组织蛋白酶V

组织蛋白酶V
已知的結構 PDB 直系同源搜索: PDBe RCSB PDBID列表 1FH0、​3H6S、​3KFQ
識別號
别名	CTSV；, cathepsin V, CATL2, CTSL2, CTSU
外部ID	OMIM：603308 MGI：88564 HomoloGene：76699 GeneCards：CTSV
基因位置（人类） 染色体 9號染色體[1] 基因座 9q22.33 起始 97,029,677 bp[1] 终止 97,156,556 bp[1]
基因位置（小鼠） 染色体 小鼠13号染色体[2] 基因座 13 B3|13 33.26 cM 起始 64,507,151 bp[2] 终止 64,518,704 bp[2]
RNA表达模式
查阅更多表达数据
基因本體 分子功能 • 半胱氨酸型肽酶活性 • peptide binding • 肽酶活性 • 血浆蛋白结合 • aminopeptidase activity • 水解酶活性 • serine-type endopeptidase activity • cysteine-type endopeptidase activity • cysteine-type carboxypeptidase activity • histone binding • kininogen binding • 大分子复合物结合 細胞組分 • 細胞質 • 細胞本體 • apical part of cell • secretory granule • 細胞外區域 • 微绒毛 • 液胞 • lysosomal lumen • neuron projection • 溶酶体 • external side of plasma membrane • 細胞外空間 • 细胞核 • 核仁 • cytoplasmic vesicle 生物學過程 • male gonad development • response to organic cyclic compound • antigen processing and presentation of exogenous peptide antigen via MHC class II • cellular response to starvation • extracellular matrix disassembly • response to glucocorticoid • response to glucose • Sertoli cell differentiation • response to gonadotropin • 蛋白酶解 • cell communication • 蛻膜化 • 精子发生 • multicellular organism aging • proteolysis involved in cellular protein catabolic process • nerve development • autophagic cell death • response to odorant • regulation of keratinocyte differentiation • negative regulation of keratinocyte proliferation • protein processing • protein autoprocessing • hair follicle morphogenesis • regulation of actin cytoskeleton reorganization Sources:Amigo / QuickGO
直系同源
物種	人類	小鼠
Entrez	1515	13039
Ensembl	ENSG00000136943	ENSMUSG00000021477
UniProt	O60911	P06797
mRNA​序列	NM_001333 ​NM_001201575	NM_009984
蛋白序列	NP_001188504 ​NP_001324	NP_034114
基因位置​（UCSC）	Chr 9: 97.03 – 97.16 Mb	Chr 13: 64.51 – 64.52 Mb
PubMed​查找	[3]	[4]
維基數據
檢視/編輯人類 檢視/編輯小鼠

组织蛋白酶V, （EC 3.4.22.43，也被称为组织蛋白酶L2或组织蛋白酶U），是一种在人类中由CTSV基因编码的蛋白质。[5][6][7][8]

该蛋白质是木瓜蛋白酶样蛋白酶家族（MEROPS家族C1）的成员，这是一种具有内肽酶活性的溶酶体半胱氨酸蛋白酶。它可能在角膜生理学中起重要作用。该基因在结肠直肠癌和乳癌中表达，但在正常结肠、乳腺或肿瘤周围组织中不表达，这表明该基因在肿瘤过程中可能发挥作用。

临床意义

组织蛋白酶V可能在圆锥角膜的发病机制中发挥作用。[9]

参考文献

1. GRCh38: Ensembl release 89: ENSG00000136943 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021477 - 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. Entrez Gene: CTSL2 cathepsin L2. 
6. Brömme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. February 1999, 38 (8): 2377–85. PMID 10029531. doi:10.1021/bi982175f. 
7. Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Investigative Ophthalmology & Visual Science. September 1998, 39 (10): 1789–96. PMID 9727401. 
8. Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Research. April 1998, 58 (8): 1624–30. PMID 9563472. 
9. Kenney MC, Chwa M, Atilano SR, Tran A, Carballo M, Saghizadeh M, Vasiliou V, Adachi W, Brown DJ. Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder. Invest. Ophthalmol. Vis. Sci. 2005, 46 (3): 823–832. PMID 15728537. doi:10.1167/iovs.04-0549 . 

阅读

• Santamaría I, Velasco G, Cazorla M, et al. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.. Cancer Res. 1998, 58 (8): 1624–30. PMID 9563472. 
• Adachi W, Kawamoto S, Ohno I, et al. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium.. Invest. Ophthalmol. Vis. Sci. 1998, 39 (10): 1789–96. PMID 9727401. 
• Brömme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization.. Biochemistry. 1999, 38 (8): 2377–85. PMID 10029531. doi:10.1021/bi982175f. 
• Itoh R, Kawamoto S, Adachi W, et al. Genomic organization and chromosomal localization of the human cathepsin L2 gene.. DNA Res. 1999, 6 (2): 137–40. PMID 10382972. doi:10.1093/dnares/6.2.137 . 
• Somoza JR, Zhan H, Bowman KK, et al. Crystal structure of human cathepsin V.. Biochemistry. 2000, 39 (41): 12543–51. PMID 11027133. doi:10.1021/bi000951p. 
• Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899 . 
• Bernard D, Méhul B, Thomas-Collignon A, et al. Analysis of proteins with caseinolytic activity in a human stratum corneum extract revealed a yet unidentified cysteine protease and identified the so-called "stratum corneum thiol protease" as cathepsin l2.. J. Invest. Dermatol. 2003, 120 (4): 592–600. PMID 12648222. doi:10.1046/j.1523-1747.2003.12086.x . 
• Tolosa E, Li W, Yasuda Y, et al. Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.. J. Clin. Invest. 2003, 112 (4): 517–26. PMC 171390 . PMID 12925692. doi:10.1172/JCI18028. 
• Clark HF, Gurney AL, Abaya E, et al. The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.. Genome Res. 2003, 13 (10): 2265–70. PMC 403697 . PMID 12975309. doi:10.1101/gr.1293003. 
• Humphray SJ, Oliver K, Hunt AR, et al. DNA sequence and analysis of human chromosome 9.. Nature. 2004, 429 (6990): 369–74. Bibcode:2004Natur.429..369H. PMC 2734081 . PMID 15164053. doi:10.1038/nature02465. 
• Yasuda Y, Li Z, Greenbaum D, et al. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages.. J. Biol. Chem. 2004, 279 (35): 36761–70. PMID 15192101. doi:10.1074/jbc.M403986200 . 
• Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).. Genome Res. 2004, 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504. 
• Hagemann S, Günther T, Dennemärker J, et al. The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles.. Eur. J. Cell Biol. 2005, 83 (11–12): 775–80. PMID 15679121. doi:10.1078/0171-9335-00404. 
• Cheng T, Hitomi K, van Vlijmen-Willems IM, et al. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification.. J. Biol. Chem. 2006, 281 (23): 15893–9. PMID 16565075. doi:10.1074/jbc.M600694200 . 
• Burden RE, Snoddy P, Jefferies CA, et al. Inhibition of cathepsin L-like proteases by cathepsin V propeptide.. Biol. Chem. 2007, 388 (5): 541–5. PMID 17516850. S2CID 6680659. doi:10.1515/BC.2007.053. 
• Viken MK, Sollid HD, Joner G, et al. Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.. Hum. Immunol. 2007, 68 (9): 748–55. PMID 17869649. doi:10.1016/j.humimm.2007.05.009. 

外部链接

• The MEROPS online database for peptidases and their inhibitors: C01.009 （页面存档备份，存于互联网档案馆）
• 醫學主題詞表（MeSH）：Cathepsin+V