Sequence of a 17 kDa vacuolar H(+)-ATPase proteolipid subunit from insect midgut and Malpighian tubules

Insect Biochem Mol Biol. 1993 Sep;23(6):675-80. doi: 10.1016/0965-1748(93)90041-p.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Digestive System / enzymology
  • Larva / enzymology
  • Malpighian Tubules / enzymology
  • Molecular Sequence Data
  • Moths / enzymology*
  • Moths / genetics
  • Proteolipids / chemistry*
  • Proteolipids / genetics
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / genetics
  • Sequence Homology, Amino Acid
  • Vacuoles / enzymology

Substances

  • Proteolipids
  • Proton-Translocating ATPases