Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
Annotation inferences using phylogenetic trees
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GO_Central assigns this protein two IBA (phylogenetic) molecular-function annotations confirming lipase activity: GO:0004620 glycerophospholipase activity and GO:0047372 monoacylglycerol lipase activity (both ECO:0000318, GO_REF:0000033, assigned 2017-02-28). These are present in AmiGO/GOlr but were NOT returned by the QuickGO GOA pull used to seed this review, so they are recorded here as out-of-band evidence rather than as existing_annotations entries.
"Annotation inferences using phylogenetic trees"
The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad
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Patatin is a lipid acyl hydrolase that uses a non-classical Ser-Asp catalytic dyad rather than the canonical Ser-His-Asp triad; this defines the catalytic mechanism of the patatin/PNPLA domain family to which this wheat protein belongs.
"patatin has a Ser-Asp catalytic dyad"
A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis
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Plant patatin-like proteins (e.g. Arabidopsis PLP2) are pathogen-inducible cytoplasmic lipid acyl hydrolases with broad substrate specificity that contribute to lipid-based signaling in plant-pathogen interactions; this is the basis for the family-level "plant defense" association but has not been shown for this wheat protein.
"PLP2 encodes a cytoplasmic lipid acyl hydrolase with wide substrate specificity"
Deep research report: PNPLA domain-containing protein A0A3B6GK97 in wheat (Triticum aestivum) - family-level functional annotation from scientific literature
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Plant PNPLA/patatin proteins function as calcium-independent phospholipases with lipase/phospholipase A-type activities. Their primary roles include lipid mobilization during seed germination, membrane phospholipid turnover, and stress adaptation. Substrate specificity includes phosphatidylcholine, phosphatidylserine, triacylglycerols, and lysophospholipids.
"The best-supported plant functions are lipid mobilization during seed germination, initiation of storage-oil breakdown, membrane phospholipid turnover, and remodeling of LD surfaces to allow access of TAG lipases"
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No direct literature exists for A0A3B6GK97; all functional inferences are family-level, drawn from rice OsPLB, Arabidopsis PLP/pPLA, rapeseed patatin-like lipase, and potato patatin studies.
"Direct literature on the wheat protein A0A3B6GK97 is not available in the current scientific literature"
Bioinformatics analysis: pPLA subfamily placement and catalytic-site integrity of A0A3B6GK97
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By sequence identity (42-50% to pPLAII / rice pPLAs vs ~23% to pPLAIII and ~16% to pPLAI) and neighbour-joining placement, A0A3B6GK97 belongs to the pPLAII subfamily of plant patatin-related phospholipase A - the soluble lipid-acyl-hydrolase (defense/wounding/stress) clade - not pPLAIII (galactolipase/growth) or pPLAI (iPLA2-like). The single-domain architecture and this placement make a membrane trafficking role very unlikely.
"A0A3B6GK97 belongs to the pPLAII subfamily"
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The modeled 302-aa sequence LACKS the N-terminal half of the patatin catalytic domain - both the oxyanion glycine-rich block (DGGG) and the catalytic-serine nucleophile elbow (G-T-S-T-G) are absent (zero G-x-S-x-G motifs in 302 aa), while the catalytic Asp is retained. As modeled the protein is predicted catalytically inactive; most parsimoniously an incomplete/incorrect gene model, though a genuine degenerate pseudo-enzyme cannot be excluded from sequence alone.
"the deposited 302-aa model lacks the N-terminal catalytic core"