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. Beta-crystallins, the most heterogeneous, differ by the presence of the;C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of;different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins.;This gene, a beta acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3.
CRYBA4; crystallin, beta A4; beta-crystallin A4; Beta A4 crystallin; Beta crystallin A4; Beta-A4 crystallin; CRBA4_HUMAN; Crystallin beta A4; Eye lens structural protein; lens structural protein; crystallin, beta polypeptide A4; MCOPCT4; zgc:109979