TMPRSS9

Polyserase-1 is also known as TMPRSS9 (transmembrane serine proteinase-9), and polyserase protease 1. Polyserase1 was originally discovered in human liver as a mosaic serine proteinase with a type II transmembrane domain and three tandem repeats of serine proteinase domains. The domain structure of polyserase1 consists of a cytoplasmic domain, followed by a transmembrane domain, a "stem" region, an LDL receptor-like domain, and three serine proteinase domains. The third serine proteinase domain does not contain the canonical Gly-Asp-Ser-Gly-Gly residues found in the first two serase domains, and is not thought to be proteolytically active. Polyserase1 is found in greatest abundance in human liver, muscle, heart, placenta, and in fetal kidney and liver. Several human tumor cell lines also express significant amounts of polyserase1. Polyserase1 is a membrane associated protein, and the cleaved serase domains are thought to be retained on the cell surface by association with the propeptide domain, although the protein may also be found shed into conditioned culture media.

TMPRSS9; transmembrane protease, serine 9; transmembrane protease serine 9; polyserase 1; polyserase-1; polyserase-I; polyserine protease 1; transmembrane serine protease 9;