Transmembrane protein 131 (TMEM131)

Transmembrane protein 131 (TMEM131) is an evolutionarily conserved multi-domain transmembrane protein implicated in critical physiological processes, especially collagen secretion and ER protein homeostasis. It contains two transmembrane segments and several domains of unknown function (DUF3651), with the N-terminus exhibiting a PapD chaperone-like fold that recruits premature collagen monomers for proper assembly in the endoplasmic reticulum. The C-terminal region interacts with TRAPPC8, facilitating collagen cargo trafficking from the ER to Golgi apparatus[1]. TMEM131 is essential for normal extracellular matrix formation across multicellular organisms. It is expressed in most tissues, with higher levels in T cells and some reproductive tissues, and its activity is linked to fibrotic disease development when dysregulated. TMEM131 is proposed as a novel potential therapeutic target for diseases associated with pathological collagen secretion and tissue fibrosis, although currently no drugs act on this target[1]. Recent evidence also implicates TMEM131 in immune function, particularly T cell maturation and regulation, with methylation changes observed in Down syndrome[2]. The full extent of its physiological roles and therapeutic potential remains under investigation.

Other names

TMEM131KIAA0257RW1CC28YR-23PRO1048Protein RW12610524E03Rik