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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)
End	111,270,483 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	142,610,410 bp
RNA expression pattern
	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
	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
	827
	12338
	ENSG00000077274
	ENSMUSG00000067276
	Q9Y6Q1
	O35646
	NM_014289
	NM_007603
	NP_055104
	NP_031629
	Wikidata
View/Edit Human	View/Edit Mouse

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

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.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000077274 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000067276 – Ensembl, May 2017
^ "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.
^ "Entrez Gene: Calpain 6". National Center for Biotechnology Information. U.S. National Library of Medicine. Archived from the original on 18 November 2020. Retrieved 2013-03-05.
^ "Summary for clan CA". MEROPS. Retrieved 20 December 2021.