Sodium and Potassium ATPase of the Teleost FishCatostomus commersoni.Sequence, Protein Structure and Evolutionary Conservation of the α-Subunit

Autor: Karl Lederis, Christiane Schönrock, Dietmar Richter, Yuji Okawara, Steven D. Morley
Rok vydání: 1991
Předmět:
Zdroj: Biological Chemistry Hoppe-Seyler. 372:279-286
ISSN: 0177-3593
DOI: 10.1515/bchm3.1991.372.1.279
Popis: The alpha-subunit of a Na+/K+ ATPase has been cloned by analysing a lambda gt11 library constructed from polyA+ RNA from the hypothalamic region of the teleost fish Catostomus commersoni (white sucker). The cDNA clone consists of 3853 bp and predicts a protein of 1027 amino-acid residues. Alignment of the sucker sequence with protein sequences previously published for alpha-subunits from various species reveals a high degree of homology throughout the entire sequence containing five potential sites for N-glycosylation, a phosphorylation site and a site for binding fluorescein 5'-isothiocyanate (FITC). A hydropathy profile predicts a secondary structure of the Na+/K+ ATPase alpha-subunit with at least eight membrane-spanning domains. Northern and southern blot analyses suggest the existence of two distinct Na+/K+ ATPase alpha-subunit genes in the sucker genome.
Databáze: OpenAIRE