Aliases for CRYAA Gene
External Ids for CRYAA Gene
Previous HGNC Symbols for CRYAA Gene
Previous GeneCards Identifiers for CRYAA Gene
Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq, Jan 2014]
GeneCards Summary for CRYAA Gene
CRYAA (Crystallin Alpha A) is a Protein Coding gene. Diseases associated with CRYAA include Cataract 9, Multiple Types and Cataract 24. Among its related pathways are Protein processing in endoplasmic reticulum and Regulation of degradation of deltaF508 CFTR in CF. Gene Ontology (GO) annotations related to this gene include identical protein binding and structural constituent of eye lens. An important paralog of this gene is CRYAA2.
UniProtKB/Swiss-Prot Summary for CRYAA Gene
Contributes to the transparency and refractive index of the lens (PubMed:18302245). In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed:22120592, PubMed:31792453). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373).