鈣蛋白酶2催化亞基

鈣蛋白酶2催化亞基
已知的結構
PDB	直系同源搜尋: PDBe RCSB
PDBID列表
	1KFU、1KFX、2NQA
識別號
別名	CAPN2；, CANP2, CANPL2, CANPml, mCANP, calpain 2
外部ID	OMIM：114230 MGI：88264 HomoloGene：1326 GeneCards：CAPN2
基因位置（人類）
染色體	1號染色體
終止	223,776,018 bp
基因位置（小鼠）
染色體	小鼠1號染色體
終止	182,345,173 bp
RNA表達模式
	查閱更多表達數據
基因本體
分子功能	• calcium ion binding; • 半胱氨酸型肽酶活性; • 金屬離子結合; • cytoskeletal protein binding; • 肽酶活性; • 血漿蛋白結合; • protein heterodimerization activity; • 水解酶活性; • calcium-dependent cysteine-type endopeptidase activity; • 酶結合;
細胞組分	• 高爾基體; • 偽足; • 膜; • 粘着斑; • perinuclear endoplasmic reticulum; • 胞內; • 樹突; • 內質網; • cortical actin cytoskeleton; • 脂筏模型; • 染色質; • 溶酶體; • 外排體; • 細胞核; • 細胞質基質; • 細胞質; • 細胞膜; • mitochondrial intermembrane space; • external side of plasma membrane; • cell projection; • neuronal cell body;
生物學過程	• response to hypoxia; • protein autoprocessing; • 蛋白酶解; • 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
直系同源
	824
	12334
	ENSG00000162909
	ENSMUSG00000026509
	P17655
	O08529
	NM_001146068; NM_001748
	NM_009794
	NP_001139540; NP_001739
	NP_033924
	維基數據
檢視/編輯人類	檢視/編輯小鼠

鈣蛋白酶2催化亞基（英語：Calpain-2 catalytic subunit）是人類中由CAPN2基因編碼的蛋白質。^[5]^[6]

Quick Facts 鈣蛋白酶2催化亞基, 已知的結構 ...

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功能

鈣蛋白酶是鈣活化的中性蛋白酶，是非溶酶體的細胞內半胱氨酸蛋白酶。哺乳動物鈣蛋白酶包括普遍存在的胃特異性和肌肉特異性蛋白質。普遍存在的酶由異二聚體組成，這些異二聚體具有與常見的小調節亞基相關的獨特的大催化亞基。該基因編碼普遍存在的酶鈣蛋白酶2的大亞基。已報道5' UTR中存在多個異質轉錄起始位點。^[7]

相互作用

CAPN2已被證明與Bcl-2產生相互作用。^[8]

參考資料

[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. Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Biochemistry. 1988, 27 (21): 8122–8. PMID 2852952. doi:10.1021/bi00421a022.
[6]
Hata A, Ohno S, Akita Y, Suzuki K. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. J. Biol. Chem. May 1989, 264 (11): 6404–11. PMID 2539381. doi:10.1016/S0021-9258(18)83364-6 .
[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. Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members. J. Biol. Chem. Jul 2002, 277 (30): 27217–26. PMID 12000759. doi:10.1074/jbc.M202945200 .

延伸閱讀

Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S. Calpain: novel family members, activation, and physiologic function. Biol. Chem. Hoppe-Seyler. 1995, 376 (9): 523–9. PMID 8561910. doi:10.1515/bchm3.1995.376.9.523.
Cohen GM. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326 (Pt 1): 1–16. PMC 1218630 . PMID 9337844. doi:10.1042/bj3260001.
Reverter D, Sorimachi H, Bode W. The structure of calcium-free human m-calpain: implications for calcium activation and function. Trends Cardiovasc. Med. 2001, 11 (6): 222–9. PMID 11673052. doi:10.1016/S1050-1738(01)00112-8.
Kopp S. Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction. Community Dent Oral Epidemiol. 1976, 4 (5): 205–9. PMID 1067155. doi:10.1111/j.1600-0528.1976.tb00985.x.
Adachi Y, Kitahara-Ozawa A, Sugamura K, Lee WJ, Yodoi J, Maki M, Murachi T, Hatanaka M. Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. J. Biol. Chem. 1992, 267 (27): 19373–8. PMID 1527057. doi:10.1016/S0021-9258(18)41785-1 .
Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K. Four genes for the calpain family locate on four distinct human chromosomes. Cytogenet. Cell Genet. 1990, 53 (4): 225–9. PMID 2209092. doi:10.1159/000132937.
Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M. 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. 1987, 26 (10): 2863–70. PMID 3038169. doi:10.1021/bi00384a030.
Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, Robertson N, Armstrong RC, Wang L, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES. 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. 1996, 271 (43): 27099–106. PMID 8900201. doi:10.1074/jbc.271.43.27099 .
Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A. 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. 1996, 229 (1): 299–304. PMID 8954122. doi:10.1006/bbrc.1996.1796.
Fujitani K, Kambayashi J, Sakon M, Ohmi SI, Kawashima S, Yukawa M, Yano Y, Miyoshi H, Ikeda M, Shinoki N, Monden M. Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. J. Cell. Biochem. 1997, 66 (2): 197–209. PMID 9213221. S2CID 85163404. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L.
Rock MT, Brooks WH, Roszman TL. 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. 1997, 272 (52): 33377–83. PMID 9407132. doi:10.1074/jbc.272.52.33377 .
Ueyama H, Kumamoto T, Fujimoto S, Murakami T, Tsuda T. Expression of three calpain isoform genes in human skeletal muscles. J. Neurol. Sci. 1998, 155 (2): 163–9. PMID 9562261. S2CID 205898607. doi:10.1016/S0022-510X(97)00309-2.
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. 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. 2000, 97 (2): 588–92. Bibcode:2000PNAS...97..588S. PMC 15374 . PMID 10639123. doi:10.1073/pnas.97.2.588 .
Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S. Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain. Acta Crystallogr. D. 2000, 56 (Pt 1): 73–5. Bibcode:2000AcCrD..56...73M. PMID 10666632. doi:10.1107/S0907444999013748.
Chua BT, Guo K, Li P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J. Biol. Chem. 2000, 275 (7): 5131–5. PMID 10671558. doi:10.1074/jbc.275.7.5131 .
Lee MS, Kwon YT, Li M, Peng J, Friedlander RM, Tsai LH. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature. 2000, 405 (6784): 360–4. Bibcode:2000Natur.405..360L. PMID 10830966. S2CID 205006589. doi:10.1038/35012636.

外部連結

The MEROPS online database for peptidases and their inhibitors: C02.002 （頁面存檔備份，存於互聯網檔案館）
Human CAPN2 genome location and CAPN2 gene details page in the UCSC Genome Browser（英語：UCSC Genome Browser）.

[refGRCh38Ensembl-1] [1]
GRCh38: Ensembl release 89: ENSG00000162909 - Ensembl, May 2017

[refGRCm38Ensembl-2] [2]
GRCm38: Ensembl release 89: ENSMUSG00000026509 - Ensembl, May 2017

[3] [3]
Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] [4]
Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2852952-5] [5]
Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K. Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Biochemistry. 1988, 27 (21): 8122–8. PMID 2852952. doi:10.1021/bi00421a022.

[pmid2539381-6] [6]
Hata A, Ohno S, Akita Y, Suzuki K. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. J. Biol. Chem. May 1989, 264 (11): 6404–11. PMID 2539381. doi:10.1016/S0021-9258(18)83364-6 .

[entrez-7] [7]
Entrez Gene: CAPN2 calpain 2, (m/II) large subunit.

[pmid12000759-8] [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. Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members. J. Biol. Chem. Jul 2002, 277 (30): 27217–26. PMID 12000759. doi:10.1074/jbc.M202945200 .

[5]

[6]

[1]

[2]

[3]

[4]

[7]

[8]