Primary structure of frog rhodopsin.
Amphibians have been employed extensively to study the anatomy, physiology, biochemistry, and cell biology of the visual system for decades, yet there have been no reports concerning the primary structure of amphibian visual transduction components. Thus, we have determined the entire nucleotide sequence of frog (Rana pipiens) rhodopsin cDNA, including a putative transcription start point and poly A tail, by sequence analysis of PCR products and mRNA. The open reading frame predicts an opsin of 354 residues, six residues longer than the mammalian rod opsins, containing 11 potential phosphorylation sites in the C-terminal domain. RNA blot analysis revealed two transcripts of ca. 1.7 and 3.1 kb. Frog rhodopsin exhibits approximately 85% identity to mammalian rhodopsin at the amino acid level. Sequence analysis of additional components will produce the framework from which a more detailed understanding of amphibian phototransduction can emerge.
Pittler
S J
SJ
Department of Ophthalmology, Cullen Eye Institute, Baylor College of Medicine, Houston, TX 77030.
Fliesler
S J
SJ
Baehr
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D006801:Humans; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D011894:Rana pipiens; D012243:Rhodopsin / Q000737:chemistry*
D012243:Rhodopsin