KLK5

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
2PSX, 2PSY

Identifiers

Aliases

KLK5, KLK-L2, KLKL2, SCTE, kallikrein related peptidase 5

External IDs

MGI: 1915918 HomoloGene: 75000 GeneCards: KLK5

Gene ontology
Molecular function	• protein binding • hydrolase activity • peptidase activity • serine-type peptidase activity • endopeptidase activity • serine-type endopeptidase activity
Cellular component	• epidermal lamellar body • extracellular region • extracellular space • cytosol
Biological process	• positive regulation of antibacterial peptide production • positive regulation of G-protein coupled receptor protein signaling pathway • proteolysis • epidermis development • cornification
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


25818


68668

Ensembl


ENSG00000167754


ENSMUSG00000074155

UniProt


Q9Y337


n/a

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 Mb

Chr 7: 43.84 – 43.85 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Kallikrein-related peptidase 5 (KLK5), 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.^[3]^[4]^[5]^[6]^[7]^[8]^[9] 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.^[9]

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.^[10]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 10514489. doi:10.1074/jbc.274.42.30033.
↑ 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. PMID 10608802. doi:10.1074/jbc.274.53.37511.
↑ 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. PMID 1680072. doi:10.1016/0020-7292(91)90059-E.
↑ Wiesmann UN, DiDonato S, Herschkowitz NN (Jan 1976). "Effect of chloroquine on cultured fibroblasts: release of lysosomal hydrolases and inhibition of their uptake". Biochem Biophys Res Commun. 66 (4): 1338–43. PMID 4. doi:10.1016/0006-291X(75)90506-9.
↑ 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. PMID 16800723. doi:10.1515/BC.2006.081.
↑ 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. PMID 17012259. doi:10.1096/fj.06-6075com.
1 2 "Entrez Gene: KLK5 kallikrein-related peptidase 5".
↑ 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. PMID 15654974. doi:10.1111/j.0022-202X.2004.23547.x.

Li, S; Garcia, M; Gewiss, RL; Winuthayanon, W (April 2017). "Crucial role of estrogen for the mammalian female in regulating semen coagulation and liquefaction in vivo.". PLoS genetics. 13 (4): e1006743. PMID 28414719.
Diamandis EP, Yousef GM, Luo LY, et al. (2001). "The new human kallikrein gene family: implications in carcinogenesis.". Trends Endocrinol. Metab. 11 (2): 54–60. PMID 10675891. doi:10.1016/S1043-2760(99)00225-8.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene. 138 (1–2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3.
Yousef GM, Luo LY, Diamandis EP (2000). "Identification of novel human kallikrein-like genes on chromosome 19q13.3-q13.4". Anticancer Res. 19 (4B): 2843–52. PMID 10652563.
Harvey TJ, Hooper JD, Myers SA, et al. (2001). "Tissue-specific expression patterns and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4". J. Biol. Chem. 275 (48): 37397–406. PMID 10969073. doi:10.1074/jbc.M004525200.
Gan L, Lee I, Smith R, et al. (2001). "Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region". Gene. 257 (1): 119–30. PMID 11054574. doi:10.1016/S0378-1119(00)00382-6.
Kim H, Scorilas A, Katsaros D, et al. (2001). "Human kallikrein gene 5 (KLK5) expression is an indicator of poor prognosis in ovarian cancer". Br. J. Cancer. 84 (5): 643–50. PMC 2363783 . PMID 11237385. doi:10.1054/bjoc.2000.1649.
Yousef GM, Scorilas A, Chang A, et al. (2002). "Down-regulation of the human kallikrein gene 5 (KLK5) in prostate cancer tissues". Prostate. 51 (2): 126–32. PMID 11948967. doi:10.1002/pros.10067.
Yousef GM, Obiezu CV, Jung K, et al. (2003). "Differential expression of Kallikrein gene 5 in cancerous and normal testicular tissues". Urology. 60 (4): 714–8. PMID 12385949. doi:10.1016/S0090-4295(02)01811-3.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
Dong Y, Kaushal A, Brattsand M, et al. (2004). "Differential splicing of KLK5 and KLK7 in epithelial ovarian cancer produces novel variants with potential as cancer biomarkers". Clin. Cancer Res. 9 (5): 1710–20. PMID 12738725.
Yousef GM, Kapadia C, Polymeris ME, et al. (2003). "The human kallikrein protein 5 (hK5) is enzymatically active, glycosylated and forms complexes with two protease inhibitors in ovarian cancer fluids". Biochim. Biophys. Acta. 1628 (2): 88–96. PMID 12890555. doi:10.1016/s0167-4781(03)00116-7.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. PMC 403697 . PMID 12975309. doi:10.1101/gr.1293003.
Caubet C, Jonca N, Brattsand M, et al. (2004). "Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7". J. Invest. Dermatol. 122 (5): 1235–44. PMID 15140227. doi:10.1111/j.0022-202X.2004.22512.x.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
Ishida-Yamamoto A, Deraison C, Bonnart C, et al. (2005). "LEKTI is localized in lamellar granules, separated from KLK5 and KLK7, and is secreted in the extracellular spaces of the superficial stratum granulosum". J. Invest. Dermatol. 124 (2): 360–6. PMID 15675955. doi:10.1111/j.0022-202X.2004.23583.x.

External links

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

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KLK5

References

Further reading

External links