TMPRSS11E: Lysates

TMPRSS11E 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. The highest degree of identity is with TMPRSS11A, which shares 43% identity at the amino acid level. TMPRSS11E 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 the role in TMPRSS11E is unclear. The cleavage of the Arg191 Ile192 bond liberates the catalytic domain. TMPRSS11E has been shown to cleave fibronectin, gelatin, casein and pro uPA in vitro, and to form complexes with serpinA5 and serpinE1.