Aquaporins (AQPs) are membrane channel proteins which facilitate the rapid transport of water across cellular membrane and are of fundamental importance to the control of cell volume and transcellular water traffic. In the present study using bioinformatic tools an in silico modeling and analysis of aquaporin protein sequences of catfish Heteropneustes fossilis was conducted. Primary structure prediction and physiochemical characterization were performed by computing theoretical isoelectric point (pI), molecular weight, extinction coefficient, instability index and aliphatic index. Secondary structure assessment of aquaporin protein of Indian catfish using GOR IV reveals greater percentage of residues as alpha helix and random coils against the beta sheets. After performing homology modeling using MODELLER, a 3D structure of aquaporin of Indian catfish have been predicted from its amino acid sequence. After the prediction structure has been validated through various validation tools. This homology modeling based structure will provide an insite to its functional aspect and further studies which are based on tertiary structure of protein. Active site of aquaporin protein has been predicted using DoGSite scorer. Analysis of aquaporin active site will provide an insight to more précised functional characterization of this protein. In future, present study will allow the designing of mutant and inhibitors for the study of physiological role of aquaporin protein in Heteropneustes fossilis
