Primary structure of V-ATPase subunit B from Manduca sexta midgut.
The amino acid sequence of a vacuolar-type ATPase (V-ATPase) subunit B has been deduced from a cDNA clone isolated from a Manduca sexta larval midgut library. The library was screened by hybridization with a labeled cDNA encoding subunit B of Arabidopsis thaliana tonoplast V-ATPase. The M. sexta V-ATPase subunit B consists of 494 amino acids with a calculated M(r) of 54,902. The amino acid sequence deduced for V-ATPase subunit B of M. sexta is between 98% and 76% identical with that of seven other V-ATPase subunits B and greater than 52% identical with three archaebacterial ATPase subunits B.
Novak
F J
FJ
Department of Biology, Temple University, Philadelphia, PA 19122.
Gräf
R
R
Waring
R B
RB
Wolfersberger
M G
MG
Wieczorek
H
H
Harvey
W R
WR
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004064:Digestive System / Q000201:enzymology; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009036:Moths / Q000201:enzymology*; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D025262:Vacuolar Proton-Translocating ATPases; D014617:Vacuoles / Q000201:enzymology
D046911:Macromolecular Substances; D004247:DNA; D000251:Adenosine Triphosphatases; D025262:Vacuolar Proton-Translocating ATPases