Tryptase alpha/beta-1

Details

Name
Tryptase alpha/beta-1
Synonyms
  • 3.4.21.59
  • TPS1
  • TPS2
  • TPSB1
  • Tryptase alpha-1
  • Tryptase I
  • Tryptase-1
Gene Name
TPSAB1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007175|Tryptase alpha/beta-1
MLNLLLLALPVLASRAYAAPAPGQALQRVGIVGGQEAPRSKWPWQVSLRVHGPYWMHFCG
GSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGA
DIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAG
VVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKKP
Number of residues
275
Molecular Weight
30514.93
Theoretical pI
7.12
GO Classification
Functions
serine-type endopeptidase activity / serine-type peptidase activity
Processes
defense response / extracellular matrix disassembly / extracellular matrix organization / proteolysis
Components
extracellular region / extracellular space
General Function
Serine-type peptidase activity
Specific Function
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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0020706|Tryptase alpha/beta-1 (TPSAB1)
ATGCTGAATCTGCTGCTGCTGGCGCTGCCCGTCCTGGCGAGCCGCGCCTACGCGGCCCCT
GCCCCAGGCCAGGCCCTGCAGCGAGTGGGCATCGTCGGGGGTCAGGAGGCCCCCAGGAGC
AAGTGGCCCTGGCAGGTGAGCCTGAGAGTCCACGGCCCATACTGGATGCACTTCTGCGGG
GGCTCCCTCATCCACCCCCAGTGGGTGCTGACCGCAGCGCACTGCGTGGGACCGGACGTC
AAGGATCTGGCCGCCCTCAGGGTGCAACTGCGGGAGCAGCACCTCTACTACCAGGACCAG
CTGCTGCCGGTCAGCAGGATCATCGTGCACCCACAGTTCTACACCGCCCAGATCGGAGCG
GACATCGCCCTGCTGGAGCTGGAGGAGCCGGTGAACGTCTCCAGCCACGTCCACACGGTC
ACCCTGCCCCCTGCCTCAGAGACCTTCCCCCCGGGGATGCCGTGCTGGGTCACTGGCTGG
GGCGATGTGGACAATGATGAGCGCCTCCCACCGCCATTTCCTCTGAAGCAGGTGAAGGTC
CCCATAATGGAAAACCACATTTGTGACGCAAAATACCACCTTGGCGCCTACACGGGAGAC
GACGTCCGCATCGTCCGTGACGACATGCTGTGTGCCGGGAACACCCGGAGGGACTCATGC
CAGGGCGACTCCGGAGGGCCCCTGGTGTGCAAGGTGAATGGCACCTGGCTGCAGGCGGGC
GTGGTCAGCTGGGGCGAGGGCTGTGCCCAGCCCAACCGGCCTGGCATCTACACCCGTGTC
ACCTACTACTTGGACTGGATCCACCACTATGTCCCCAAAAAGCCGTGA
Chromosome Location
16
Locus
16p13.3
External Identifiers
ResourceLink
UniProtKB IDQ15661
UniProtKB Entry NameTRYB1_HUMAN
GenBank Protein ID339981
GenBank Gene IDM33491
HGNC IDHGNC:12019
General References
  1. Miller JS, Westin EH, Schwartz LB: Cloning and characterization of complementary DNA for human tryptase. J Clin Invest. 1989 Oct;84(4):1188-95. [Article]
  2. Vanderslice P, Ballinger SM, Tam EK, Goldstein SM, Craik CS, Caughey GH: Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family. Proc Natl Acad Sci U S A. 1990 May;87(10):3811-5. [Article]
  3. Pallaoro M, Fejzo MS, Shayesteh L, Blount JL, Caughey GH: Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3. J Biol Chem. 1999 Feb 5;274(6):3355-62. [Article]
  4. Jackson NE, Wang HW, Bryant KJ, McNeil HP, Husain A, Liu K, Tedla N, Thomas PS, King GC, Hettiaratchi A, Cairns J, Hunt JE: Alternate mRNA splicing in multiple human tryptase genes is predicted to regulate tetramer formation. J Biol Chem. 2008 Dec 5;283(49):34178-87. doi: 10.1074/jbc.M807553200. Epub 2008 Oct 14. [Article]
  5. Trivedi NN, Tamraz B, Chu C, Kwok PY, Caughey GH: Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations. J Allergy Clin Immunol. 2009 Nov;124(5):1099-105.e1-4. doi: 10.1016/j.jaci.2009.07.026. Epub 2009 Sep 12. [Article]
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  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  8. Cromlish JA, Seidah NG, Marcinkiewicz M, Hamelin J, Johnson DA, Chretien M: Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates. J Biol Chem. 1987 Jan 25;262(3):1363-73. [Article]
  9. Strik MC, Wolbink A, Wouters D, Bladergroen BA, Verlaan AR, van Houdt IS, Hijlkema S, Hack CE, Kummer JA: Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast cells and forms complexes with beta-tryptase monomers. Blood. 2004 Apr 1;103(7):2710-7. Epub 2003 Dec 11. [Article]
  10. Fukuoka Y, Schwartz LB: Active monomers of human beta-tryptase have expanded substrate specificities. Int Immunopharmacol. 2007 Dec 20;7(14):1900-8. Epub 2007 Jul 27. [Article]
  11. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  12. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  13. Marquardt U, Zettl F, Huber R, Bode W, Sommerhoff C: The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region. J Mol Biol. 2002 Aug 16;321(3):491-502. [Article]
  14. Guida M, Riedy M, Lee D, Hall J: Characterization of two highly polymorphic human tryptase loci and comparison with a newly discovered monkey tryptase ortholog. Pharmacogenetics. 2000 Jul;10(5):389-96. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB068481-(1'-{[3-(methylsulfanyl)-2-benzothiophen-1-yl]carbonyl}spiro[1-benzofuran-3,4'-piperidin]-5-yl)methanamineexperimentalunknownDetails
DB068491-[1'-(3-phenylacryloyl)spiro[1-benzofuran-3,4'-piperidin]-5-yl]methanamineexperimentalunknownDetails