期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 275, 期 4, 页码 2581-2588出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.275.4.2581
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资金
- NIDDK NIH HHS [R01 DK55734-01] Funding Source: Medline
We report the isolation and characterization of a cDNA encoding the novel mammalian serine protease Omi. Omi protein consists of 458 amino acids and has homology to bacterial HtrA endoprotease, which acts as a chaperone at low temperatures and as a proteolytic enzyme that removes denatured or damaged substrates at elevated temperatures. The carboxyl terminus of Omi has extensive homology to a mammalian protein called L56 (human HtrA), but unlike L56, which is secreted, Omi is localized in the endoplasmic reticulum, Omi has several novel putative protein-protein interaction motifs, as well as a PDZ domain and a Src homology 3-binding domain, Omi mRNA is expressed ubiquitously, and the gene is localized on human chromosome 2p12, Omi interacts with Mxi2, an alternatively spliced form of the p38 stress-activated kinase, Omi protein, when made in a heterologous system, shows proteolytic activity against a nonspecific substrate beta-casein, The proteolytic activity of Omi is markedly up-regulated in the mouse kidney following ischemia/reperfusion.
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