Background: Solute carrier family 27 family (SLC27As) have been identified to be involved in long chain fatty acid uptake in various tissues and cells, but their function in buffalo is unclear. Buffalo is an important dairy animal in some parts of the world. Buffalo milk contains more fat, protein, lactose and minerals than cow’s milk. The objective of this study was to identify the buffalo SLC27A1, 2 and 6 genes and to describe their characteristics, structure and basic function. Methods: The full-length coding sequences (CDSs) of SLC27A1, 2 and 6 were isolated from Binglangjiang buffalo and bioinformatics analyses were used to provide insights into the physicochemical characteristics, structure and function of their encoded proteins. Result: The CDSs of buffalo SLC27A1, 2 and 6 were 1941 bp, 1863 bp and 1905 bp in length, respectively, encoding 646, 620 and 634 amino acid residues accordingly. Their proteins FATP1, 2 and 6 have no signal peptide but a transmembrane helix with the N-terminus located outside the membrane and the C-terminus located in cytoplasmic side. All three proteins contain AMP-binding domains that belonged to AFD_class_I superfamily and may play a crucial role in the transport of fatty acids. The amino acid sequences of buffalo FATP1, 2 and 6 showed more than 88.6% identity with other species of Bovidae and more than 76.4% identity with other species of mammals. The phylogenetic tree showed that buffalo FATP1, 2 and 6 clustered in their respective clades and buffalo was more closely genetically related to other species of the Bovidae family. These findings suggest that buffalo FATPs are more similar in function to other species. The present study will provide a theoretical basis for further investigation of the functions of FATP1, 2 and 6 in buffalo lipid metabolism, especially milk fat metabolism.
Read full abstract