Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3.[7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Matena K, Boehm T, Dear N (Apr 1998). "Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily". Genomics. 48 (1): 117–20. doi:10.1006/geno.1997.5133. PMID9503024.
^Mugita N, Kimura Y, Ogawa M, Saya H, Nakao M (Dec 1997). "Identification of a novel, tissue-specific calpain htra-3; a human homologue of the Caenorhabditis elegans sex determination gene". Biochem Biophys Res Commun. 239 (3): 845–50. doi:10.1006/bbrc.1997.7571. PMID9367857.
Sato K, Kawashima S (2002). "Calpain function in the modulation of signal transduction molecules". Biol. Chem. 382 (5): 743–51. doi:10.1515/BC.2001.090. PMID11517927.
Dear N, Matena K, Vingron M, Boehm T (1997). "A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution". Genomics. 45 (1): 175–84. doi:10.1006/geno.1997.4870. PMID9339374.
Waghray A, Wang DS, McKinsey D, et al. (2004). "Molecular cloning and characterization of rat and human calpain-5". Biochem. Biophys. Res. Commun. 324 (1): 46–51. doi:10.1016/j.bbrc.2004.09.012. PMID15464980.
