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TPSG1
Identifiers
Aliases	TPSG1, PRSS31, TMT, trpA, tryptase gamma 1
External IDs	OMIM: 609341; MGI: 1349391; HomoloGene: 74994; GeneCards: TPSG1; OMA:TPSG1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16p13.3 Start 1,221,651 bp End 1,225,268 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17 A3.3|17 12.53 cM Start 25,588,247 bp End 25,593,416 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon jejunal mucosa mucosa of sigmoid colon muscle layer of sigmoid colon duodenum Pituitary Gland testicle anterior pituitary left ovary rectum Top expressed in intestinal villus ileum jejunum morula left colon duodenum lip dentate gyrus of hippocampal formation granule cell dermis precursor cell More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity Cellular component integral component of membrane integral component of plasma membrane membrane extracellular space Biological process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 25823 26945 Ensembl ENSG00000116176 ENSMUSG00000033200 UniProt Q9NRR2 Q9QUL7 RefSeq (mRNA) NM_012467 NM_012034 NM_001357726 RefSeq (protein) NP_036599 n/a Location (UCSC) Chr 16: 1.22 – 1.23 Mb Chr 17: 25.59 – 25.59 Mb PubMed search
Wikidata
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Tryptase gamma, also known as serine protease 31 or transmembrane tryptase, is an enzyme that in humans is encoded by the TPSG1 gene.

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. There is uncertainty regarding the number of genes in this cluster. Currently four functional genes - alpha I, beta I, beta II and gamma I - have been identified. And beta I has an allelic variant named alpha II, beta II has an allelic variant beta III, also gamma I has an allelic variant gamma II. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha-tryptases predominant. This gene differs from other members of the tryptase gene family in that it has C-terminal hydrophobic domain, which may serve as a membrane anchor. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000116176 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000033200 – 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 gamma 1".

Further reading

• 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.
• 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.
• Wong GW, Foster PS, Yasuda S, et al. (2002). "Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway". J. Biol. Chem. 277 (44): 41906–15. doi:10.1074/jbc.M205868200. PMID 12194977.
• 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.
• Wong GW, Tang Y, Feyfant E, et al. (1999). "Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension". J. Biol. Chem. 274 (43): 30784–93. doi:10.1074/jbc.274.43.30784. PMID 10521469.
• Xiang M, Gu Y, Zhao F, et al. (2010). "Mast cell tryptase promotes breast cancer migration and invasion". Oncol. Rep. 23 (3): 615–9. doi:10.3892/or_00000676. PMID 20126998.

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

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