. In lung, expressed in bronchial epithelial cells and alveolar macrophages, but scarcely detected in alveolar epithelium, arterial walls and interstitial fibroblasts (at protein level). In joints of osteoarthritis and rheumatoid arthritis, expressed in endothelial cells (at protein level). In normal heart, detected in some vessels. In myocardial tissues with acute infarction, expressed in vascular endothelial cells adjacent to cardiomyocytes and those in lesions with granulation. Expression in cardiomyocytes is scarce (at protein level). In uterus, breast and colon cancers, detected in tumor cells and neighboring microvascular endothelium, but not in normal glandular tissues (at protein level). INDUCTION: By IL1B/interleukin-1 beta and TNF in microvascular endothelial cells (at protein level). PTM: N-glycosylation does not affect the catalytic activity, but is required for proper secretion. A nonglycosylated form was observed in several cell types. PTM: In several cell types, the N- and C-termini are cleaved off. SIMILARITY: Belongs to the phospholipase A2 family. SEQUENCE CAUTION: Sequence=AAD15617.1; Type=Erroneous gene model prediction;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9NZ20
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.