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. SCCE cleaves insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
J. Biol. Chem. 269, 19420-19426 (1994)[PubMed:8034709]
The cDNA encoding human stratum corneum chymotryptic enzyme (SCCE); an epidermal serine-proteinase which was recently purified from human stratum corneum, was isolated from a keratinocyte derived library. The obtained nucleotide sequence contained an open reading frame sufficient to encode a preproprotein consisting of 253 amino acid residues. Expression of two mRNA species hybridizing with SCCE cDNA, 1.2 and 2.0 kilobases, respectively, was detected to human skin. These two forms differ with respect to the length of the 3'-untranslated sequence. Analysis of mRNA derived from various human tissues showed that abundant expression of the SCCE gene was restricted to human skin. The cloned cDNA was introduced to a bovine papilloma virus-based expression system and recombinant protein was purified and characterized. The results show that recombinant SCCE is produced with a 22-amino acid residue signal peptide and a propeptide of 7 amino acid residues. Tryptic digestion removed this propeptide and yielded a proteolytically active protein with the same NH2-terminal amino acid sequence as native SCCE. The deduced amino acid sequence contains the conserved active site regions of serine proteinases. The calculated molecular mass of unglycosylated active SCCE was 24.4 kDa. The sequence indicates one tentative N-glycosylation site located near the C terminus. Recombinant SCCE was found to be heterogenous regarding glycosylation in a manner similar to that of the native enzyme.
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of a plant or animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
J. Biol. Chem. 269, 19420-19426 (1994)[PubMed:8034709]
The cDNA encoding human stratum corneum chymotryptic enzyme (SCCE); an epidermal serine-proteinase which was recently purified from human stratum corneum, was isolated from a keratinocyte derived library. The obtained nucleotide sequence contained an open reading frame sufficient to encode a preproprotein consisting of 253 amino acid residues. Expression of two mRNA species hybridizing with SCCE cDNA, 1.2 and 2.0 kilobases, respectively, was detected to human skin. These two forms differ with respect to the length of the 3'-untranslated sequence. Analysis of mRNA derived from various human tissues showed that abundant expression of the SCCE gene was restricted to human skin. The cloned cDNA was introduced to a bovine papilloma virus-based expression system and recombinant protein was purified and characterized. The results show that recombinant SCCE is produced with a 22-amino acid residue signal peptide and a propeptide of 7 amino acid residues. Tryptic digestion removed this propeptide and yielded a proteolytically active protein with the same NH2-terminal amino acid sequence as native SCCE. The deduced amino acid sequence contains the conserved active site regions of serine proteinases. The calculated molecular mass of unglycosylated active SCCE was 24.4 kDa. The sequence indicates one tentative N-glycosylation site located near the C terminus. Recombinant SCCE was found to be heterogenous regarding glycosylation in a manner similar to that of the native enzyme.
Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the hydrogen and hydroxyl ions of water to a molecule with its consequent splitting into two or more simpler molecules.
Proteolytic enzyme with a serine residue (Ser) in its active site. The reactivity of the serine residue is ensured by the vicinity of a histidine and an aspartate residue (catalytic triad), all three residues are required for the charge relay system to take place.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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