CAPNS1

CAPNS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1KFU, 1KFX, 4PHJ, 4PHK, 4PHM, 4WQ2, 4WQ3, 5D69
Identifiers
Aliases	CAPNS1 , 30K, CALPAIN4, CANP, CANPS, CAPN4, CDPS, CSS1, calpain small subunit 1
External IDs	OMIM: 114170 MGI: 88266 HomoloGene: 1327 GeneCards: CAPNS1
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19q13.12 Start 36,139,953 bp [1] End 36,150,353 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7 B1|7 17.31 cM Start 30,186,936 bp [2] End 30,198,811 bp [2]
Gene ontology Molecular function • calcium ion binding • GO:0001948 protein binding • calcium-dependent cysteine-type endopeptidase activity • metal ion binding • endopeptidase activity Cellular component • cytoplasm • extracellular exosome • membrane • cytosol • plasma membrane Biological process • extracellular matrix disassembly • regulation of macroautophagy • positive regulation of cell population proliferation • proteolysis • cornification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	826	12336
Ensembl	ENSG00000126247	ENSMUSG00000001794
UniProt	P04632	O88456
RefSeq (mRNA)	NM_001003962 NM_001302632 NM_001302633 NM_001749	NM_009795
RefSeq (protein)	NP_001003962 NP_001289561 NP_001289562 NP_001740	NP_033925
Location (UCSC)	Chr 19: 36.14 – 36.15 Mb	Chr 7: 30.19 – 30.2 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Calpain small subunit 1, also known as CAPN4, is a protein that in humans is encoded by the CAPNS1 gene. ^{[5] [6] [7]}

Function

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. The small regulatory subunit consists of an N-terminal domain, containing about 30% glycine residues and a C-terminal Ca-binding domain. ^[8] Two transcript variants encoding the same protein have been identified for this gene. ^[7]

Functions

Myotonic dystrophy

This gene encodes a small subunit common to both calpain I and II and is associated with myotonic dystrophy. ^[7]

Biomarker

Elevated expression of Capn4 has been found to be associated with progression of various cancers such as hepatocellular and renal carcinoma. ^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000126247 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001794 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Miyake S, Emori Y, Suzuki K (November 1986). "Gene organization of the small subunit of human calcium-activated neutral protease". Nucleic Acids Research. 14 (22): 8805–17. doi:10.1093/nar/14.22.8805. PMC   311912 . PMID   3024120.
6. Ohno S, Emori Y, Suzuki K (July 1986). "Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease". Nucleic Acids Research. 14 (13): 5559. PMC   311560 . PMID   3016651.
7. "Entrez Gene: CAPNS1 calpain, small subunit 1".
8. Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, Hatanaka M, DeLucas LJ, Narayana SV (July 1997). "Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding". Nature Structural Biology. 4 (7): 539–47. doi:10.1038/nsb0797-539. PMID   9228946. S2CID   31913560.
9. Zhuang Q, Qian X, Cao Y, Fan M, Xu X, He X (April 2014). "Capn4 mRNA level is correlated with tumour progression and clinical outcome in clear cell renal cell carcinoma". The Journal of International Medical Research. 42 (2): 282–91. doi: 10.1177/0300060513505524 . PMID   24514433.

External links

• Human CAPNS1 genome location and CAPNS1 gene details page in the UCSC Genome Browser .

Further reading

• Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (September 1995). "Calpain: novel family members, activation, and physiologic function". Biological Chemistry Hoppe-Seyler. 376 (9): 523–9. doi:10.1515/bchm3.1995.376.9.523. PMID   8561910.
• Tidball JG, Spencer MJ (January 2000). "Calpains and muscular dystrophies". The International Journal of Biochemistry & Cell Biology. 32 (1): 1–5. doi:10.1016/S1357-2725(99)00095-3. PMID   10661889.
• Huang Y, Wang KK (August 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 (August 2001). "The structure of calcium-free human m-calpain: implications for calcium activation and function". Trends in Cardiovascular Medicine. 11 (6): 222–9. doi:10.1016/S1050-1738(01)00112-8. PMID   11673052.
• Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL (July 1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP". Journal of Neuroscience Research. 29 (3): 346–54. doi:10.1002/jnr.490290310. PMID   1656060. S2CID   40120102.
• Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenetics and Cell Genetics. 53 (4): 225–9. doi:10.1159/000132937. PMID   2209092.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID   8619474.
• Zhang W, Lane RD, Mellgren RL (August 1996). "The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells". The Journal of Biological Chemistry. 271 (31): 18825–30. doi: 10.1074/jbc.271.31.18825 . PMID   8702541.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Noguchi M, Sarin A, Aman MJ, Nakajima H, Shores EW, Henkart PA, Leonard WJ (October 1997). "Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain". Proceedings of the National Academy of Sciences of the United States of America. 94 (21): 11534–9. doi: 10.1073/pnas.94.21.11534 . PMC   23528 . PMID   9326644.
• Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W (January 2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium". Proceedings of the National Academy of Sciences of the United States of America. 97 (2): 588–92. doi: 10.1073/pnas.97.2.588 . PMC   15374 . PMID   10639123.
• Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S (January 2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain". Acta Crystallographica Section D. 56 (Pt 1): 73–5. doi:10.1107/S0907444999013748. PMID   10666632.
• Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (March 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. doi: 10.1073/pnas.97.7.3491 . PMC   16267 . PMID   10737800.
• Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W (May 2001). "Structural basis for possible calcium-induced activation mechanisms of calpains". Biological Chemistry. 382 (5): 753–66. doi:10.1515/BC.2001.091. PMID   11517928. S2CID   23221865.