Analysis of Keratin-Associated Protein-7 (KRTAP7) protein structure and function in Indian dromedary camel (Camelus dromedarius)

NISTHA  YADAV; URMILA  PANNU; BASANTI  JYOTSANA; VED  PRAKASH; GAYATRI  GUJAR; MANJU  NEHARA

doi:10.56093/ijans.v95i11.158678

Authors

NISTHA YADAV Animal Genetics and Breeding, Arawali Veterinary College Sikar-332403, Rajasthan, India
URMILA PANNU College of Veterinary and Animal Science, RAJUVAS, Bikaner-334001, Rajasthan, India
BASANTI JYOTSANA ICAR-National Research Center on Camel, Bikaner-334 001, Rajasthan, India
VED PRAKASH ICAR-National Research Center on Camel, Bikaner-334 001, Rajasthan, India
GAYATRI GUJAR College of Veterinary and Animal Science, Jodhpur-342037, Rajasthan, India
MANJU NEHARA College of Veterinary and Animal Science, Jodhpur-342037, Rajasthan, India

https://doi.org/10.56093/ijans.v95i11.158678

Keywords:

Camel Hair, Dromedary camel, Glycosylation sites, Insilico, KRTAP7 protein

Abstract

Studies on regulatory genes and proteins responsible for variation in hair quality attributes amongst Indian dromedary camel breeds are lacking. Keratin and keratin-associated proteins enable trichocytes, the hair-producing cells, to produce hair fibers. These proteins also specify the distinct molecular and structural properties of hair, fur, wool, and quills of the various animal species. The molecules of hair-keratin proteins are cross-linked by the keratin-associated proteins (KRTAPs), which are responsible for important properties of hair fibers, such as their thickness and curliness for its mechanical and physical characteristics. The amino acid sequence of KRTAP7 gene of Bikaneri, Kachchhi, Mewari and Jaisalmeri camel breeds were subjected to bioinformatics analysis using various bioinformatics software for determining the biophysical properties, the two-dimensional hydrophobicity or hydrophilicity plots, subcellular localization of the KRTAP7 protein and the protein-protein interaction. Prediction of various post-translational modifications (PTMs) for the KRTAP7 protein was done with specific server tools based on the neural network model. Prediction of secondary and three-dimensional (3-D) structures of KRTAP7 protein was also done. All four breeds shared identical KRTAP7 gene sequence with 87 amino acids long KRTAP7 protein. The KRTAP7 protein amino acid sequence revealed 13 phosphorylation sites, S-S bonding patterns, and glycosylation sites besides high hydrophilicity, high proportion of specific amino acids, absence of signal peptides, and internal acetylation sites. The protein-protein association networks predicted both direct and indirect interactions with other regulatory genes and proteins essential for the process of keratin biosynthesis and hair characteristics.

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