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).
The process whose specific outcome is the progression of the exocrine pancreas over time, from its formation to the mature structure. The exocrine pancreas produces and store zymogens of digestive enzymes, such as chymotrypsinogen and trypsinogen in the acinar cells.
The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
The process whose specific outcome is the progression of the organism over time, from the completion of embryonic development to the mature structure. See embryonic development.
Any process that modulates the frequency, rate or extent of cell differentiation, the process in which relatively unspecialized cells acquire specialized structural and functional features.
The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.
IEAOrtholog Compara
Enzymatic activity
This protein acts as an enzyme. It is known to catalyze the following reaction
EC 3.4.21.36: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
In spite of its original name "Pancreatic elastase 1", CELA1 is not detected in the pancreas. Elastase activity described in the pancreas may be in fact due to CELA2A (PubMed10620133).
Human pancreatic elastase 1 is a serine protease which maps to the chromosomal region 12q13 close to a locus for an autosomal dominant skin disease, diffuse nonepidermolytic palmoplantar keratoderma, and was investigated as a possible candidate gene for this disorder. Expression of two elastase inhibitors, elafin and SLPI, has been related to several hyperproliferative skin conditions. elastase 1 is functionally silent in the human pancreas but elastase 1 expression at the mRNA level was detected in human cultured primary keratinocytes. Antibody staining localized the protein to the basal cell layer of the human epidermis at a number of sites including the palmoplanta. Sequencing of genomic DNA from individuals with/without the keratoderma revealed a sequence variant, which would result in a premature truncation of the protein. This sequence variant, however, did not segregate with the skin disease and, indeed, was found to occur at a relatively high frequency in the population. Individuals homozygous for the variant do not have any obvious skin abnormalities. Based on the analysis of the secondary structure of the translated putative protein, the truncation is unlikely to result in knock-out of the elastase, but may cause destabilization of the enzyme-inhibitor complex.
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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