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. 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;peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric;proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early;development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is;monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant;gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have;been involved in cataract formation.
CRYGS; crystallin, gamma S; CRYG8; beta-crystallin S; crystallin; gamma 8; rncat; AI327013; CRBS_HUMAN; Crystallin, gamma 8; Crystallin, gamma polypeptide 8; Gamma crystallin S; Gamma S crystallin; Gamma-crystallin S; Gamma-S-crystallin; Opacity due to poor secondary fiber cell junction; recessive nuclear cataract; Opj; OTTHUMP00000210173; OTTHUMP00000210174; gamma S-crystallin