GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

file:CANAL/LPL1/LPL1-goa.tsv

GOA annotations for C. albicans LPL1

The fetched GOA line for the contested GO:0047372 IBA annotation traces the propagation to PANTHER:PTN000773837 and SGD:S000003112 (S. cerevisiae ROG1).

"GO:0047372 monoacylglycerol lipase activity molecular_function ECO:0000318 IBA GO_REF:0000033 PANTHER:PTN000773837|SGD:S000003112"

file:CANAL/LPL1/LPL1-hypotheses/function-hypothesis-go-0047372/openscientist.md

OpenScientist hypothesis investigation - LPL1 monoacylglycerol lipase activity

OpenScientist concluded that GO:0047372 on Candida LPL1 is a wrong-subfamily phylogenetic transfer from the ROG1 monoacylglycerol lipase branch.

"The core issue is that GO:0047372 was a phylogenetic transfer from the wrong subfamily."
The report found that PAINT correctly scopes GO:0047372 to ROG1/SF62 rather than the LPL1/SF24 phospholipase branch, but the exact current source node must be taken from GOA rather than the report.

"The MAG lipase evidence applies to ROG1 (SF62), not LPL1 (SF24)."

file:CANAL/LPL1/LPL1-deep-research.md

Deep research analysis of C. albicans LPL1 gene

S. cerevisiae homolog LPL1 encodes phospholipase B with conserved catalytic motif

"Contains the canonical lipase motif GXSXG essential for catalytic activity"
Phospholipase B enzymes have three distinct enzymatic activities

"Fungal phospholipase B (PLB) enzymes harbor three distinct activities: 1. sn-1 and sn-2 fatty acid ester hydrolase activity, 2. Lysophospholipase activity, 3. Transacylase activity"
Exclusive localization to lipid droplets during stationary phase

"The S. cerevisiae LPL1 (YOR059c) gene encodes a phospholipase B localized to lipid droplets during stationary phase... Exclusively localized to lipid droplets at stationary phase"
Broad substrate specificity for glycerophospholipids

"Shows phospholipase activity with broad substrate specificity, acting on all glycerophospholipids primarily at sn-2 position, then at sn-1 position"

file:CANAL/LPL1/LPL1-uniprot.txt

UniProt entry for C. albicans LPL1 (Q5AMS2)

Contains DUF676 lipase-like domain

"DOMAIN 14..213 /note="DUF676""
Predicted hydrophobic region for lipid droplet association

"TRANSMEM 286..306 /note="Helical""
Member of putative lipase ROG1 family

"SIMILARITY: Belongs to the putative lipase ROG1 family"