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DNAJC3
DNAJC3 (DnaJ homolog subfamily C member 3, also known as P58, P58IPK, HP58, ERdj6 and PRKRI) is an endoplasmic reticulum co-chaperone of the DNAJ (HSP40) family. It takes part in the unfolded protein response and inhibits several eIF-2-alpha kinases. Browse Assay Genie's current range of DNAJC3 research reagents below, or read on for the biology behind the target.
DNAJC3 is involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. It acts as a negative regulator of EIF2AK4/GCN2 kinase activity by preventing phosphorylation of eIF-2-alpha at Ser-52, which attenuates general protein synthesis under ER stress, hypothermic and amino acid starvation conditions. DNAJC3 is also a co-chaperone of HSPA8/HSC70 and stimulates its ATPase activity. It may inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyse phosphorylation of EIF2A, and it may also inhibit EIF2AK3/PERK activity.
The DNAJC3 gene encodes a protein with multiple tetratricopeptide repeat (TPR) motifs and the highly conserved J domain found in members of the DNAJ chaperone family. It belongs to the tetratricopeptide repeat family of proteins and is classed by HGNC within the DNAJ (HSP40) heat shock proteins. The protein localises to the endoplasmic reticulum. Mouse and rat both carry a Dnajc3 ortholog.
The protein has been described as an inhibitor of the interferon-induced, dsRNA-activated protein kinase (PKR), which explains the aliases P58IPK and PRKRI. The gene was previously named DnaJ (Hsp40) homolog, subfamily C, member 3, and the ERdj6 name reflects its place among ER-resident J-domain proteins. Researchers studying DNAJC3 protein or the DNAJC3 gene often do so in the context of ER stress, translational control and chaperone biology.
DNAJC3 is involved in the UPR during ER stress and may inhibit PERK, making it a useful node for studying stress signalling.
By limiting eIF-2-alpha phosphorylation, DNAJC3 attenuates general protein synthesis under ER stress, hypothermic and amino acid starvation conditions.
As a co-chaperone of HSPA8/HSC70, DNAJC3 stimulates ATPase activity, which links J-domain proteins to chaperone cycle regulation.
DNAJC3 acts as an inhibitor of the interferon-induced, dsRNA-activated kinase PKR, relevant to studies of eIF-2-alpha kinase control.
DNAJC3 is an ER co-chaperone involved in the unfolded protein response. It stimulates the ATPase activity of HSPA8/HSC70 and negatively regulates eIF-2-alpha kinases such as GCN2, and it may inhibit PKR and PERK, thereby attenuating general protein synthesis under stress.
DNAJC3 is also called P58, P58IPK, p58(IPK), HP58, ERdj6 and PRKRI. Its earlier HGNC name was DnaJ (Hsp40) homolog, subfamily C, member 3. The names P58IPK and PRKRI refer to its role as an inhibitor of the kinase PKR.
Yes. Mouse and rat each have an ortholog named Dnajc3. The human protein contains TPR motifs and a conserved J domain typical of DNAJ chaperones. Check the datasheet of any product for its validated reactivity.
Other DnaJ (HSP40) family members involved in chaperone function and protein folding.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13217; product specifications from Assay Genie datasheets.
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