Capns1

Calpain, small subunit 1

PDB rendering based on 1aj5.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1KFU, 1KFX

Identifiers

Symbols

CAPNS1; 30K; CALPAIN4; CANP; CANPS; CAPN4; CDPS; CSS1

External IDs

OMIM: 114170 MGI: 88266 HomoloGene: 1327 ChEMBL: 4962 GeneCards: CAPNS1 Gene

EC number

3.4.22.17

Gene Ontology
Molecular function	• calcium-dependent cysteine-type endopeptidase activity • calcium ion binding • protein binding • protein heterodimerization activity
Cellular component	• cytoplasm • plasma membrane
Biological process	• proteolysis • metabolic process • positive regulation of cell proliferation
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
36.63 – 36.64 Mb

Chr 7:
30.97 – 30.98 Mb

PubMed search

[1]

[2]

Calpain small subunit 1 is a protein that in humans is encoded by the CAPNS1 gene.^[1]^[2]^[3]

Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. Calpain families have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. Calpain I and II are heterodimeric with distinct large subunits associated with common small subunits, all of which are encoded by different genes. This gene encodes a small subunit common to both calpain I and II and is associated with myotonic dystrophy. Two transcript variants encoding the same protein have been identified for this gene.^[3]

References [link]

^ Miyake S, Emori Y, Suzuki K (Jan 1987). "Gene organization of the small subunit of human calcium-activated neutral protease". Nucleic Acids Res 14 (22): 8805–17. DOI:10.1093/nar/14.22.8805. PMC 311912. PMID 3024120. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311912.
^ Ohno S, Emori Y, Suzuki K (Sep 1986). "Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease". Nucleic Acids Res 14 (13): 5559. PMC 311560. PMID 3016651. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311560.
^ ^a ^b "Entrez Gene: CAPNS1 calpain, small subunit 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=826.

Further reading [link]

Suzuki K, Sorimachi H, Yoshizawa T et al. (1996). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler 376 (9): 523–9. PMID 8561910.
Tidball JG, Spencer MJ (2000). "Calpains and muscular dystrophies". Int. J. Biochem. Cell Biol. 32 (1): 1–5. DOI:10.1016/S1357-2725(99)00095-3. PMID 10661889.
Huang Y, Wang KK (2001). "The calpain family and human disease". Trends in molecular medicine 7 (8): 355–62. DOI:10.1016/S1471-4914(01)02049-4. PMID 11516996.
Reverter D, Sorimachi H, Bode W (2001). "The structure of calcium-free human m-calpain: implications for calcium activation and function". Trends Cardiovasc. Med. 11 (6): 222–9. DOI:10.1016/S1050-1738(01)00112-8. PMID 11673052.
Banik NL, DeVries GH, Neuberger T et al. (1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP". J. Neurosci. Res. 29 (3): 346–54. DOI:10.1002/jnr.490290310. PMID 1656060.
Ohno S, Minoshima S, Kudoh J et al. (1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet. Cell Genet. 53 (4): 225–9. DOI:10.1159/000132937. PMID 2209092.
Andersson B, Wentland MA, Ricafrente JY et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. DOI:10.1006/abio.1996.0138. PMID 8619474.
Zhang W, Lane RD, Mellgren RL (1996). "The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells". J. Biol. Chem. 271 (31): 18825–30. DOI:10.1074/jbc.271.31.18825. PMID 8702541.
Yu W, Andersson B, Worley KC et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. DOI:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
Noguchi M, Sarin A, Aman MJ et al. (1997). "Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain". Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11534–9. DOI:10.1073/pnas.94.21.11534. PMC 23528. PMID 9326644. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23528.
Strobl S, Fernandez-Catalan C, Braun M et al. (2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 588–92. DOI:10.1073/pnas.97.2.588. PMC 15374. PMID 10639123. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15374.
Masumoto H, Nakagawa K, Irie S et al. (2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain". Acta Crystallogr. D Biol. Crystallogr. 56 (Pt 1): 73–5. DOI:10.1107/S0907444999013748. PMID 10666632.
Dias Neto E, Correa RG, Verjovski-Almeida S et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. DOI:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16267.
Reverter D, Strobl S, Fernandez-Catalan C et al. (2002). "Structural basis for possible calcium-induced activation mechanisms of calpains". Biol. Chem. 382 (5): 753–66. DOI:10.1515/BC.2001.091. PMID 11517928.