Protease, Serine 36 (PRSS36)

The deduced 855-amino acid protein has a predicted molecular mass of 93 kD and contains 9 potential N-glycosylation sites. PRSS36 contains a signal peptide, followed by a propeptide domain, an active serine protease domain with the catalytic his, asp, and ser residues, and 2 serine protease domains predicted to be catalytically inactive. The first serine protease domain shares amino acid identity of 40 to 42% with gamma-1 tryptase (TPSG1), pancreasin, matriptase (ST14;), matriptase-2 (TMPRSS6), and polyserase-1 (TMPRSS9). Northern blot analysis detected a 5-kb transcript in fetal kidney and adult skeletal muscle, liver, placenta, and heart. A 2.2-kb transcript was detected in placenta, prostate, and colon and lung adenocarcinoma cell lines, and may be produced by alternative splicing.