CRYZ
Sign in to saveAlso known as crystallin zeta
Quinone oxidoreductase is an enzyme that in humans is encoded by the CRYZ gene.
Gene data
CRYZ- Name
- crystallin zeta
- Type
- protein-coding
- Position
- 74,701,488–74,733,104 (−)
- Ensembl
- ENSG00000116791
- RefSeq RNA
- NM_001130042.2, NM_001130043.2, NM_001134759.2, NM_001889.4, XM_011540747.3
- RefSeq protein
- NP_001123514.1, NP_001123515.1, NP_001128231.1, NP_001880.2, XP_011539049.1
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. The former class is also called phylogenetically-restricted crystallins. This gene encodes a taxon-specific crystallin protein which has NADPH-dependent quinone reductase activity distinct from other known quinone reductases. It lacks alcohol dehydrogenase activity although by similarity it is considered a member of the zinc-containing alcohol dehydrogenase family. Unlike other mammalian species, in humans, lens expression is low. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. One pseudogene is known to exist. [provided by RefSeq, Sep 2008].
Gene Ontology
Biological process
Molecular function
Cellular component
via MyGene.info
Wikidata facts
- Image
- Protein CRYZ PDB 1yb5.png
Show 5 more facts
- HomoloGene ID
- 133907
- exact match
- identifiers.org/ncbigene/1429
- genomic end
- 75199092
- genomic start
- 75171170
- cytogenetic location
- 1p31.1
Sources (3)
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Quinone oxidoreductase is an enzyme that in humans is encoded by the CRYZ gene.
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. The former class is also called phylogenetically-restricted crystallins. This gene encodes a taxon-specific crystallin protein which has NADPH-dependent quinone reductase activity distinct from other known quinone reductases. It lacks alcohol dehydrogenase activity although by similarity it is considered a member of the zinc-containing alcohol dehydrogenase family. Unlike other mammalian species, in humans, lens expression is low. One pseudogene is known to exist.