Target intelligence / Profile preview

Lipase maturation factor 1 (LMF1)

Target
LMF1
Molecular classification
Transmembrane protein, Endoplasmic reticulum-associated protein, Protein-folding chaperone
01

Overview

Lipase maturation factor 1 (LMF1) is a membrane-bound protein located in the endoplasmic reticulum, essential for the folding and assembly of a selected group of secreted, dimeric lipases, including lipoprotein lipase, hepatic lipase, and endothelial lipase[1][2][3]. LMF1 interacts with enzymes involved in N-linked glycosylation and endoplasmic reticulum-resident oxidoreductases, supporting the formation and maintenance of correct disulfide bonds during protein maturation. LMF1 also assists the secretion of other disulfide-rich oligomeric proteins such as fibronectin and LDL receptor[2][3]. Mutations in LMF1 can cause combined lipase deficiency and severe hypertriglyceridemia in humans due to impaired lipase activity, confirming its crucial role in human lipid metabolism and redox homeostasis in the ER[1][2][3].

Other names
C16orf26TMEM112HMFN1876JFP11FLJ12681FLJ22302TMEM112ATransmembrane protein 112
02

Biological functions

Maturation and folding of dimeric secreted lipases (e.g. lipoprotein lipase, hepatic lipase, endothelial lipase)Contributes to redox homeostasis in the endoplasmic reticulumInteracts with protein disulfide isomerases and N-glycosylation enzymesFacilitates efficient secretion of disulfide-rich oligomeric proteins (fibronectin, LDL receptor)
03

Disease associations

Hypertriglyceridemia due to combined lipase deficiencyPotential contribution to lipid metabolism disorders
04

Safety considerations

Genetic mutations can result in severe metabolic disorders, such as neonatal lethal hyperchylomicronemiaNo known therapeutic safety concerns since LMF1 is not a current drug target
05

Biomarkers

Mutations in LMF1 (e.g. causing truncated DUF1222 domain) as biomarkers for genetic combined lipase deficiency and severe hypertriglyceridemia

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