The Primary Structure of Mantid Opsin

Gene. 1994 Jun 10;143(2):227-31. doi: 10.1016/0378-1119(94)90101-5.

Abstract

The sequence encoding opsin from the mantid Sphodromantis sp. has been determined by dideoxynucleotide sequencing of PCR products from a cDNA derived from eye cup tissue. The 376-amino-acid (aa) residues show approx. 56% identity and 85% similarity to known insect opsins (Drosophila melanogaster and Calliphora erythrocephala). The predicted protein structure, based on the hydropathy profile and placement of key aa residues, reveals a seven-transmembrane structure typical of a rhodopsin. Unlike the previously characterised insect visual pigments which have 3-hydroxy retinal in their binding sites, mantid rhodopsin contains 11-cis retinal. Comparison of transmembrane sequences from the opsin family was performed in order to identify any specific aa substitutions which are able to account for the selection of retinal or its 3-hydroxy derivative by insect opsins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Hydrogen Bonding
  • Molecular Sequence Data
  • Orthoptera / chemistry*
  • Polymerase Chain Reaction
  • Protein Structure, Secondary
  • Retinaldehyde / analogs & derivatives
  • Retinaldehyde / metabolism
  • Rod Opsins / chemistry*
  • Rod Opsins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Rod Opsins
  • 3-hydroxyretinal
  • Retinaldehyde

Associated data

  • GENBANK/X71665