Calpain 6 Proteins

Protein Information

Calpain-6, also known as calpamodulin or calpain-X, is an intracellular, calcium-dependent cysteine protease. Calpain-6 has a much more tissue-specific expression in adults than the ubiquitous calpain-1 and calpain-2, and has thus far been found primarily in the placenta, although it is expressed embryonically in a number of tissues. The classical calpain family members consist of a common small subunit (calpain-4), and a large variable subunit, but it is not known if calpain-6 associates with a small subunit. Domains in the large subunit include the amino terminal domain-I, the proteinase domain-II, domain-III, and the EF-hand domain-IV (domain T in calpains 5 and 6). Located on the X chromosome, the calpain-6 sequence lacks the "EF hand" calcium-binding motif found in domain-IV of the classical calpains. In addition, the canonical active site Cys, His and Asn are modified to Lys, His, Asn in human and Lys, Tyr, Asn in mouse calpain-6, making it unlikely that calpain-6 is proteolytically active.

Synonyms

calpain 6; calpain-6; Calpain-like protease X-linked; calpamodulin; CalpM; CANPX; Capa6; CAPN6; CAPNX; DJ914P14.1