Sequence of a 17 kDa vacuolar H(+)-ATPase proteolipid subunit from insect midgut and Malpighian tubules.
A 0.4 kb polymerase chain reaction (PCR) product obtained from cDNA made from the midgut and Malpighian tubules of fifth instar larvae of Heliothis virescens was used to screen a larval midgut and Malpighian tubules cDNA library. Four clones were obtained, one of 1.9 kb and others of 1.4 kb. The 1.9 kb clone encodes a 17.2 kDa protein which is highly homologous to other vacuolar ATPases proteolipids. Putative N-glycosylation and DCCD binding sites were observed at amino acid residues 83 and 139, respectively.
Pietrantonio
P V
PV
Department of Entomology, University of California, Riverside 92521.
Gill
S S
SS
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004064:Digestive System / Q000201:enzymology; D007814:Larva / Q000201:enzymology; D008317:Malpighian Tubules / Q000201:enzymology; D008969:Molecular Sequence Data; D009036:Moths / Q000201:enzymology* / Q000235:genetics; D011510:Proteolipids / Q000737:chemistry* / Q000235:genetics; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014617:Vacuoles / Q000201:enzymology
D011510:Proteolipids; D006180:Proton-Translocating ATPases