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kallikrein-7; hK7; serine protease 6; stratum corneum chymotryptic enzyme; hSCCE (KLK7, PRSS6, SCCE)

Function: - may catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface - specific for amino acid residues with aromatic side chains in the P1 position - cleaves insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' & '26-Tyr-|-Thr-27' - could play a role in the activation of precursors to inflammatory cytokines Inhibition: - inhibited by Zn2+ & Cu2+ at low micromolar concentrations Structure: - belongs to the peptidase S1 family, kallikrein subfamily - contains 1 peptidase S1 domain Compartment: - secreted - in ovarian carcinoma, secreted & also observed at the apical membrane & in cytoplasm at the invasive front Alternative splicing: named isoforms=2 Expression: - abundantly expressed in the skin & is expressed by keratinocytes in the epidermis - also expressed in the brain, mammary gland, cerebellum, spinal cord & kidney - lower expression in salivary glands, uterus, thymus, thyroid, placenta, trachea & testis - induced by estrogens & glucocorticoids in a breast carcinoma cell line Pathology: - up-regulated in ovarian carcinoma, especially late-stage serous carcinoma, compared with normal ovaries & benign adenomas (at protein level)

General

glycoprotein kallikrein

Properties

SIZE: entity length = 253 aa MW = 28 kD COMPARTMENT: cytoplasm MOTIF: signal sequence {1-22} S1 domain {30-250} MOTIF: cysteine residue {C36} MODIFICATION: cysteine residue {C165} cysteine residue {C55} MODIFICATION: cysteine residue {C71} histidine residue {H70} cysteine residue {C71} MODIFICATION: cysteine residue {C55} histidine residue {109} aspartate residue {D112} cysteine residue {C137} MODIFICATION: cysteine residue {C239} cysteine residue {C144} MODIFICATION: cysteine residue {C211} cysteine residue {C165} MODIFICATION: cysteine residue {C36} cysteine residue {C176} MODIFICATION: cysteine residue {C190} cysteine residue {C190} MODIFICATION: cysteine residue {C176} cysteine residue {C201} MODIFICATION: cysteine residue {C226} serine residue {S205} cysteine residue {C211} MODIFICATION: cysteine residue {C144} cysteine residue {C226} MODIFICATION: cysteine residue {C201} cysteine residue {C239} MODIFICATION: cysteine residue {C137} N-glycosylation site {N246}

Database Correlations

OMIM 604438 UniProt P49862 Pfam PF00089 Entrez Gene 5650 Kegg hsa:5650 ENZYME 3.4.21.117

References

  1. UniProt :accession P49862
  2. Entrez Gene :accession 5650