CAPNS1
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
Further reading
- 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. http://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. http://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. http://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. http://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.
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PDB gallery
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1aj5: CALPAIN DOMAIN VI APO
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1alv: CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN
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1alw: INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN
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1df0: CRYSTAL STRUCTURE OF M-CALPAIN
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1dvi: CALPAIN DOMAIN VI WITH CALCIUM BOUND
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1kfu: Crystal Structure of Human m-Calpain Form II
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1kfx: Crystal Structure of Human m-Calpain Form I
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1np8: 18-k C-terminally trunucated small subunit of calpain
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1nx0: Structure of Calpain Domain 6 in Complex with Calpastatin DIC
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1nx1: Calpain Domain VI Complexed with Calpastatin Inhibitory Domain C (DIC)
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1nx3: Calpain Domain VI in Complex with the Inhibitor PD150606
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1u5i: Crystal Structure analysis of rat m-calpain mutant Lys10 Thr
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| Caspase |
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| Fruit-derived |
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| Calpain |
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| Cathepsin |
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| Other |
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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