Abstract:
-ATP-Binding cassette (ABC) proteins are a kind of transporter found in eukaryotes and prokaryotes that regulates the transit of chemicals between the internal and external environments as well as between body organs. These proteins are present in cell membrane and function as ATP-dependent biochemical pumps that enable a variety of metals and organic molecules to leave the cell. The present study was aimed to characterize ABC superfamily so as to identify its members, their physiochemical properties and mutations in Tilapia fish. To identify the ABC genes, genomic sequences of zebra fish were used as a query to retrieve related sequences from NCBI. These sequences were then blasted for identification and validation of ABC genes in Tilapia. Phylogenetic analysis, gene structure and mutation analysis were performed using bioinformatics tools. Phylogenetic analysis revealed 42 ABC transporter genes in the tilapia genome that are classified and grouped as follows: 7 ABCAs, 7 ABCBs, 11 ABCCs, 4 ABCDs, 1 ABCEs, 3 ABCFs, 8 ABCGs and 1 ABCH. Overall, phylogenetic relationship revealed that tilapia ABC gene family is more closely related to zebrafish and common carp. Gene structure analysis revealed that the ABC transporters consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved trans membrane domain (TMD). Ten different motifs of ABC gene family were observed in Tilapia including motif 1 and 3 (consisting of 41 and 28 amino acids) which were annotated as the ABC trans domain, while 8 motifs were annotated as ABC membrane in Pfam search. In conclusion, the findings of the present study help to better understand the evolution of ABC gene family in Tilapia fish. Furthermore, identified mutations can help in selection of fish for efficient energy utilization and growth.
Page(s):
0-0
DOI:
DOI not available
Published:
Journal: First International Conference on Revamped Scientific Outlook of 21st Century (Abstract Book), Volume: 0, Issue: 0, Year: 2022