The primary structure of iodopsin, a chicken red-sensitive cone pigment

Osamu Kuwata, Yasushi Imamoto, Toshiyuki Okano, Koichi Kokame, Daisuke Kojima, Hiroki Matsumoto, Akihiro Morodome, Yoshitaka Fukada, Yoshinori Shichida, Kunio Yasuda, Yoshiro Shimura, Tôru Yoshizawa

Research output: Contribution to journalArticle

65 Citations (Scopus)


A purified iodopsin was digested by CNBr or several proteolytic enzymes into fragments, the amino acid sequences of which were determined. A partial sequence of the C-terminal fragment was utilized for synthesizing an oligonucleotide probe which identified the iodopsin cDNA (1339 bases). The deduced amino acid sequence (362 residues) had 80%, 42% or 43% homology to that of human red-sensitive cone pigment, cattle or chicken rhodospin, respectively. Although the hydropathy profile implies that iodopsin, like rhodopsin, has 7 transmembrane α-helical segments, iodopsin may have a hydrophilic pocket near the seventh segment on the basis of the unexpected cleavages in the middle of the segment VII by chymotrypsin under nondenaturing conditions.

Original languageEnglish
Pages (from-to)128-132
Number of pages5
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 1990 Oct 15
Externally publishedYes


  • Chicken retina
  • Color vision
  • Cone visual pigment
  • Iodopsin
  • Primary structure
  • cDNA cloning

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Kuwata, O., Imamoto, Y., Okano, T., Kokame, K., Kojima, D., Matsumoto, H., Morodome, A., Fukada, Y., Shichida, Y., Yasuda, K., Shimura, Y., & Yoshizawa, T. (1990). The primary structure of iodopsin, a chicken red-sensitive cone pigment. FEBS Letters, 272(1-2), 128-132.