Cloned (Comment) | Organism |
---|---|
gene LPAAT4, isolated from seed of unsaturated fatty acid (UFA)-rich Paeonia rockii, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant overexpression of the enzyme in Arabidopsis thaliana resulting in a significant increase in the content of oleic acid (OA) and total fatty acids (FAs) in seeds. AtDGAT1, AtGPAT9, and Atoleosin, involved in TAG assembly, are upregulated in PrLPAAT4-overexpressing lines. Recombinnat expression of GFP-tagged enzyme in tobacco lower epidermal cell plama membranes | Paeonia rockii |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
plasma membrane | a transmembrane enzyme, it exhibits an overlap between the transmembrane and LPLAT_AGPAT-like domains | Paeonia rockii | 5886 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paeonia rockii | KX256279 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | tissue-specific expression profile of PrLPAAT4 | Paeonia rockii | - |
seed | - |
Paeonia rockii | - |
Subunits | Comment | Organism |
---|---|---|
? | x * 42900, about, sequence calculation | Paeonia rockii |
Synonyms | Comment | Organism |
---|---|---|
LPAAT4 | - |
Paeonia rockii |
lysophosphatidic acid acyltransferase | - |
Paeonia rockii |
lysophosphatidyl acyltransferase 4 | - |
Paeonia rockii |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family, PrLPAAT4 possesses a 1-acyl-sn-glycerol-3-phosphate acyltransferase-related domain, it is subordinated to cluster III. Comparative analysis of gene structure and conserved domain in the LPAAT4 proteins | Paeonia rockii |
metabolism | PrLPAAT4 plays an important role in seed fatty acid biosynthesis | Paeonia rockii |
additional information | comparative structure deduction and analysis of PrLPAAT4 | Paeonia rockii |
physiological function | lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. PrLPAAT4, a putative lysophosphatidic acid acyltransferase from Paeonia rockii, plays an important role in seed fatty acid biosynthesis. LPAATs play a crucial role in catalyzing the second step of triacylglycerol (TAG) formation, determining TAGs acyl composition at the sn-2-position, and controlling the conversion of LPA to PA. PrLPAAT4 might function as a positive regulator in seed fatty acid biosynthesis | Paeonia rockii |