2-Aminoethanethiol Dioxygenase (ADO)
C10orf22; Cysteamine Dioxygenase
To identify the ADO protein, Dominy et al. (2007) searched in silico for sequences similar to those in CDO, including the cupin motif, which is found in proteins that bind metal cofactors. In CDO, which binds iron, the cupin motif is unusual in the lack of a conserved glutamate. Dominy et al. (2007) identified a predicted 771-amino acid Ado protein (Gm237) in mouse that had about 14% overall sequence identity with CDO and, like CDO, was missing the highly conserved glutamate found in other cupins. Dominy et al. (2007) also identified a human ortholog, which shares 85% sequence similarity with the mouse protein. An antibody raised against mouse Ado showed that the protein is ubiquitously expressed, with highest levels in brain, heart, and skeletal muscle. This pattern differs from that of CDO, which is primarily expressed in liver.
Organism species: Homo sapiens (Human)
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Organism species: Mus musculus (Mouse)
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Organism species: Rattus norvegicus (Rat)
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