TPSAB1

TPSAB1
Available structures
PDB	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 Contents Function ; References ; Further reading ;
Identifiers
Aliases	TPSAB1 , TPS1, TPS2, TPSB1, tryptase alpha/beta 1, TPSB2, Tryptase-2
External IDs	OMIM: 191080 MGI: 96942 HomoloGene: 55729 GeneCards: TPSAB1
Gene location (Human)
Chr.	Chromosome 16 (human)
End	1,242,554 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	25,588,072 bp
RNA expression pattern
	Top expressed in
	gallbladder; ; fundus; ; duodenum; ; right lung; ; upper lobe of left lung; ; gastric mucosa; ; right coronary artery; ; body of stomach; ; urinary bladder; ; subcutaneous adipose tissue;
	Top expressed in
	dermis; ; lip; ; foreskin; ; extraocular muscle; ; skin of back; ; ankle; ; gastric mucosa; ; mucous cell of stomach; ; skin of abdomen; ; sciatic nerve;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	peptidase activity ; serine-type peptidase activity ; protein binding ; hydrolase activity ; serine-type endopeptidase activity ; identical protein binding ;
Cellular component	extracellular region ; extracellular matrix ; extracellular space ; collagen-containing extracellular matrix ;
Biological process	proteolysis ; defense response ; extracellular matrix disassembly ;
	Sources:Amigo / QuickGO
Orthologs
	7177
	17229
	ENSG00000172236
	ENSMUSG00000033825
	P20231 ; Q15661
	P21845
	NM_003294
	NM_010781
	NP_077078 ; NP_003285
	NP_034911
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 23, 2023

Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene.^[5]^[6] Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate.^[7]

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.^[7]

Related Research Articles

<span class="mw-page-title-main">Tryptase</span> Class of enzymes

Tryptase is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. Club cells contain tryptase, which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.

Granzyme A is a tryptase and is one of the five granzymes encoded in the human genome. In humans, GzmA is encoded by the GZMA gene in proximity to the GZMK gene on chromosome 5. This enzyme is present in cytotoxic T lymphocyte (CTL) granules.

CD11c, also known as Integrin, alpha X (ITGAX), is a gene that encodes for CD11c.

CD1D is the human gene that encodes the protein CD1d, a member of the CD1 family of glycoproteins expressed on the surface of various human antigen-presenting cells. They are non-classical MHC proteins, related to the class I MHC proteins, and are involved in the presentation of lipid antigens to T cells. CD1d is the only member of the group 2 CD1 molecules.

<span class="mw-page-title-main">CXCL5</span> Mammalian protein found in Homo sapiens

C-X-C motif chemokine 5 is a protein that in humans is encoded by the CXCL5 gene.

<span class="mw-page-title-main">Chymase</span> Class of enzymes

Chymases are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes. Recently, Derakhshan et al. reported that a specific mast cell population expressed transcripts for Mcpt8. They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by connective tissue-type mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response, and chymase mcp1 and mcp2 are used for marker for mast cell degranulation in parasite infection such as Nematode, Trichuris muris Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis.

CD49d is an integrin alpha subunit. It makes up half of the α4β1 lymphocyte homing receptor.

<span class="mw-page-title-main">HLA-DRB5</span> Protein-coding gene in the species Homo sapiens

HLA class II histocompatibility antigen, DRB5 beta chain is a protein that in humans is encoded by the HLA-DRB5 gene.

Chymase is an enzyme that in humans is encoded by the CMA1 gene.

Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide, also known as FCER1A, is a protein which in humans is encoded by the FCER1A gene.

<span class="mw-page-title-main">Major histocompatibility complex, class II, DQ alpha 1</span> Protein-coding gene in the species Homo sapiens

Major histocompatibility complex, class II, DQ alpha 1, also known as HLA-DQA1, is a human gene present on short arm of chromosome 6 (6p21.3) and also denotes the genetic locus which contains this gene. The protein encoded by this gene is one of two proteins that are required to form the DQ heterodimer, a cell surface receptor essential to the function of the immune system.

C-C chemokine receptor type 3 is a protein that in humans is encoded by the CCR3 gene.

Chemokine-binding protein 2 is a protein that in humans is encoded by the CCBP2 gene.

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4 is an enzyme that in humans is encoded by the PLCB4 gene.

Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 gene. The "CPA3" gene expression has only been detected in mast cells and mast-cell-like lines, and CPA3 is located in secretory granules. CPA3 is one of 8-9 members of the A/B subfamily that includes the well-studied pancreatic enzymes carboxypeptidase A1 (CPA1), carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. The enzyme now called CPA3 was originally named mast cell carboxypeptidase A, and another protein was initially called CPA3. A gene nomenclature committee renamed mast cell carboxypeptidase A as CPA3, and the original CPA3 reported by Huang et al. became CPA4 to reflect the order of their discovery.

CD79b molecule, immunoglobulin-associated beta, also known as CD79B, is a human gene.

Tryptase delta is an enzyme that in humans is encoded by the TPSD1 gene.

Tryptase beta-2, also known as tryptase II, is a proteolytic enzyme that in humans is encoded by the TPSB2 gene.

Tryptase gamma, also known as serine protease 31 or transmembrane tryptase, is an enzyme that in humans is encoded by the TPSG1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000172236 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033825 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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. Bibcode:1990PNAS...87.3811V. 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. doi:10.4049/jimmunol.135.4.2762. 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. doi:10.4049/jimmunol.126.4.1290. 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. doi:10.4049/jimmunol.154.10.5472. 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. S2CID 22041090.
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. doi:10.4049/jimmunol.156.1.275. 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. doi:10.4049/jimmunol.159.6.2911. PMID 9300715. S2CID 45026410.
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. Bibcode:1998Natur.392..306P. doi:10.1038/32703. PMID 9521329. S2CID 4421972.
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. Bibcode:1999PNAS...9610984S. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000172236 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid2203827-5] 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.

[pmid9920877-6] 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.

[entrez-7] 1 2 "Entrez Gene: TPSAB1 tryptase alpha/beta 1".

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v t e 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/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

TPSAB1

Contents

Function

Related Research Articles

References

Further reading