Calpain-6

Calpain-6 (also known as calpamodulin) is a protein in humans that is encoded by the CAPN6 gene.^[5]

CAPN6
Identifiers
Aliases	CAPN6, CANPX, CAPNX, CalpM, DJ914P14.1, calpain 6, calpamodulin
External IDs	OMIM: 300146; MGI: 1100850; HomoloGene: 7252; GeneCards: CAPN6; OMA:CAPN6 - orthologs
Gene location (Human) Chr. X chromosome (human)[1] Band Xq23 Start 111,245,099 bp[1] End 111,270,483 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X|X F2 Start 142,585,227 bp[2] End 142,610,410 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tail of epididymis caput epididymis tibia corpus epididymis placenta seminal vesicula cartilage tissue gallbladder body of uterus rectum Top expressed in mandibular prominence condyle efferent ductule saccule atrium hand human fetus fossa maxillary prominence genital tubercle More reference expression data BioGPS n/a
Gene ontology Molecular function microtubule binding calcium-dependent cysteine-type endopeptidase activity Cellular component cytoplasm perinuclear region of cytoplasm spindle spindle microtubule microtubule intracellular anatomical structure cytoskeleton cytosol Biological process regulation of cytoskeleton organization microtubule bundle formation proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 827 12338 Ensembl ENSG00000077274 ENSMUSG00000067276 UniProt Q9Y6Q1 O35646 RefSeq (mRNA) NM_014289 NM_007603 RefSeq (protein) NP_055104 NP_031629 Location (UCSC) Chr X: 111.25 – 111.27 Mb Chr X: 142.59 – 142.61 Mb PubMed search [3] [4]
Wikidata
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Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. In the MEROPS protease enzyme classification system, they are members of clan CA (papain-like proteases).^[6] The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The protein encoded by this gene is highly expressed in the placenta. Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks a critical catalytic triad residue in its active site (cysteine nucleophile mutated to lysine) and thus is suggested to be proteolytically inactive. The protein may play a role in tumor formation by inhibiting apoptosis and promoting angiogenesis.