Trypsin-3

Details

Name
Trypsin-3
Synonyms
  • 3.4.21.4
  • Brain trypsinogen
  • Mesotrypsinogen
  • PRSS4
  • Serine protease 3
  • Serine protease 4
  • TRY3
  • TRY4
  • Trypsin III
  • Trypsin IV
Gene Name
PRSS3
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037144|Trypsin-3
MCGPDDRCPARWPGPGRAVKCGKGLAAARPGRVERGGAQRGGAGLELHPLLGGRTWRAAR
DADGCEALGTVAVPFDDDDKIVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAH
CYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARV
STISLPTTPPAAGTECLISGWGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDSGGPVVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTI
AANS
Number of residues
304
Molecular Weight
32528.565
Theoretical pI
7.54
GO Classification
Functions
calcium ion binding / serine-type endopeptidase activity / serine-type peptidase activity
Processes
cobalamin metabolic process / digestion / endothelial cell migration / innate immune response / proteolysis / small molecule metabolic process / vitamin metabolic process / water-soluble vitamin metabolic process / zymogen activation
Components
extracellular exosome / extracellular region / extracellular space
General Function
Serine-type peptidase activity
Specific Function
Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0016483|Trypsin-3 (PRSS3)
ATGCACATGAGAGAGACAAGTGGCTTCACATTGAAGAAGGGGAGGAGTGCGCCATTGGTT
TTCCATCCTCCAGATGCACTGATTGCTGTCCCCTTTGACGATGATGACAAGATTGTTGGG
GGCTACACCTGTGAGGAGAATTCTCTCCCCTACCAGGTGTCCCTGAATTCTGGCTCCCAC
TTCTGCGGTGGCTCCCTCATCAGCGAACAGTGGGTGGTATCAGCAGCTCACTGCTACAAG
ACCCGCATCCAGGTGAGACTGGGAGAGCACAACATCAAAGTCCTGGAGGGGAATGAGCAG
TTCATCAATGCGGCCAAGATCATCCGCCACCCTAAATACAACAGGGACACTCTGGACAAT
GACATCATGCTGATCAAACTCTCCTCACCTGCCGTCATCAATGCCCGCGTGTCCACCATC
TCTCTGCCCACCGCCCCTCCAGCTGCTGGCACTGAGTGCCTCATCTCCGGCTGGGGCAAC
ACTCTGAGCTTTGGTGCTGACTACCCAGACGAGCTGAAGTGCCTGGATGCTCCGGTGCTG
ACCCAGGCTGAGTGTAAAGCCTCCTACCCTGGAAAGATTACCAACAGCATGTTCTGTGTG
GGCTTCCTTGAGGGAGGCAAGGATTCCTGCCAGCGTGACTCTGGTGGCCCTGTGGTCTGC
AACGGACAGCTCCAAGGAGTTGTCTCCTGGGGCCATGGCTGTGCCTGGAAGAACAGGCCT
GGAGTCTACACCAAGGTCTACAACTATGTGGACTGGATTAAGGACACCATCGCTGCCAAC
AGCTAA
Chromosome Location
9
Locus
9p11.2
External Identifiers
ResourceLink
UniProtKB IDP35030
UniProtKB Entry NameTRY3_HUMAN
GenBank Protein ID6066378
GenBank Gene IDX72781
GenAtlas IDPRSS3
HGNC IDHGNC:9486
General References
  1. Wiegand U, Corbach S, Minn A, Kang J, Muller-Hill B: Cloning of the cDNA encoding human brain trypsinogen and characterization of its product. Gene. 1993 Dec 22;136(1-2):167-75. [Article]
  2. Tani T, Kawashima I, Mita K, Takiguchi Y: Nucleotide sequence of the human pancreatic trypsinogen III cDNA. Nucleic Acids Res. 1990 Mar 25;18(6):1631. [Article]
  3. Nakanishi J, Yamamoto M, Koyama J, Sato J, Hibino T: Keratinocytes synthesize enteropeptidase and multiple forms of trypsinogen during terminal differentiation. J Invest Dermatol. 2010 Apr;130(4):944-52. doi: 10.1038/jid.2009.364. Epub 2009 Nov 19. [Article]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [Article]
  5. 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]
  6. Ghosh D, Porter E, Shen B, Lee SK, Wilk D, Drazba J, Yadav SP, Crabb JW, Ganz T, Bevins CL: Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol. 2002 Jun;3(6):583-90. Epub 2002 May 20. [Article]
  7. Szmola R, Kukor Z, Sahin-Toth M: Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitors. J Biol Chem. 2003 Dec 5;278(49):48580-9. Epub 2003 Sep 24. [Article]
  8. Katona G, Berglund GI, Hajdu J, Graf L, Szilagyi L: Crystal structure reveals basis for the inhibitor resistance of human brain trypsin. J Mol Biol. 2002 Feb 1;315(5):1209-18. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB023084-(1,3,2-Dioxaborolan-2-Yloxy)Butan-1-AminiumexperimentalunknownDetails
DB025414-Hydroxybutan-1-AminiumexperimentalunknownDetails
DB025854-(Hydroxymethyl)BenzamidineexperimentalunknownDetails
DB03637Guanidine-3-propanolexperimentalunknownDetails
DB043691,3,2-Dioxaborolan-2-OlexperimentalunknownDetails
DB03127BenzamidineexperimentalunknownDetails
DB03129Diamino-N-[3-(1,3,2-dioxaborolan-2-yloxy)propyl]methaniminiumexperimentalunknownDetails
DB04109[4-(1,3,2-Dioxaborolan-2-Yloxy)Methyl]BenzamidineexperimentalunknownDetails