CRYGC

Crystallin, gamma C, also known as CRYGC, is a is_associated_with::protein which in humans is encoded by the CRYGC is_associated_with::gene.

Function
is_associated_with::Crystallins are separated into two classes: is_associated_with::taxon-specific, or is_associated_with::enzyme, and ubiquitous. The latter class constitutes the major is_associated_with::proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting is_associated_with::peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, is_associated_with::monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three is_associated_with::pseudogenes (gamma-E, gamma-F, gamma-G) are organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in is_associated_with::cataract formation.

Interactions
CRYGC has been shown to interact with is_associated_with::CRYBB2, is_associated_with::CRYAA and is_associated_with::CRYAB.