Tryptase (TPSAB1) Native Protein

Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. These genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. The alleles of this gene exhibit an unusual amount of sequence variation, such that the alleles were once thought to represent two separate genes, alpha and beta 1. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. [provided by RefSeq, Jul 2008]

TPSAB1: Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. Belongs to the peptidase S1 family. Tryptase subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Protease; EC 3.4.21.59; Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 16p13.3

Cellular Component: extracellular matrix; extracellular space; extracellular region

Molecular Function: protein binding; serine-type peptidase activity; serine-type endopeptidase activity

Biological Process: extracellular matrix disassembly; extracellular matrix organization and biogenesis; defense response; proteolysis