Proteasomes are large, multisubunit particles that act as the proteolytic machinery for most regulated intracellular protein breakdown in eukaryotic cells. The core proteinase of this complex, the 20S proteasome, is comprised of four stacked rings with seven subunits each. The outer two rings are made up of seven, distinct α-type subunits, while the two inner rings are composed of seven, different β-type subunits. Here we present the cloning, sequencing and expression analysis of Carassius auratus, α2_ca, which encodes one of the proteasome α subunits from goldfish ovary. The cloned cDNA is 838 bp long and encodes 234 amino acids. The deduced amino acid sequence is highly homologous to α2 subunits from other vertebrates. The expression of mRNA for α2_ca occurs at very high levels in ovary and muscle and moderately high levels in testis, brain and gill. It was also shown that protein content was different from mRNA expression levels.