CAPN2

From Wikipedia, the free encyclopedia

Calpain 2, (m/II) large subunit

PDB rendering based on 1df0.

Available structures: 1df0, 1kfu, 1kfx, 1mdw, 1u5i

Identifiers

Symbol(s)

CAPN2; CANPL2; CANPml; FLJ39928; mCANP

External IDs

OMIM: 114230 MGI: 88264 HomoloGene: 1326

Gene ontology
Molecular Function:	• calpain activity • calcium ion binding • protein binding
Cellular Component:	• intracellular
Biological Process:	• proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001748 (mRNA)
NP_001739 (protein)

XM_977623 (mRNA)
XP_982717 (protein)

Location

Chr 1: 221.97 - 222.03 Mb

Chr 1: 184.31 - 184.35 Mb

Pubmed search

[1]

[2]

Calpain 2, (m/II) large subunit, also known as CAPN2, is a human gene.

The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported.^[1]

[edit] References

^ Entrez Gene: CAPN2 calpain 2, (m/II) large subunit.

[edit] 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.
Cohen GM (1997). "Caspases: the executioners of apoptosis.". Biochem. J. 326 ( Pt 1): 1–16. PMID 9337844.
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. PMID 11673052.
Kopp S (1976). "Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction.". Community dentistry and oral epidemiology 4 (5): 205–9. PMID 1067155.
Adachi Y, Kitahara-Ozawa A, Sugamura K, et al. (1992). "Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I.". J. Biol. Chem. 267 (27): 19373–8. PMID 1527057.
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. PMID 2209092.
Hata A, Ohno S, Akita Y, Suzuki K (1989). "Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease.". J. Biol. Chem. 264 (11): 6404–11. PMID 2539381.
Imajoh S, Aoki K, Ohno S, et al. (1989). "Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.". Biochemistry 27 (21): 8122–8. PMID 2852952.
Ishiguro H, Higashiyama S, Namikawa C, et al. (1987). "Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations.". Biochemistry 26 (10): 2863–70. PMID 3038169.
Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, et al. (1996). "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32.". J. Biol. Chem. 271 (43): 27099–106. PMID 8900201.
Corasaniti MT, Navarra M, Catani MV, et al. (1997). "NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain.". Biochem. Biophys. Res. Commun. 229 (1): 299–304. doi:10.1006/bbrc.1996.1796. PMID 8954122.
Fujitani K, Kambayashi J, Sakon M, et al. (1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells.". J. Cell. Biochem. 66 (2): 197–209. PMID 9213221.
Rock MT, Brooks WH, Roszman TL (1998). "Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events.". J. Biol. Chem. 272 (52): 33377–83. PMID 9407132.
Ueyama H, Kumamoto T, Fujimoto S, et al. (1998). "Expression of three calpain isoform genes in human skeletal muscles.". J. Neurol. Sci. 155 (2): 163–9. PMID 9562261.
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. PMID 10639123.
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. PMID 10666632.
Chua BT, Guo K, Li P (2000). "Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases.". J. Biol. Chem. 275 (7): 5131–5. PMID 10671558.
Lee MS, Kwon YT, Li M, et al. (2000). "Neurotoxicity induces cleavage of p35 to p25 by calpain.". Nature 405 (6784): 360–4. doi:10.1038/35012636. PMID 10830966.