AYR1 (YIL124W, P40471) notes

Evidence journal for the YeastPathways triacylglycerol_biosynthesis batch. No paid deep research was run; sources are UniProt and cached publications.

• Catalytic identity: NADPH-dependent 1-acyl-DHAP reductase (EC 1.1.1.101), an SDR family enzyme. PMID:10617610
• Deletion abolishes ADR activity in lipid particles; microsomes keep about one third of the activity, so a second microsomal ADR must exist. PMID:10617610
• The ADR activity in yeast membranes was first detected in 1992. PMID:1512203
• Location: Ayr1 is a constitutive lipid droplet protein, also found in the ER, and by fractionation in the mitochondrial outer membrane. PMID:24868093 PMID:28916712
• Secondary activity: minor TAG lipase; TAG mobilisation persists without it in a tgl3/4/5 background. PMID:24187129
• Channel claim: reconstituted Ayr1 forms an NADPH-stimulated cation channel. This comes from a single study. PMID:28916712
• Curation decisions: ADR activity, PA biosynthesis, and the LD/ER locations are core. Lipase, TAG catabolism, the mitochondrial locations and the channel are kept as non-core. The YeastPathways RCA "cytosol" rows are removed because the protein sits on LDs and the ER.