Phylogenetic, molecular and evolutionary study of PALM gene in sheep

Paralemmin, novel lipid-anchored membrane protein, involved in cell process formation. In this study nucleotide and amino acid sequences of PALM gene in sheep and several other species, were obtained from the NCBI and BLAST databases. MotifScan software and Conserved Domain Database (CDD) to identify domains; PANTHER and ProDom servers to recognize motifs and potential performance of the Paralemmin protein and STRING software were applied to detect protein interactions with other proteins. Prediction of three-dimensional structure of protein was performed via I-TASSER and 2PHYRE software, and comparing the sequences and drawing phylogenetic tree, MEGA6 software was used. This protein has 3 motifs, which is involved in the regulation of cell shape, cytoskeleton organization and binding to protein kinase A and D3 Dopamine receptor. Prediction results of secondary and tertiary structures revealed the existence of coiled helix structure and its interaction with other proteins. Also phylogenetic results showed that under high selection pressure during the evolutionary process, PALM3 isoforms in all species have been isolated early rather than the other isoforms. Considering to existence of three motifs in sequence of Paralemmin protein and its structural similarity with A chain of Tropomyosin protein in sheep, this protein plays key role in interaction with other proteins in the level of cell membrane.