CAPN3

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CAPN3
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CAPN3, CANP3, CANPL3, LGMD2, LGMD2A, nCL-1, p94, calpain 3
External IDs MGI: 107437 HomoloGene: 52 GeneCards: CAPN3
Gene location (Human)
Chromosome 15 (human)
Chr. Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for CAPN3
Genomic location for CAPN3
Band 15q15.1 Start 42,359,500 bp[1]
End 42,412,318 bp[1]
RNA expression pattern
PBB GE CAPN3 gnf1h08766 s at fs.png

PBB GE CAPN3 gnf1h06575 at fs.png

PBB GE CAPN3 gnf1h02293 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001109761
NM_001177799
NM_007601

RefSeq (protein)

NP_001103231
NP_001171270
NP_031627

Location (UCSC) Chr 15: 42.36 – 42.41 Mb Chr 15: 120.46 – 120.5 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Calpain-3 is a protein that in humans is encoded by the CAPN3 gene.[5][6]

Function[edit]

Calpain, a heterodimer consisting of a large and a small subunit, is a major intracellular protease, although its function has not been well established. This gene encodes a muscle-specific member of the calpain large subunit family that specifically binds to titin. Mutations in this gene are associated with limb-girdle muscular dystrophies type 2A. Alternate promoters and alternative splicing result in multiple transcript variants encoding different isoforms and some variants are ubiquitously expressed.[7]

In melanocytic cells CAPN3 gene expression may be regulated by MITF.[8]

Interactions[edit]

CAPN3 has been shown to interact with Titin.[9][10]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000092529 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079110 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, Minami Y, Suzuki K (December 1989). "Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle". J. Biol. Chem. 264 (33): 20106–11. PMID 2555341. 
  6. ^ Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, Bourg N, Brenguier L, Devaud C, Pasturaud P, Roudaut C (May 1995). "Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A". Cell. 81 (1): 27–40. PMID 7720071. doi:10.1016/0092-8674(95)90368-2. 
  7. ^ "Entrez Gene: CAPN3 calpain 3, (p94)". 
  8. ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. PMID 19067971. doi:10.1111/j.1755-148X.2008.00505.x. 
  9. ^ Ono Y, Shimada H, Sorimachi H, Richard I, Saido TC, Beckmann JS, Ishiura S, Suzuki K (July 1998). "Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A". J. Biol. Chem. 273 (27): 17073–8. PMID 9642272. doi:10.1074/jbc.273.27.17073. 
  10. ^ Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K (December 1995). "Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence". J. Biol. Chem. 270 (52): 31158–62. PMID 8537379. doi:10.1074/jbc.270.52.31158. 

Further reading[edit]

External links[edit]