Similar alternative splicing events generate two sarcoplasmic or endoplasmic reticulum Ca-ATPase isoforms in the crustacean Artemia franciscana and in vertebrates.

A second isoform of the Artemia franciscana sarcoplasmic or endoplasmic reticulum Ca-ATPase has been identified through the isolation of cDNA clones. This isoform differs from the previously identified one only at the C-terminal end of the protein. The last 6 amino acids of the former isoform change to 30 hydrophobic amino acids in the newly identified isoform that have the potentiality of being an additional transmembrane domain. The two A. franciscana isoforms are highly homologous to the two isoforms coded by the mammalian and bird SERCA2 gene, except that the C-terminal extensions share their hydrophobic character but have no significant amino acid homology. The isolation of genomic clones coding for this region of the gene shows that both isoforms arise from the same gene by alternative splicing. The donor splicing site of the penultimate exon can either be recognized and fused to the last exon, giving rise to the mRNA coding for the shortest protein, or remain unrecognized, in which case a polyadenylation site is recognized before the last exon of the gene and the mRNA coding for the largest protein is originated. The alternative splicing used to originate the two isoforms is similar in Artemia and vertebrates. The conservation of the alternative splicing between species so distant in evolution suggests an important physiological role for the existence of the two isoforms of the protein.