HSP70 — Camelina sativa

Summary

CsHSC70-7 (CSA18G020420) encodes a member of the HSP70 chaperone family, characterized by DnaK, ATPase_NBD, and heat shock 70 domains, with ATP hydrolase activity, protein folding chaperone function, and ethene binding. In Camelina sativa, this 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 signaling, and downregulation of ethylene signaling. 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, trichome morphology, flowering time, seed development, root morphology, and abscisic acid sensitivity. The protein localizes to the ER lumen, plastid stroma, thylakoid, chloroplast envelope, and apoplast. Studies of related genes in other species link the family to chloroplast development, thermotolerance, and osmotic stress tolerance.