NameCationic trypsin
Synonyms
  • 3.4.21.4
  • Beta-trypsin
Gene NameNot Available
OrganismBovine
Amino acid sequence
>lcl|BSEQ0013602|Cationic trypsin
MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVS
AAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLN
SRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQIT
SNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIK
QTIASN
Number of residues246
Molecular Weight25785.025
Theoretical pINot Available
GO Classification
Functions
  • metal ion binding
  • serine-type endopeptidase activity
Processes
  • digestion
  • proteolysis
Components
  • extracellular space
General FunctionSerine-type endopeptidase activity
Specific FunctionNot Available
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP00760
UniProtKB Entry NameTRY1_BOVIN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0013603|Cationic trypsin
ATGAAGACCTTCATCTTTCTAGCTCTCCTGGGAGCTGCTGTTGCTTTCCCTGTGGACGAT
GATGACAAGATCGTGGGCGGCTACACCTGTGGGGCAAATACTGTCCCCTACCAAGTGTCC
CTGAACTCTGGCTACCACTTCTGCGGGGGCTCCCTCATCAACAGCCAGTGGGTGGTGTCT
GCGGCTCACTGCTACAAGTCCGGAATCCAAGTGCGTCTGGGAGAAGACAACATTAATGTC
GTTGAGGGCAATGAGCAATTCATCAGCGCATCCAAGAGCATCGTCCATCCCAGCTACAAC
TCAAACACCTTAAACAACGACATCATGCTGATTAAACTGAAATCAGCTGCCAGTCTCAAC
AGCCGAGTAGCCTCTATCTCTCTGCCAACATCCTGTGCCTCTGCTGGCACCCAGTGTCTC
ATCTCTGGCTGGGGCAACACCAAAAGCAGTGGCACCAGCTACCCTGATGTCCTGAAGTGT
CTGAAGGCTCCCATCCTATCAGACAGCTCTTGCAAAAGTGCCTACCCAGGCCAGATCACC
AGCAACATGTTCTGTGCGGGCTACCTGGAGGGCGGAAAGGACTCCTGCCAGGGTGACTCC
GGTGGCCCTGTGGTCTGCAGTGGAAAGCTCCAGGGCATTGTCTCCTGGGGCTCTGGCTGC
GCTCAGAAAAACAAGCCTGGTGTCTACACCAAGGTCTGCAACTACGTGAGCTGGATTAAG
CAGACCATCGCCTCCAACTAA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Mikes O, Holeysovsky V, Tomasek V, Sorm F: Covalent structure of bovine trypsinogen. The position of the remaining amides. Biochem Biophys Res Commun. 1966 Aug 12;24(3):346-52. 5967094
  2. Hartley BS: Homologies in serine proteinases. Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):77-87. 4399051
  3. Titani K, Ericsson LH, Neurath H, Walsh KA: Amino acid sequence of dogfish trypsin. Biochemistry. 1975 Apr 8;14(7):1358-66. 1092332
  4. Sahin-Toth M, Kukor Z, Nemoda Z: Human cationic trypsinogen is sulfated on Tyr154. FEBS J. 2006 Nov;273(22):5044-50. 17087724
  5. Kauffman DL: The disulphide bridges of trypsin. J Mol Biol. 1965 Jul;12(3):929-32. 5892911
  6. Bode W, Schwager P: The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J Mol Biol. 1975 Nov 15;98(4):693-717. 512
  7. Kossiakoff AA, Chambers JL, Kay LM, Stroud RM: Structure of bovine trypsinogen at 1.9 A resolution. Biochemistry. 1977 Feb 22;16(4):654-64. 556951
  8. Conners R, Konarev AV, Forsyth J, Lovegrove A, Marsh J, Joseph-Horne T, Shewry P, Brady RL: An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.). J Biol Chem. 2007 Sep 21;282(38):27760-8. Epub 2007 Jul 19. 17640870
  9. Millers EK, Johnson LA, Birrell GW, Masci PP, Lavin MF, de Jersey J, Guddat LW: The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. PLoS One. 2013;8(1):e54104. doi: 10.1371/journal.pone.0054104. Epub 2013 Jan 15. 23335990