HSP70 — Camelina sativa

Summary

CsHSP70-8 (CSA05G026860) on Camelina sativa chromosome 5 encodes a member of the Hsp70 family, characterized by an ATPase nucleotide-binding domain and a peptide-binding domain, with ATP hydrolase activity, ATP binding, heat shock protein binding, and protein folding chaperone functions. The gene is associated with protein folding and refolding, the endoplasmic reticulum unfolded protein response (erUPR), the ERAD pathway, the MAPK cascade, signal transduction, and responses to stress, heat, salt, and virus. It is linked to localization in the ER lumen, ER chaperone complex, cytoplasm, nucleus, membrane, and chloroplast membrane. Related genes in other species are linked to similar stress-responsive chaperone roles.