DnaJ/HSP40 Homolog Subfamily C, Member 6 (DNAJC6)

DNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus, a glycine/phenylalanine (G/F)-rich region, and a cysteine-rich domain containing 4 motifs resembling a zinc-finger domain.

The predicted protein contains 913 amino acids and shares 95% amino acid identity with bovine auxilin. the 910-amino acid bovine auxilin protein, which is homologous to DNAJC6, has a J domain at residues 841 to 910, but it does not have G/F-rich or cys-rich domains. PSORT analysis suggested both a nuclear and cytoplasmic localization.