Calpain-2 catalytic subunit

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 182,294,825 bp [2] End 182,345,173 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell glomerulus right uterine tube parotid gland metanephric glomerulus parietal pleura visceral pleura oral cavity amniotic fluid germinal epithelium Top expressed in facial motor nucleus belly cord left lung right lung right lung lobe cornea aorta white adipose tissue ankle left lung lobe 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 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: 182.29 – 182.35 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. S2CID   85163404.
• 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. Bibcode:2000AcCrD..56...73M. 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 Archived 2008-04-12 at the Wayback Machine
• Human CAPN2 genome location and CAPN2 gene details page in the UCSC Genome Browser .