PRSS2

Protein-coding gene in the species Homo sapiens
PRSS2
Identifiers
AliasesPRSS2, TRY2, TRY8, TRYP2, protease, serine 2, serine protease 2
External IDsOMIM: 601564; MGI: 102759; HomoloGene: 122141; GeneCards: PRSS2; OMA:PRSS2 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for PRSS2
Genomic location for PRSS2
Band7q34Start142,760,398 bp[1]
End142,774,564 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for PRSS2
Genomic location for PRSS2
Band6|6 B1Start41,498,721 bp[2]
End41,502,013 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • islet of Langerhans

  • duodenum

  • testicle

  • fundus

  • ectocervix

  • right coronary artery

  • body of stomach

  • canal of the cervix

  • right uterine tube
Top expressed in
  • pyloric antrum

  • islet of Langerhans

  • pancreatic acinus

  • duodenum

  • sexually immature organism

  • mucous cell of stomach

  • masseter muscle

  • intercostal muscle

  • brown adipose tissue

  • quadriceps femoris muscle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • calcium ion binding
  • peptidase activity
  • protein binding
  • hydrolase activity
  • metal ion binding
  • serine-type endopeptidase activity
  • serine-type peptidase activity
  • metalloendopeptidase activity
Cellular component
  • extracellular matrix
  • extracellular region
  • extracellular space
  • azurophil granule lumen
Biological process
  • collagen catabolic process
  • digestion
  • positive regulation of cell growth
  • extracellular matrix disassembly
  • proteolysis
  • positive regulation of cell adhesion
  • antimicrobial humoral response
  • neutrophil degranulation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5645

22072

Ensembl

ENSG00000282049
ENSG00000275896

ENSMUSG00000057163

UniProt

P07478

P07146

RefSeq (mRNA)

NM_001303414
NM_002770

NM_009430

RefSeq (protein)

NP_001290343
NP_002761

NP_033456

Location (UCSC)Chr 7: 142.76 – 142.77 MbChr 6: 41.5 – 41.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protease, serine, 2 (trypsin 2) is a protein that in humans is encoded by the PRSS2 gene.[5]

Function

This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7. [provided by RefSeq, Jul 2008].

References

  1. ^ a b c ENSG00000275896 GRCh38: Ensembl release 89: ENSG00000282049, ENSG00000275896 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000057163 – 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.
  5. ^ "Entrez Gene: Protease, serine, 2 (trypsin 2)".

Further reading

  • Williams SJ, Gotley DC, Antalis TM (July 2001). "Human trypsinogen in colorectal cancer". International Journal of Cancer. 93 (1): 67–73. doi:10.1002/ijc.1304. PMID 11391623. S2CID 22649653.
  • Mayumi T, Inui K, Maetani I, Yokoe M, Sakamoto T, Yoshida M, Ko S, Hirata K, Takada T (August 2012). "Validity of the urinary trypsinogen-2 test in the diagnosis of acute pancreatitis". Pancreas. 41 (6): 869–75. doi:10.1097/MPA.0b013e3182480ab7. PMID 22481290. S2CID 24109182.
  • Shelton, C.; Solomon, S.; Larusch, J.; Whitcomb, D. C.; Adam, M. P.; Ardinger, H. H.; Pagon, R. A.; Wallace, S. E.; Bean LJH; Stephens, K.; Amemiya, A. (1993). "PRSS1-Related Hereditary Pancreatitis". PMID 22379635. {{cite journal}}: Cite journal requires |journal= (help)
  • Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". Journal of Proteome Research. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.
  • Vilen ST, Suojanen J, Salas F, Risteli J, Ylipalosaari M, Itkonen O, Koistinen H, Baumann M, Stenman UH, Sorsa T, Salo T, Nyberg P (October 2012). "Trypsin-2 enhances carcinoma invasion by processing tight junctions and activating ProMT1-MMP". Cancer Investigation. 30 (8): 583–92. doi:10.3109/07357907.2012.716467. PMID 22909050. S2CID 29172202.
  • Lempinen M, Isoniemi H, Mäkisalo H, Nordin A, Halme L, Arola J, Höckerstedt K, Stenman UH (November 2007). "Enhanced detection of cholangiocarcinoma with serum trypsinogen-2 in patients with severe bile duct strictures". Journal of Hepatology. 47 (5): 677–83. doi:10.1016/j.jhep.2007.05.017. PMID 17640760.
  • Galey D, Becker K, Haughey N, Kalehua A, Taub D, Woodward J, Mattson MP, Nath A (June 2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". Journal of Neurovirology. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
  • Baptista AM, Jonson PH, Hough E, Petersen SB (September 1998). "The origin of trypsin: evidence for multiple gene duplications in trypsins". Journal of Molecular Evolution. 47 (3): 353–62. Bibcode:1998JMolE..47..353B. doi:10.1007/PL00006393. PMID 9732462. S2CID 15271694.
  • Gao J, Zhu F, Lv S, Li Z, Ling Z, Gong Y, Jie C, Ma L (June 2010). "Identification of pancreatic juice proteins as biomarkers of pancreatic cancer". Oncology Reports. 23 (6): 1683–92. doi:10.3892/or_00000812. PMID 20428826.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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