Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities.

A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis.

Expression and characterization of a PNPLA3 protein isoform (I148M) associated with nonalcoholic fatty liver disease.

Adiponutrin functions as a nutritionally regulated lysophosphatidic acid acyltransferase.

PNPLA3/adiponutrin functions in lipid droplet formation.

PNPLA3 mediates hepatocyte triacylglycerol remodeling.

PNPLA3 is a triglyceride lipase that mobilizes polyunsaturated fatty acids to facilitate hepatic secretion of large-sized very low-density lipoprotein.

PNPLA3(148M) is a gain-of-function mutation that promotes hepatic steatosis by inhibiting ATGL-mediated triglyceride hydrolysis.

Lipid droplet targeting of the lipase coactivator ABHD5 and the fatty liver disease-causing variant PNPLA3 I148M is required to promote liver steatosis.

Loss or gain of function: The functional complexity of the PNPLA3 I148M variant.

PNPLA3-I148M is a neomorph that interferes with two primary hepatic triglyceride clearance pathways.

2-MAG and DAG are transacylated to TAG by PNPLA2/3

2-MAG is transacylated to DAG by PNPLA2/3

TAG is hydrolyzed to DAG by PNPLA2/3

DAG is hydrolyzed to 2-MAG by PNPLA2/3

Acyl chain remodeling of DAG and TAG