HSP70 — Camelina sativa

Summary

CSA11G020460 (HSP70, CsHSC70-7) encodes a member of the Hsp70 family of molecular chaperones, possessing ATP hydrolase activity, heat shock protein binding, and protein folding chaperone functions, along with additional annotated activities including ethene binding, histidine kinase activity, and SUMO transferase activity. The gene is associated with protein folding in the endoplasmic reticulum, the ER unfolded protein response, ERAD pathway, protein-chloroplast targeting, sumoylation, MAPK cascade, brassinosteroid-mediated signalling, and downregulation of ethylene-mediated signalling. It is linked to responses to heat, salt, and hypoxia, as well as pollen germination and development, embryo development ending in seed dormancy, and traits including leaf position, stem elongation, stomatal resistance and opening, leaf senescence, flowering time, seed growth, root morphology, and abscisic acid sensitivity. The protein localises to the ER lumen and chaperone complex, plastid stroma, thylakoid, chloroplast envelope, tonoplast, and apoplast. Related genes in other species link the family to thermotolerance, osmotic stress tolerance, ROS scavenging, and chloroplast development.