Genome-wide characterization of Major Intrinsic Proteins (MIPs) family in Momordica charantia

Shifa Begum 1, * and Ruhul A. Khan

1 Department of Genetic Engineering and Biotechnology, University of Chittagong, Chittagong-4331, Bangladesh.
2 Institute of Radiation and Polymer Technology, Atomic Energy Research Establishment, Savar, Dhaka, Bangladesh.
 
Research Article
GSC Biological and Pharmaceutical Sciences, 2022, 18(02), 111–129.
Article DOI: 10.30574/gscbps.2022.18.2.0047
Publication history: 
Received on 24 December 2021; revised on 27 January 2022; accepted on 29 January 2022
 
Abstract: 
Major intrinsic proteins (MIPs) family include the group of proteins also called channel proteins or water channels. Aquaporins facilitate the transport of water and other uncharged small molecules, forming pores in cellular boundaries which help in plant growth, development, and sometimes in plant adaptation. They usually have six tranSmembrane alpha-helical domains with conserved amino acids residues along with hydrophobic and hydrophilic regions. Though aquaporins were found both in animals and plants, also in bacteria, fungi cells, it comprises the largest and most complex group in plant species. A little is known about the aquaporins family of the plant Momordica charantia. About 25 aquaporins of its are characterized in this study. The aquaporins of M. charantia are divided into five sub-families here, they are PIPs, TIPs, XIPs, SIPs, and NIPs. There are twelve PIPs, three TIPs, eight NIPs, and one AQPs in both XIP and SIP. In the XIP subfamily, it contains SPI other than the NPA motif. Moreover, SIP and NIP subfamily also contain different motifs both in loop B and loop E other than NPA motifs. McSIPs contain NPT in loop B and McNIPs contain NPS in loop B (McNIP1; 1, McNIP1; 3 and McNIP3; 1). Again, McNIPs contain NPV in loop E (McNIP2; 2, McNIP3; 1). The conserved residues and motifs of this plant show its transportation of water and the possibility of other molecules' transportation through those channel proteins.
 
Keywords: 
Intrinsic protein; Aquaporin; Amino acid; Protein channel
 
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