Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (By similarity).
TMPRSS11F is a type-II transmembrane protease, similar to hepsin (TMPRSS1). TMPRSS11F is a member of a larger family of membrane attached serine proteases, a poorly defined group that includes TMPRSS11A, B, C, D, E, F, Hepsin, Corin, Matriptase-1, 2 and 3. TMPRSS11F has a domain structure of an aminoterminal cytoplasmic domain, followed by a transmembrane domain, a SEA domain (Sea urchin sperm protein, Enterokinase, Agrin), a short spacer, then the trypsin-like serine protease domain. The SEA domain is thought to play a role in carbohydrate binding in the analogous protein sequences where it is found, but its role in TMPRSS11F is unclear. The cleavage of the Arg206-Ile207 bond is thought to liberate the catalytic domain.
This gene encodes a member of the type II transmembrane serine protease family. Transmembrane serine proteases are regulated by protease inhibitors and known to function in development, homeostasis, infection, and tumorigenesis. Multiple transcript variants encoding different isoforms have been found for this gene.
A synthesized peptide derived from human TMPRSS2, corresponding to a region within the internal amino acids.
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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