This article presents a genome-wide analysis of LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. The study identifies 51 LEA protein-encoding genes, which are classified into nine distinct groups. Expression analysis shows that all 51 genes are expressed under various conditions, with higher expression levels in seeds compared to vegetative tissues. Many genes contain ABRE and/or LTRE promoter elements, which are responsive to abscisic acid, cold, and drought. Approximately 33% of the genes are arranged in tandem repeats, and 43% are part of homeologous pairs. Most LEA proteins are predicted to be highly hydrophilic and natively unstructured, but some are folded. The study highlights the diversity of sequence, expression, and subcellular localization among LEA proteins. The high fraction of retained duplicate genes and inferred functional diversification suggest an evolutionary advantage for stress tolerance. The findings provide a comprehensive understanding of LEA proteins, which are crucial for cellular dehydration tolerance in various organisms. The study also discusses the functional significance of LEA proteins, their regulatory elements, and their structural and subcellular characteristics. The results indicate that LEA proteins play a key role in stress tolerance, and their expression is influenced by various environmental factors. The study emphasizes the importance of systematic biochemical and functional studies to elucidate the role of LEA proteins in plant stress tolerance.This article presents a genome-wide analysis of LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. The study identifies 51 LEA protein-encoding genes, which are classified into nine distinct groups. Expression analysis shows that all 51 genes are expressed under various conditions, with higher expression levels in seeds compared to vegetative tissues. Many genes contain ABRE and/or LTRE promoter elements, which are responsive to abscisic acid, cold, and drought. Approximately 33% of the genes are arranged in tandem repeats, and 43% are part of homeologous pairs. Most LEA proteins are predicted to be highly hydrophilic and natively unstructured, but some are folded. The study highlights the diversity of sequence, expression, and subcellular localization among LEA proteins. The high fraction of retained duplicate genes and inferred functional diversification suggest an evolutionary advantage for stress tolerance. The findings provide a comprehensive understanding of LEA proteins, which are crucial for cellular dehydration tolerance in various organisms. The study also discusses the functional significance of LEA proteins, their regulatory elements, and their structural and subcellular characteristics. The results indicate that LEA proteins play a key role in stress tolerance, and their expression is influenced by various environmental factors. The study emphasizes the importance of systematic biochemical and functional studies to elucidate the role of LEA proteins in plant stress tolerance.