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zeta-crystallin; quinone oxidoreductase; NADPH:quinone reductase (CRYZ)

Function: - does not have alcohol dehydrogenase activity - binds NADP & acts through a one-electron transfer process - orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro) - may act in the detoxification of xenobiotics - interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species - enhances the stability of mRNA coding for BCL2 - NADPH binding interferes with mRNA binding NADPH + 2 quinone = NADP+ + 2 semiquinone Structure: - homotetramer - belongs to the Zn+2-containing alcohol dehydrogenase family, quinone oxidoreductase subfamily Compartment: cytoplasm Alternative splicing: named isoforms=2 Expression: only very low amounts found in the lens

General

crystallin quinone reductase

Properties

SIZE: entity length = 329 aa MW = 35 kD COMPARTMENT: cytoplasm MOTIF: cofactor-binding site [53-53] COFACTOR-BOUND: NADP cofactor-binding site [158-161] COFACTOR-BOUND: NADP cofactor-binding site [181-181] COFACTOR-BOUND: NADP cofactor-binding site [200-200] COFACTOR-BOUND: NADP cofactor-binding site [229-229] COFACTOR-BOUND: NADP cofactor-binding site [246-249] COFACTOR-BOUND: NADP cofactor-binding site [269-271] COFACTOR-BOUND: NADP

Database Correlations

OMIM 123691 UniProt Q08257 PFAM correlations Entrez Gene 1429 Kegg hsa:1429 ENZYME 1.6.5.5

References

  1. UniProt :accession Q08257
  2. Entrez Gene :accession 1429