[11] The protein DNAJC28 is 388 amino acids long and contains a conserved N-terminal J (DnaJ) domain, which is critical for interaction with Hsp70s.
[12] Molecular weight and isoelectric point of human DNAJC28 without post-translational modification are 45.8 kDal and 9.57 pI, respectively.
J domains are highly conserved and are an integral part of protein translation, folding, translocation, and degradation through stimulating the ATPase activity of members of the Hsp70 family.
[18] There is a coiled-coil region from approximately amino acids 288 to 318 that is conserved throughout all listed orthologs (through fungi and plants).
[31] A mitochondrial targeting signal presequence traditionally has a high composition of arginine, a very low amount of negatively charged residues at the N-terminus, and forms an amphipathic helix with a positively charged side and a hydrophobic side opposite it.
[16] Heat Shock Protein genes are generally activated when the cell is exposed to stress, such as high temperature, infection, and low oxygen.
[39] The Hsp70/Hsp40 chaperone system works in proteostasis processes, which involves breaking down protein aggregations like a-synuclein which accumulates in Parkinson’s disease.
[40] A study found that damaging missense variants of DNAJC28 are likely related to sporadic late-onset Parkinson’s disease.
[41] DNAJC28 was found to be excessively expressed in the hippocampus of the lupus-prone mice model MRL/lpr during TWEAK (TNF-like weak inducer of apoptosis) activation, which is associated with the neuropsychiatric impacts of lupus.
[42] Overexpression of other genes in the DnaJ family has been shown to contribute to neuroprotective effects in multiple neurodegenerative disease models.