TPSB2

Tryptase beta-2, also known as tryptase II, is an enzyme that in humans is encoded by the TPSB2 gene.[5]

TPSB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1A0L, 2BM2, 2FPZ, 2FS8, 2FS9, 2FWW, 2FXR, 2GDD, 2ZA5, 3V7T
Identifiers
Aliases	TPSB2, TPS2, tryptaseB, tryptaseC, tryptase beta 2 (gene/pseudogene), tryptase beta 2
External IDs	OMIM: 191081 MGI: 96942 HomoloGene: 55729 GeneCards: TPSB2
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 1,227,272 bp[1] End 1,230,184 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 A3.3|17 12.53 cM Start 25,366,305 bp[2] End 25,369,098 bp[2]
Gene ontology Molecular function • peptidase activity • serine-type peptidase activity • GO:0001948 protein binding • hydrolase activity • serine-type endopeptidase activity Cellular component • extracellular region • extracellular matrix • extracellular • collagen-containing extracellular matrix Biological process • proteolysis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64499	17229
Ensembl	ENSG00000197253	ENSMUSG00000033825
UniProt	P20231	P21845
RefSeq (mRNA)	NM_024164	NM_010781
RefSeq (protein)	NP_077078	NP_034911
Location (UCSC)	Chr 16: 1.23 – 1.23 Mb	Chr 17: 25.37 – 25.37 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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, beta II and beta III. 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.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000197253 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033825 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: tryptase beta 2 (gene/pseudogene)".

Further reading

• Miller JS, Moxley G, Schwartz LB (1990). "Cloning and characterization of a second complementary DNA for human tryptase". J. Clin. Invest. 86 (3): 864–70. doi:10.1172/JCI114786. PMC 296804. PMID 2203827.
• Hallgren J, Lindahl S, Pejler G (2005). "Structural requirements and mechanism for heparin-dependent activation and tetramerization of human betaI- and betaII-tryptase". J. Mol. Biol. 345 (1): 129–39. doi:10.1016/j.jmb.2004.10.029. PMID 15567416.
• Sommerhoff CP, Bode W, Matschiner G, et al. (2000). "The human mast cell tryptase tetramer: a fascinating riddle solved by structure". Biochim. Biophys. Acta. 1477 (1–2): 75–89. doi:10.1016/s0167-4838(99)00265-4. PMID 10708850.
• Huang C, Li L, Krilis SA, et al. (1999). "Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft". J. Biol. Chem. 274 (28): 19670–6. doi:10.1074/jbc.274.28.19670. PMID 10391906.
• Caughey GH, Raymond WW, Blount JL, et al. (2000). "Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families". J. Immunol. 164 (12): 6566–75. doi:10.4049/jimmunol.164.12.6566. PMID 10843716.
• Vanderslice P, Ballinger SM, Tam EK, et al. (1990). "Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family". Proc. Natl. Acad. Sci. U.S.A. 87 (10): 3811–5. doi:10.1073/pnas.87.10.3811. PMC 53993. PMID 2187193.
• Guida M, Riedy M, Lee D, Hall J (2000). "Characterization of two highly polymorphic human tryptase loci and comparison with a newly discovered monkey tryptase ortholog". Pharmacogenetics. 10 (5): 389–96. doi:10.1097/00008571-200007000-00002. PMID 10898108.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Blom T, Hellman L (1993). "Characterization of a tryptase mRNA expressed in the human basophil cell line KU812". Scand. J. Immunol. 37 (2): 203–8. doi:10.1111/j.1365-3083.1993.tb01757.x. PMID 8434231.
• Pallaoro M, Fejzo MS, Shayesteh L, et al. (1999). "Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3". J. Biol. Chem. 274 (6): 3355–62. doi:10.1074/jbc.274.6.3355. PMID 9920877.
• Caughey GH (2002). "New developments in the genetics and activation of mast cell proteases". Mol. Immunol. 38 (16–18): 1353–7. doi:10.1016/S0161-5890(02)00087-1. PMID 12217407.
• Akin C, Soto D, Brittain E, et al. (2007). "Tryptase haplotype in mastocytosis: relationship to disease variant and diagnostic utility of total tryptase levels". Clin. Immunol. 123 (3): 268–71. doi:10.1016/j.clim.2007.02.007. PMC 1949411. PMID 17449330.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Sommerhoff CP, Bode W, Pereira PJ, et al. (1999). "The structure of the human betaII-tryptase tetramer: fo(u)r better or worse". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 10984–91. doi:10.1073/pnas.96.20.10984. PMC 34230. PMID 10500112.
• Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
• Trivedi NN, Tamraz B, Chu C, et al. (2009). "Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations". J. Allergy Clin. Immunol. 124 (5): 1099–1105.e4. doi:10.1016/j.jaci.2009.07.026. PMC 2783561. PMID 19748655.
• Pereira PJ, Bergner A, Macedo-Ribeiro S, et al. (1998). "Human beta-tryptase is a ring-like tetramer with active sites facing a central pore". Nature. 392 (6673): 306–11. doi:10.1038/32703. PMID 9521329. S2CID 4421972.
• Wu C, Ma MH, Brown KR, et al. (2007). "Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening". Proteomics. 7 (11): 1775–85. doi:10.1002/pmic.200601006. PMID 17474147.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.