TPSAB1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1A0L, 2BM2, 2FPZ, 2FS8, 2FS9, 2FWW, 2FXR, 2GDD, 2ZA5, 3V7T,%%s1LTO, 2F9N, 2F9O, 2F9P, 2ZEB, 2ZEC, 4A6L, 4MPU, 4MPV, 4MPW, 4MPX, 4MQA, 5F03

Identifiers

Aliases

TPSAB1, TPS1, TPS2, TPSB1, tryptase alpha/beta 1

External IDs

MGI: 96942 HomoloGene: 55729 GeneCards: TPSAB1

Targeted by Drug

gabexate, nafamostat^[1]

Gene ontology
Molecular function	• peptidase activity • serine-type peptidase activity • protein binding • hydrolase activity • serine-type endopeptidase activity
Cellular component	• extracellular region • extracellular matrix • extracellular fluid
Biological process	• proteolysis • defense response • extracellular matrix disassembly
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


7177


17229

Ensembl


ENSG00000172236


ENSMUSG00000033825

UniProt


P20231 Q15661


P21845

RefSeq (mRNA)


NM_003294


NM_010781

RefSeq (protein)


NP_003285.2 NP_077078.5 NP_003285.2


n/a

Location (UCSC)

Chr 16: 1.24 – 1.24 Mb

Chr 17: 25.37 – 25.37 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene.^[4]^[5] Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate.^[6]

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, alpha and beta 1.Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.^[6]

References

↑ "Drugs that physically interact with Tryptase alpha/beta-1 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Miller JS, Moxley G, Schwartz LB (Oct 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.
↑ Pallaoro M, Fejzo MS, Shayesteh L, Blount JL, Caughey GH (Feb 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.
1 2 "Entrez Gene: TPSAB1 tryptase alpha/beta 1".

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.
Kam CM, Hudig D, Powers JC (2000). "Granzymes (lymphocyte serine proteases): characterization with natural and synthetic substrates and inhibitors". Biochim. Biophys. Acta. 1477 (1–2): 307–23. doi:10.1016/s0167-4838(99)00282-4. PMID 10708866.
Caughey GH (2003). "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.
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.
Miller JS, Westin EH, Schwartz LB (1989). "Cloning and characterization of complementary DNA for human tryptase". J. Clin. Invest. 84 (4): 1188–95. doi:10.1172/JCI114284. PMC 329777. PMID 2677049.
Schwartz LB, Bradford TR, Littman BH, Wintroub BU (1985). "The fibrinogenolytic activity of purified tryptase from human lung mast cells". J. Immunol. 135 (4): 2762–7. PMID 3161948.
Schwartz LB, Lewis RA, Seldin D, Austen KF (1981). "Acid hydrolases and tryptase from secretory granules of dispersed human lung mast cells". J. Immunol. 126 (4): 1290–4. PMID 7009736.
Xia HZ, Kepley CL, Sakai K, et al. (1995). "Quantitation of tryptase, chymase, Fc epsilon RI alpha, and Fc epsilon RI gamma mRNAs in human mast cells and basophils by competitive reverse transcription-polymerase chain reaction". J. Immunol. 154 (10): 5472–80. PMID 7730649.
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.
Cairns JA, Walls AF (1996). "Mast cell tryptase is a mitogen for epithelial cells. Stimulation of IL-8 production and intercellular adhesion molecule-1 expression". J. Immunol. 156 (1): 275–83. PMID 8598474.
Schwartz LB, Sakai K, Bradford TR, et al. (1996). "The alpha form of human tryptase is the predominant type present in blood at baseline in normal subjects and is elevated in those with systemic mastocytosis". J. Clin. Invest. 96 (6): 2702–10. doi:10.1172/JCI118337. PMC 185977. PMID 8675637.
Cairns JA, Walls AF (1997). "Mast cell tryptase stimulates the synthesis of type I collagen in human lung fibroblasts". J. Clin. Invest. 99 (6): 1313–21. doi:10.1172/JCI119290. PMC 507947. PMID 9077541.
Xia HZ, Du Z, Craig S, et al. (1997). "Effect of recombinant human IL-4 on tryptase, chymase, and Fc epsilon receptor type I expression in recombinant human stem cell factor-dependent fetal liver-derived human mast cells". J. Immunol. 159 (6): 2911–21. PMID 9300715.
Thomas VA, Wheeless CJ, Stack MS, Johnson DA (1998). "Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption". Biochemistry. 37 (8): 2291–8. doi:10.1021/bi972119z. PMID 9485375.
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.
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.
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.
Romagnani P, De Paulis A, Beltrame C, et al. (1999). "Tryptase-chymase double-positive human mast cells express the eotaxin receptor CCR3 and are attracted by CCR3-binding chemokines". Am. J. Pathol. 155 (4): 1195–204. doi:10.1016/S0002-9440(10)65222-4. PMC 1867029. PMID 10514402.

PDB gallery

1a0l: HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE

1lto: Human alpha1-tryptase

2bm2: HUMAN BETA-II TRYPTASE IN COMPLEX WITH 4-(3-AMINOMETHYL-PHENYL)-PIPERIDIN-1-YL-(5-PHENETHYL- PYRIDIN-3-YL)-METHANONE

2f9n: Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant K192Q/D216G in Complex with Leupeptin

2f9o: Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G

2f9p: Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin

2fpz: Human tryptase with 2-amino benzimidazole

2fs8: Human beta-tryptase II with inhibitor CRA-29382

2fs9: Human beta tryptase II with inhibitor CRA-28427

2fww: human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme

2fxr: human beta tryptase II complexed with activated ketone inhibitor CRA-29382

2gdd: Human beta II tryptase with inhibitor CRA-27592

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)

Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic

Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator

Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase

Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin

Venombin	Ancrod Batroxobin

Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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TPSAB1

Function

References

Further reading