Caspase-5 (CASP5) Active Protein

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 2010]

CASP5: Mediator of programmed cell death (apoptosis). Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunits. Up-regulated by bacterial lipopolysaccharides (LPS). Expressed in barely detectable amounts in most tissues except brain, highest levels being found in lung, liver and skeletal muscle. Belongs to the peptidase C14A family. 6 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.22.58; Protease

Chromosomal Location of Human Ortholog: 11q22.2-q22.3

Cellular Component: neuron projection; cell soma; cytoplasm

Molecular Function: cysteine-type endopeptidase activity; cysteine-type peptidase activity

Biological Process: regulation of apoptosis; substantia nigra development; apoptosis; regulation of inflammatory response; germ cell programmed cell death; positive regulation of interleukin-1 beta secretion; proteolysis