Transmembrane protease serine 7 (TMPRSS7)

Matriptase-3, canonically known as Transmembrane protease serine 7 (TMPRSS7), is a member of the type II transmembrane serine protease (TTSP) family. It is a cell-surface glycoprotein characterized by a multi-domain structure including a short N-terminal cytoplasmic tail, a transmembrane domain, and an extracellular stem region containing SEA, CUB, and LDLRa domains, followed by a C-terminal catalytic serine protease domain (10, 11). Matriptase-3 is primarily expressed in the brain, skin, reproductive, and oropharyngeal tissues, where it functions as an active protease that preferentially hydrolyzes substrates with Arginine at the P1 position (4, 10). Recent studies have identified TMPRSS7 as a critical gene for normal neurodevelopment, with loss-of-function variants linked to recurrent central nervous system malformations and neurodevelopmental disorders characterized by impaired synaptic function and neurobehavioral deficits (1). While it is regulated endogenously by various serpins such as plasminogen activator inhibitor-1 and antithrombin III, it remains a potential therapeutic target for conditions involving dysregulated extracellular proteolysis, including cancer and neurological diseases (4, 12).

Other names

Matriptase-3Type II transmembrane serine protease 7TMPS7

Proteolytic cleavage of substrates with a preference for Arginine at the P1 position, leading to the activation of downstream signaling pathways or the shedding of functional domains into the extracellular space.