Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis.
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PLP2 is a cytoplasmic lipid acyl hydrolase with wide substrate specificity.
"PLP2 encodes a cytoplasmic lipid acyl hydrolase with wide substrate specificity"
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PLP2 levels correlate with cell death and reduce HR-based restriction of avirulent bacteria.
"PLP2 potentiates plant cell death inflicted by Botrytis and reduces the efficiency of the hypersensitive response in restricting the multiplication of avirulent bacteria"
Proteome changes in Arabidopsis thaliana roots upon exposure to Cd2+.
The Arabidopsis patatin-like protein 2 (PLP2) plays an essential role in cell death execution and differentially affects biosynthesis of oxylipins and resistance to pathogens.
The AP2/ERF transcription factor AtERF73/HRE1 modulates ethylene responses during hypoxia in Arabidopsis.
Evidence for network evolution in an Arabidopsis interactome map.
Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.
Extensive signal integration by the phytohormone protein network.
The patatin-containing phospholipase A pPLAIIα modulates oxylipin formation and water loss in Arabidopsis thaliana.
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Purified PLP2 deacylates glycerophospholipids at sn-1 and sn-2 and galactolipids to lyso-galactolipids.
"Phospholipids are cleaved by pPLAIIα at the sn -1 and sn -2 positions, and galactolipids, including those containing oxophytodienoic acids, can also serve as substrates."
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The knockout has reduced LPC/LPE, elevated JA/OPDA, and faster water loss.
"These results indicate that pPLAIIα negatively regulates oxylipin production and suggest a role in the removal of oxidatively modified fatty acids from membranes."
Molecular identification of cytosolic, patatin-related phospholipases A from Arabidopsis with potential functions in plant signal transduction.
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AtPLA IIA (PLP2)-GFP is cytoplasmic, not vacuolar; the transcript is mainly in roots.
"For AtPLA IIA, AtPLA IVA, and AtPLA IVC, a cytoplasmic localization is suggested, but association with membranes (e.g. plasma membrane or ER) cannot be excluded."
Expression profiles of Arabidopsis phospholipase A IIA gene in response to biotic and abiotic stresses.
UniProtKB entry O48723 for Arabidopsis PLP2