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Gene Review

Jon99Ci  -  Jonah 99Ci

Drosophila melanogaster

Synonyms: 143341_at, 99Calpha, CG17951, CG31039, Dmel\CG31039, ...
 
 
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Disease relevance of Jon99Ci

  • Hepatitis C virus (HCV) nonstructural 3 (NS3) serine protease disrupts important cellular antiviral signaling pathways and plays a pivotal role in the proteolytic maturation of the HCV polyprotein precursor [1].
  • Finally, a mutation called disorganization, which is located near the serine protease complex, is of considerable interest because it causes an extraordinarily wide variety of congenital defects [2].
 

High impact information on Jon99Ci

 

Biological context of Jon99Ci

 

Anatomical context of Jon99Ci

 

Associations of Jon99Ci with chemical compounds

 

Other interactions of Jon99Ci

  • To activate the pathway, we overexpressed an activated form of the EGFR (UAS-caEGFR), and an activated form of the signal transducer Raf (UAS-caRaf); we also over- or ectopically expressed the downstream homeobox transcription factor Mirror (UAS-mirr) and the ligand-activating serine protease Rhomboid (UAS-rho) [17].
  • The easter gene encodes a serine protease that generates processed Spätzle, which is proposed to act as the Toll ligand [18].
  • The gut-specific sequences encode a maltase, a V-ATPase subunit, a GTP binding protein, two different lectins, and a nontrypsin serine protease [19].
  • Easter is the final protease in a serine protease cascade in which initial reaction steps appear not to be ventrally restricted, but where Easter activity is promoted ventrally through the action of a spatial cue at an unknown step in the pathway [20].
  • Evidence of serine-protease activity closely associated with Drosophila alcohol dehydrogenase [21].
 

Analytical, diagnostic and therapeutic context of Jon99Ci

References

  1. Serpin mechanism of hepatitis C virus nonstructural 3 (NS3) protease inhibition: induced fit as a mechanism for narrow specificity. Richer, M.J., Juliano, L., Hashimoto, C., Jean, F. J. Biol. Chem. (2004) [Pubmed]
  2. A complex of serine protease genes expressed preferentially in cytotoxic T-lymphocytes is closely linked to the T-cell receptor alpha- and delta-chain genes on mouse chromosome 14. Crosby, J.L., Bleackley, R.C., Nadeau, J.H. Genomics (1990) [Pubmed]
  3. Multiple extracellular activities in Drosophila egg perivitelline fluid are required for establishment of embryonic dorsal-ventral polarity. Stein, D., Nüsslein-Volhard, C. Cell (1992) [Pubmed]
  4. Dominant and recessive alleles of the Drosophila easter gene are point mutations at conserved sites in the serine protease catalytic domain. Jin, Y.S., Anderson, K.V. Cell (1990) [Pubmed]
  5. A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease. DeLotto, R., Spierer, P. Nature (1986) [Pubmed]
  6. CIAP1 and the serine protease HTRA2 are involved in a novel p53-dependent apoptosis pathway in mammals. Jin, S., Kalkum, M., Overholtzer, M., Stoffel, A., Chait, B.T., Levine, A.J. Genes Dev. (2003) [Pubmed]
  7. Levels of RNA from a family of putative serine protease genes are reduced in Drosophila melanogaster dunce mutants and are regulated by cyclic AMP. Yun, Y., Davis, R.L. Mol. Cell. Biol. (1989) [Pubmed]
  8. The serine protease Sp7 is expressed in blood cells and regulates the melanization reaction in Drosophila. Castillejo-López, C., Häcker, U. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  9. Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity. Zou, Z., Lopez, D.L., Kanost, M.R., Evans, J.D., Jiang, H. Insect Mol. Biol. (2006) [Pubmed]
  10. Recombinant prolylcarboxypeptidase activates plasma prekallikrein. Shariat-Madar, Z., Mahdi, F., Schmaier, A.H. Blood (2004) [Pubmed]
  11. The making of a fly leg: a model for epithelial morphogenesis. von Kalm, L., Fristrom, D., Fristrom, J. Bioessays (1995) [Pubmed]
  12. Fluorescently labeled inhibitors detect localized serine protease activities in Drosophila melanogaster pole cells, embryos, and ovarian egg chambers. Jakobsen, R.K., Ono, S., Powers, J.C., DeLotto, R. Histochem. Cell Biol. (2005) [Pubmed]
  13. Induction of a putative serine protease transcript in immune challenged Drosophila. Coustau, C., Rocheleau, T., Carton, Y., Nappi, A.J., ffrench-Constant, R.H. Dev. Comp. Immunol. (1996) [Pubmed]
  14. Association of a protease with polytene chromosomes of Drosophila melanogaster. Cavagnaro, J., Pierce, D.A., Lucchesi, J.C., Chae, C.B. J. Cell Biol. (1980) [Pubmed]
  15. Evidence for the ancient origin of the NF-kappaB/IkappaB cascade: its archaic role in pathogen infection and immunity. Wang, X.W., Tan, N.S., Ho, B., Ding, J.L. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  16. Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Lee, S.Y., Cho, M.Y., Hyun, J.H., Lee, K.M., Homma, K.I., Natori, S., Kawabata, S.I., Iwanaga, S., Lee, B.L. Eur. J. Biochem. (1998) [Pubmed]
  17. Genome wide analysis of transcript levels after perturbation of the EGFR pathway in the Drosophila ovary. Jordan, K.C., Hatfield, S.D., Tworoger, M., Ward, E.J., Fischer, K.A., Bowers, S., Ruohola-Baker, H. Dev. Dyn. (2005) [Pubmed]
  18. Regulation of Easter activity is required for shaping the Dorsal gradient in the Drosophila embryo. Chang, A.J., Morisato, D. Development (2002) [Pubmed]
  19. Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae. Dimopoulos, G., Richman, A., della Torre, A., Kafatos, F.C., Louis, C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  20. Spatially dependent activation of the patterning protease, Easter. LeMosy, E.K. FEBS Lett. (2006) [Pubmed]
  21. Evidence of serine-protease activity closely associated with Drosophila alcohol dehydrogenase. Fibla, J., Atrian, S., Gonzàlez-Duarte, R. Eur. J. Biochem. (1993) [Pubmed]
  22. Interallelic complementation at the Drosophila melanogaster gastrulation defective locus defines discrete functional domains of the protein. Ponomareff, G., Giordano, H., DeLotto, Y., DeLotto, R. Genetics (2001) [Pubmed]
  23. Recognition of pathogens and activation of immune responses in Drosophila and horseshoe crab innate immunity. Kurata, S., Ariki, S., Kawabata, S. Immunobiology (2006) [Pubmed]
 
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