Transmembrane protein 33 (TMEM33)

Transmembrane protein 33 (TMEM33) is an endoplasmic reticulum (ER)-resident multipass transmembrane protein involved in several cellular processes, including the modulation of ER stress, regulation of the unfolded protein response (UPR), and organization of ER tubular networks[1][3][5]. It binds and modulates the activity of key UPR sensors (notably PERK and IRE1α), influencing downstream signaling events that control apoptosis and autophagy in response to ER stress, particularly in cancer cells[1][3][4][5]. TMEM33 also participates in lipid metabolism by facilitating the degradation of SREBP-cleavage activating protein (SCAP) and modulates intracellular calcium signaling, impacting angiogenesis and other processes[1][5]. It forms complexes with other proteins involved in innate immune signaling, such as those modulating the cGAS-STING pathway[4][5]. TMEM33 is highly conserved and broadly expressed, and increased expression has been linked to poorer outcomes in certain cancers, supporting its emerging role as a disease biomarker[4]. No small molecule drugs or inhibitors directly targeting TMEM33 are currently known[5].

Other names

1600019D15RikDB83FLJ10525Pom33Protein DB83SHINC-3SHINC3TMEM33