Kallikrein-5, formerly known as stratum corneum tryptic enzyme (SCTE), is a serine protease expressed in the epidermis. In humans it is encoded by the KLK5 gene.[5][6][7][8][9][10] This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Its expression is up-regulated by estrogens and progestins. Alternative splicing results in multiple transcript variants encoding the same protein.[10]

KLK5
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesKLK5, KLK-L2, KLKL2, SCTE, kallikrein related peptidase 5
External IDsOMIM: 605643; MGI: 1915918; HomoloGene: 75000; GeneCards: KLK5; OMA:KLK5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001077491
NM_001077492
NM_012427

NM_026806

RefSeq (protein)

NP_001070959
NP_001070960
NP_036559

n/a

Location (UCSC)Chr 19: 50.94 – 50.95 MbChr 7: 43.49 – 43.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

KLK5 has been suggested to regulate cell shedding (desquamation) in conjunction with KLK7 and KLK14, given its ability to degrade proteins which form the extracellular component of cell junctions in the stratum corneum. It is proposed that KLK5 regulates this process since it is able to self-activate in addition to activating KLK7 and KLK14.[11]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167754Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074155Ensembl, 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. ^ Brattsand M, Egelrud T (Nov 1999). "Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation". J Biol Chem. 274 (42): 30033–40. doi:10.1074/jbc.274.42.30033. PMID 10514489.
  6. ^ Yousef GM, Diamandis EP (Feb 2000). "The new kallikrein-like gene, KLK-L2. Molecular characterization, mapping, tissue expression, and hormonal regulation". J Biol Chem. 274 (53): 37511–6. doi:10.1074/jbc.274.53.37511. PMID 10608802.
  7. ^ Zulkifli SN, Paine LL, Greener DL, Subramaniam R (Oct 1991). "Trends in selected obstetric complications from University Hospital, Kuala Lumpur, Malaysia". Int J Gynaecol Obstet. 35 (1): 29–36. doi:10.1016/0020-7292(91)90059-E. PMID 1680072. S2CID 46529409.
  8. ^ Diamandis, Eleftherios P.; Deperthes, David; Lundwall, Åke (Jun 2006). "Proceedings of the 1st International Symposium on Kallikreins, Lausanne, Switzerland, September 1-3, 2005". Biol Chem. 387 (6): 635–824. doi:10.1515/BC.2006.081. PMID 16800723. S2CID 83910246.
  9. ^ Yamasaki K, Schauber J, Coda A, Lin H, Dorschner RA, Schechter NM, Bonnart C, Descargues P, Hovnanian A, Gallo RL (Oct 2006). "Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin". FASEB J. 20 (12): 2068–80. doi:10.1096/fj.06-6075com. PMID 17012259. S2CID 18170331.
  10. ^ a b "Entrez Gene: KLK5 kallikrein-related peptidase 5".
  11. ^ Brattsand M, Stefansson K, Lundh C, et al. (2005). "A proteolytic cascade of kallikreins in the stratum corneum". J. Invest. Dermatol. 124 (1): 198–203. doi:10.1111/j.0022-202X.2004.23547.x. PMID 15654974.

Further reading

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  • The MEROPS online database for peptidases and their inhibitors: S01.017