Aliases for TPSAB1 Gene
External Ids for TPSAB1 Gene
Previous HGNC Symbols for TPSAB1 Gene
Previous GeneCards Identifiers for TPSAB1 Gene
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]
GeneCards Summary for TPSAB1 Gene
TPSAB1 (Tryptase Alpha/Beta 1) is a Protein Coding gene. Diseases associated with TPSAB1 include Candida Glabrata and Amebiasis. Among its related pathways are Degradation of the extracellular matrix and Matrix Metalloproteinases. GO annotations related to this gene include serine-type endopeptidase activity and serine-type peptidase activity. An important paralog of this gene is TPSB2.
UniProtKB/Swiss-Prot for TPSAB1 Gene
Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315).