This article provides a comprehensive analysis of LEA (Late Embryogenesis Abundant) proteins and their encoding genes in *Arabidopsis thaliana*. The authors identified 51 LEA protein-encoding genes, which were classified into nine distinct groups. Expression studies using quantitative RT-PCR revealed that all 51 genes were expressed, with higher levels in seeds compared to vegetative tissues. Most genes contained abscisic acid response (ABRE) and/or low temperature response (LTRE) elements in their promoters, and many were induced by abscisic acid, cold, or drought. The study also found that 33% of the genes are arranged in tandem repeats and 43% are part of homeologous pairs. The majority of LEA proteins were predicted to be highly hydrophilic and natively unstructured, but some were folded. The analyses indicate a wide range of sequence diversity, intracellular localizations, and expression patterns, suggesting that LEA proteins play crucial roles in cellular dehydration tolerance under various stressful environmental conditions. The high fraction of retained duplicate genes and functional diversification indicate evolutionary advantages for organisms under varying stress conditions.This article provides a comprehensive analysis of LEA (Late Embryogenesis Abundant) proteins and their encoding genes in *Arabidopsis thaliana*. The authors identified 51 LEA protein-encoding genes, which were classified into nine distinct groups. Expression studies using quantitative RT-PCR revealed that all 51 genes were expressed, with higher levels in seeds compared to vegetative tissues. Most genes contained abscisic acid response (ABRE) and/or low temperature response (LTRE) elements in their promoters, and many were induced by abscisic acid, cold, or drought. The study also found that 33% of the genes are arranged in tandem repeats and 43% are part of homeologous pairs. The majority of LEA proteins were predicted to be highly hydrophilic and natively unstructured, but some were folded. The analyses indicate a wide range of sequence diversity, intracellular localizations, and expression patterns, suggesting that LEA proteins play crucial roles in cellular dehydration tolerance under various stressful environmental conditions. The high fraction of retained duplicate genes and functional diversification indicate evolutionary advantages for organisms under varying stress conditions.