Calpain-2 catalytic subunit

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

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; OMA:CAPN2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q41 Start 223,701,593 bp End 223,776,018 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 H5 Start 182,294,825 bp End 182,345,173 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell nasal epithelium glomerulus mucosa of sigmoid colon right uterine tube parotid gland metanephric glomerulus parietal pleura cartilage tissue visceral pleura Top expressed in endothelial cell of lymphatic vessel genital tubercle facial motor nucleus gastrula umbilical cord left lung tail of embryo right lung right lung lobe cornea More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding cysteine-type peptidase activity metal ion binding cytoskeletal protein binding peptidase activity protein binding protein heterodimerization activity hydrolase activity calcium-dependent cysteine-type endopeptidase activity enzyme binding Cellular component Golgi apparatus pseudopodium membrane focal adhesion perinuclear endoplasmic reticulum intracellular anatomical structure dendrite endoplasmic reticulum cortical actin cytoskeleton membrane raft chromatin lysosome extracellular exosome nucleus cytosol cytoplasm plasma membrane mitochondrial intermembrane space external side of plasma membrane cell projection soma 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: 182.29 – 182.35 Mb PubMed search
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.

Interactions

CAPN2 has been shown to interact with Bcl-2.

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 8561910.523-9&rft.date=1995&rft_id=info:doi/10.1515/bchm3.1995.376.9.523&rft_id=info:pmid/8561910&rft.aulast=Suzuki&rft.aufirst=K&rft.au=Sorimachi, H&rft.au=Yoshizawa, T&rft.au=Kinbara, K&rft.au=Ishiura, S&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 (Pt 1): 1–16. doi:10.1042/bj3260001. PMC 1218630. PMID 9337844.1-16&rft.date=1997&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218630#id-name=PMC&rft_id=info:pmid/9337844&rft_id=info:doi/10.1042/bj3260001&rft.aulast=Cohen&rft.aufirst=GM&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1218630&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 11673052.222-9&rft.date=2001&rft_id=info:doi/10.1016/S1050-1738(01)00112-8&rft_id=info:pmid/11673052&rft.aulast=Reverter&rft.aufirst=D&rft.au=Sorimachi, H&rft.au=Bode, W&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 1067155.205-9&rft.date=1976&rft_id=info:doi/10.1111/j.1600-0528.1976.tb00985.x&rft_id=info:pmid/1067155&rft.aulast=Kopp&rft.aufirst=S&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 1527057.19373-8&rft.date=1992&rft_id=info:doi/10.1016/S0021-9258(18)41785-1&rft_id=info:pmid/1527057&rft.aulast=Adachi&rft.aufirst=Y&rft.au=Kitahara-Ozawa, A&rft.au=Sugamura, K&rft.au=Lee, WJ&rft.au=Yodoi, J&rft.au=Maki, M&rft.au=Murachi, T&rft.au=Hatanaka, M&rft_id=https://doi.org/10.1016%2FS0021-9258%2818%2941785-1&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 2209092.225-9&rft.date=1990&rft_id=info:doi/10.1159/000132937&rft_id=info:pmid/2209092&rft.aulast=Ohno&rft.aufirst=S&rft.au=Minoshima, S&rft.au=Kudoh, J&rft.au=Fukuyama, R&rft.au=Shimizu, Y&rft.au=Ohmi-Imajoh, S&rft.au=Shimizu, N&rft.au=Suzuki, K&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 3038169.2863-70&rft.date=1987&rft_id=info:doi/10.1021/bi00384a030&rft_id=info:pmid/3038169&rft.aulast=Ishiguro&rft.aufirst=H&rft.au=Higashiyama, S&rft.au=Namikawa, C&rft.au=Kunimatsu, M&rft.au=Takano, E&rft.au=Tanaka, K&rft.au=Ohkubo, I&rft.au=Murachi, T&rft.au=Sasaki, M&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 8900201.27099-106&rft.date=1996&rft_id=info:doi/10.1074/jbc.271.43.27099&rft_id=info:pmid/8900201&rft.aulast=Srinivasula&rft.aufirst=SM&rft.au=Fernandes-Alnemri, T&rft.au=Zangrilli, J&rft.au=Robertson, N&rft.au=Armstrong, RC&rft.au=Wang, L&rft.au=Trapani, JA&rft.au=Tomaselli, KJ&rft.au=Litwack, G&rft.au=Alnemri, ES&rft_id=https://doi.org/10.1074%2Fjbc.271.43.27099&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 8954122.299-304&rft.date=1996&rft_id=info:doi/10.1006/bbrc.1996.1796&rft_id=info:pmid/8954122&rft.aulast=Corasaniti&rft.aufirst=MT&rft.au=Navarra, M&rft.au=Catani, MV&rft.au=Melino, G&rft.au=Nisticò, G&rft.au=Finazzi-Agrò, A&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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. S2CID 85163404.197-209&rft.date=1997&rft_id=https://api.semanticscholar.org/CorpusID:85163404#id-name=S2CID&rft_id=info:pmid/9213221&rft_id=info:doi/10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L&rft.aulast=Fujitani&rft.aufirst=K&rft.au=Kambayashi, J&rft.au=Sakon, M&rft.au=Ohmi, SI&rft.au=Kawashima, S&rft.au=Yukawa, M&rft.au=Yano, Y&rft.au=Miyoshi, H&rft.au=Ikeda, M&rft.au=Shinoki, N&rft.au=Monden, M&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 9407132.33377-83&rft.date=1997&rft_id=info:doi/10.1074/jbc.272.52.33377&rft_id=info:pmid/9407132&rft.aulast=Rock&rft.aufirst=MT&rft.au=Brooks, WH&rft.au=Roszman, TL&rft_id=https://doi.org/10.1074%2Fjbc.272.52.33377&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 205898607.163-9&rft.date=1998&rft_id=https://api.semanticscholar.org/CorpusID:205898607#id-name=S2CID&rft_id=info:pmid/9562261&rft_id=info:doi/10.1016/S0022-510X(97)00309-2&rft.aulast=Ueyama&rft.aufirst=H&rft.au=Kumamoto, T&rft.au=Fujimoto, S&rft.au=Murakami, T&rft.au=Tsuda, T&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 10639123.588-92&rft.date=2000&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15374#id-name=PMC&rft_id=info:pmid/10639123&rft_id=info:doi/10.1073/pnas.97.2.588&rft_id=info:bibcode/2000PNAS...97..588S&rft.aulast=Strobl&rft.aufirst=S&rft.au=Fernandez-Catalan, C&rft.au=Braun, M&rft.au=Huber, R&rft.au=Masumoto, H&rft.au=Nakagawa, K&rft.au=Irie, A&rft.au=Sorimachi, H&rft.au=Bourenkow, G&rft.au=Bartunik, H&rft.au=Suzuki, K&rft.au=Bode, W&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15374&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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. Bibcode:2000AcCrD..56...73M. doi:10.1107/S0907444999013748. PMID 10666632.73-5&rft.date=2000&rft_id=info:pmid/10666632&rft_id=info:doi/10.1107/S0907444999013748&rft_id=info:bibcode/2000AcCrD..56...73M&rft.aulast=Masumoto&rft.aufirst=H&rft.au=Nakagawa, K&rft.au=Irie, S&rft.au=Sorimachi, H&rft.au=Suzuki, K&rft.au=Bourenkov, GP&rft.au=Bartunik, H&rft.au=Fernandez-Catalan, C&rft.au=Bode, W&rft.au=Strobl, S&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 10671558.5131-5&rft.date=2000&rft_id=info:doi/10.1074/jbc.275.7.5131&rft_id=info:pmid/10671558&rft.aulast=Chua&rft.aufirst=BT&rft.au=Guo, K&rft.au=Li, P&rft_id=https://doi.org/10.1074%2Fjbc.275.7.5131&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">
• 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 205006589.360-4&rft.date=2000&rft_id=info:doi/10.1038/35012636&rft_id=https://api.semanticscholar.org/CorpusID:205006589#id-name=S2CID&rft_id=info:pmid/10830966&rft_id=info:bibcode/2000Natur.405..360L&rft.aulast=Lee&rft.aufirst=MS&rft.au=Kwon, YT&rft.au=Li, M&rft.au=Peng, J&rft.au=Friedlander, RM&rft.au=Tsai, LH&rfr_id=info:sid/en.wikipedia.org:Calpain-2 catalytic subunit" class="Z3988">

External links

• The MEROPS online database for peptidases and their inhibitors: C02.002 Archived 2008-04-12 at the Wayback Machine
• Human CAPN2 genome location and CAPN2 gene details page in the UCSC Genome Browser.