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
-
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
-
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"
-
Mutation of the catalytic serine or aspartate abolishes patatin esterase activity, so a patatin-family protein lacking the serine is not expected to be an active hydrolase.
"Ser77 and Asp215 were
critical for both esterase and bioactivity"
A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis
-
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
-
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"
-
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
-
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"
-
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 modeled 302-aa sequence lacks the entire N-terminal half of the patatin"
Re-review analysis (2026-10-20): gene model, homoeologs and phylogenetic placement of A0A3B6GK97
-
The 302-aa TraesCS3D02G033600 model is incomplete; genomic sequence about 1.5 kb upstream encodes an N-terminal region matching the 444-aa 3B homoeolog A0A3B6FIU7.
"The 302-aa model is an incomplete gene model"
-
Neither the reconstructed 3D N-terminus nor the 3B homoeolog carries the catalytic serine elbow or the canonical oxyanion glycines, so the product is predicted to be a non-catalytic patatin-like protein.
"Even the reconstructed full-length product, and the full-length 3B homoeolog, lack the catalytic serine nucleophile and the canonical oxyanion glycines."
-
In the PANTHER 19 tree the protein sits in grass-specific subfamily SF103, sister to rice PLP2, and is separated from the Arabidopsis pPLAII proteins by duplication node PTN009133995.
"A0A3B6GK97 is therefore not an ortholog of any Arabidopsis pPLAII protein."
UniProtKB entry A0A3B6GK97