CAPN2

Calpain-2 catalytic subunit is a protein that in humans is encoded by the CAPN2 gene.[5][6]

CAPN2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1KFU, 1KFX, 2NQA
Identifiers
Aliases	CAPN2, CANP2, CANPL2, CANPml, mCANP, calpain 2
External IDs	OMIM: 114230 MGI: 88264 HomoloGene: 1326 GeneCards: CAPN2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q41 Start 223,701,593 bp[1] End 223,776,018 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H5 Start 182,467,260 bp[2] End 182,517,608 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • cysteine-type peptidase activity • metal ion binding • cytoskeletal protein binding • peptidase activity • GO:0001948 protein binding • protein heterodimerization activity • hydrolase activity • calcium-dependent cysteine-type endopeptidase activity • enzyme binding Cellular component • Golgi apparatus • pseudopodia • membrane • focal adhesion • perinuclear endoplasmic reticulum • intracellular • dendrite • endoplasmic reticulum • cortical actin cytoskeleton • membrane raft • chromatin • lysosome • extracellular exosome • cell nucleus • cytosol • cytoplasm • cell membrane • mitochondrial intermembrane space • external side of plasma membrane • cell projection • neuronal cell body Biological process • response to hypoxia • protein autoprocessing • proteolysis • cellular response to amino acid stimulus • myoblast fusion • proteolysis involved in cellular protein catabolic process • regulation of cytoskeleton organization • blastocyst development • extracellular matrix disassembly • female pregnancy • positive regulation of cardiac muscle cell apoptotic process • regulation of interleukin-6 production • cellular response to interferon-beta • response to hydrogen peroxide • behavioral response to pain • cellular response to lipopolysaccharide • positive regulation of neuron death • positive regulation of myoblast fusion • positive regulation of phosphatidylcholine biosynthetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	824	12334
Ensembl	ENSG00000162909	ENSMUSG00000026509
UniProt	P17655	O08529
RefSeq (mRNA)	NM_001146068 NM_001748	NM_009794
RefSeq (protein)	NP_001139540 NP_001739	NP_033924
Location (UCSC)	Chr 1: 223.7 – 223.78 Mb	Chr 1: 182.47 – 182.52 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

Interactions

CAPN2 has been shown to interact with Bcl-2.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000162909 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026509 - 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. Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K (1988). "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. doi:10.1021/bi00421a022. PMID 2852952.
6. Hata A, Ohno S, Akita Y, Suzuki K (May 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. doi:10.1016/S0021-9258(18)83364-6. PMID 2539381.
7. "Entrez Gene: CAPN2 calpain 2, (m/II) large subunit".
8. Gil-Parrado S, Fernández-Montalván A, Assfalg-Machleidt I, Popp O, Bestvater F, Holloschi A, Knoch TA, Auerswald EA, Welsh K, Reed JC, Fritz H, Fuentes-Prior P, Spiess E, Salvesen GS, Machleidt W (Jul 2002). "Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members". J. Biol. Chem. 277 (30): 27217–26. doi:10.1074/jbc.M202945200. PMID 12000759.

Further reading

• Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (1995). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler. 376 (9): 523–9. doi:10.1515/bchm3.1995.376.9.523. PMID 8561910.
• Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 (Pt 1): 1–16. doi:10.1042/bj3260001. PMC 1218630. 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. doi:10.1016/S1050-1738(01)00112-8. PMID 11673052.
• Kopp S (1976). "Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction". Community Dent Oral Epidemiol. 4 (5): 205–9. doi:10.1111/j.1600-0528.1976.tb00985.x. PMID 1067155.
• Adachi Y, Kitahara-Ozawa A, Sugamura K, Lee WJ, Yodoi J, Maki M, Murachi T, Hatanaka M (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. doi:10.1016/S0021-9258(18)41785-1. PMID 1527057.
• 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". Cytogenet. Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092.
• Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M (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. doi:10.1021/bi00384a030. PMID 3038169.
• Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, Robertson N, Armstrong RC, Wang L, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES (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. doi:10.1074/jbc.271.43.27099. PMID 8900201.
• Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A (1996). "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, Ohmi SI, Kawashima S, Yukawa M, Yano Y, Miyoshi H, Ikeda M, Shinoki N, Monden M (1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. Biochem. 66 (2): 197–209. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L. PMID 9213221.
• Rock MT, Brooks WH, Roszman TL (1997). "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. doi:10.1074/jbc.272.52.33377. PMID 9407132.
• Ueyama H, Kumamoto T, Fujimoto S, Murakami T, Tsuda T (1998). "Expression of three calpain isoform genes in human skeletal muscles". J. Neurol. Sci. 155 (2): 163–9. doi:10.1016/S0022-510X(97)00309-2. PMID 9562261. S2CID 205898607.
• 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 (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. Bibcode:2000PNAS...97..588S. 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 (2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain". Acta Crystallogr. D. 56 (Pt 1): 73–5. doi:10.1107/S0907444999013748. 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. doi:10.1074/jbc.275.7.5131. PMID 10671558.
• Lee MS, Kwon YT, Li M, Peng J, Friedlander RM, Tsai LH (2000). "Neurotoxicity induces cleavage of p35 to p25 by calpain". Nature. 405 (6784): 360–4. Bibcode:2000Natur.405..360L. doi:10.1038/35012636. PMID 10830966. S2CID 205006589.

External links

• The MEROPS online database for peptidases and their inhibitors: C02.002
• Human CAPN2 genome location and CAPN2 gene details page in the UCSC Genome Browser.