TMX1

Thioredoxin domain-containing protein that participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Acts as a key inhibitor of the alternative triglyceride biosynthesis pathway by inhibiting the activity of TMEM68/DIESL at the endoplasmic reticulum, thereby restricting accumulation of triacylglycerol. The alternative triglyceride biosynthesis pathway mediates formation of triacylglycerol from diacylglycerol and membrane phospholipids. Acts as a protein disulfide isomerase by catalyzing formation or reduction of disulfide bonds. Specifically mediates formation of disulfide bonds of transmembrane proteins at the endoplasmic reticulum membrane. Involved in endoplasmic reticulum-associated degradation (ERAD) via its protein disulfide isomerase activity by acting on folding-defective polypeptides at the endoplasmic reticulum membrane. Acts as a negative regulator of platelet aggregation following secretion in the extracellular space. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals. Regulates endoplasmic reticulum-mitochondria Ca(2+) flux..

Function from UniProtKB (Q9H3N1), read 2026-09-23. CC BY 4.0.