Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung

Biochim Biophys Acta. 2001 Mar 19;1518(1-2):204-9. doi: 10.1016/s0167-4781(01)00184-1.


Two cDNAs encoding novel mosaic proteins with a serine protease domain and potential regulatory modules, consisting of a protein kinase substrate and a low-density lipoprotein receptor, were cloned from a human lung cDNA library by PCR. One with a transmembrane domain (MSPL) and the other without one (MSPS) comprise 581 and 537 amino acids, respectively. Except for the C-terminal ends, the two isoforms had an identical serine protease domain exhibiting 42, 39 and 43% identity with those of plasma kallikrein, hepsin and transmembrane protease serine 2, respectively. Both genes were predominantly expressed in human lung, placenta, pancreas and prostate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Cell Membrane / metabolism
  • Cloning, Molecular
  • DNA, Complementary
  • Gene Expression
  • Humans
  • Lung / enzymology
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Receptors, LDL / genetics*
  • Serine Endopeptidases / genetics*
  • Serine Endopeptidases / metabolism
  • Tissue Distribution
  • Trypsin / genetics*


  • DNA, Complementary
  • Membrane Proteins
  • Receptors, LDL
  • Serine Endopeptidases
  • TMPRSS13 protein, human
  • Trypsin

Associated data

  • GENBANK/AB048796
  • GENBANK/AB048797