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Literature summary for 3.4.22.29 extracted from

  • Qiu, Y.; Ye, X.; Zhang, H.M.; Hanson, P.; Zhao, G.; Tong, L.; Xie, R.; Yang, D.
    Cleavage of osmosensitive transcriptional factor NFAT5 by Coxsackieviral protease 2A promotes viral replication (2017), PLoS Pathog., 13, e1006744 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.29

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nuclear factor of activated T cells 5/tonicity enhancer binding protein Coxsackievirus B3 NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, inactivation of NFAT5 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Coxsackievirus B3
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nuclear factor of activated T cells 5/tonicity enhancer binding protein NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, inactivation of NFAT5 Coxsackievirus B3 ?
-
 ?
nuclear factor of activated T cells 5/tonicity enhancer binding protein NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, which is the only CVB3 protease 2A cleavage site on NFAT5, leading to inactivation of NFAT5 Coxsackievirus B3 ?
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 ?

Synonyms

Synonyms Comment Organism
2Apro
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 Coxsackievirus B3
protease 2A
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 Coxsackievirus B3

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Coxsackievirus B3

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Coxsackievirus B3

General Information

General Information Comment Organism
physiological function the enzyme cleaves cellular transcription factor nuclear factor of activated T cells 5/tonicity enhancer binding protein (NFAT5/TonEBP). The 70-kDa N-terminal cleavage product (p70-NFAT5, amino acid residues 175-471 within the N-terminal fragment of NFAT5) exerts a dominant negative effect on the full-length NFAT5 protein. Elevated expression of NFAT5 to counteract viral protease cleavage, especially overexpression of a non-cleavable mutant of NFAT5, significantly inhibits CVB3 replication. Ectopic expression of NFAT5 results in elevated expression of inducible nitric oxide synthase (iNOS), a factor reported to inhibit CVB3 replication. The anti-CVB3 activity of NFAT5 is impaired during CVB3 infection due to 2A-mediated cleavage of NFAT5 Coxsackievirus B3