Crystallin Beta A1 (CRYbA1)

CRYB1; Eye Lens Structural Protein

Crystallin Beta A1 (CRYbA1)
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.
CRYbA1, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)