InterPro : IPR029531

Name  Calpain-3 Short Name  CAPN3
Type  Family Description  Calpain-3 (CAPN3) belongs to the calpain family, which consists of a group of Ca2+ dependent cysteine proteases that regulate functions of substrates by proteolysis [, ]. Calpain-3 is a calcium-dependent cysteine protease mainly expressed in skeletal muscle. It is involved in sarcomere maintenance and remodelling []. It interacts with myospryn, which is a muscle-specific protein that functions in vesicular trafficking and protein kinase A signalling []. Mutations of the calpain-3 gene cause limb-girdle muscular dystrophy 2A (LGMD2A), an autosomal recessive degenerative myopathy characterised by progressive symmetrical atrophy and weakness of the proximal limb muscles and elevated serum creatine kinase [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR022684 Peptidase C2, calpain family Calpain_cysteine_protease Family

6 Publications

First Author Title Year Journal Volume Pages
Goll DE The calpain system. 2003 Physiol Rev 83 731-801
Richard I Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. 1995 Cell 81 27-40
Kawai H Clinical, pathological, and genetic features of limb-girdle muscular dystrophy type 2A with new calpain 3 gene mutations in seven patients from three Japanese families. 1998 Muscle Nerve 21 1493-501
Sarparanta J Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies. 2010 J Biol Chem 285 30304-15
Duguez S Calpain 3: a key regulator of the sarcomere? 2006 FEBS J 273 3427-36
Jeong SY Calpain-dependent cytoskeletal rearrangement exploited for anthrax toxin endocytosis. 2013 Proc Natl Acad Sci U S A 110 E4007-15

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)