Sequence analysis of bovine retinal S-antigen. Relationships with alpha-transducin and G-proteins.
S-Antigen is a major soluble protein of the retina and pineal. It is capable of inducing experimental autoimmune uveitis (EAU) in laboratory animals and also seems to play an important role in the visual cycle. The results of partial cDNA sequence analysis reveal interesting homologies with alpha-transducin, a GTP-binding protein of retina and other purine nucleotide-binding proteins. In particular S-antigen shows over 50% identity to the proposed pertussis toxin ADP-ribosylation site of alpha-transducin. It also contains the Gly-X-X-X-X-Gly-Lys pattern common to phosphoryl binding sites. A possible relationship between S-antigen and purine nucleotide-binding proteins is discussed. There is also evidence for a repetitious beta-structure in the C-terminal half of S-antigen, with a monoclonal antibody epitope in a helical region at the C-terminus.
Wistow
G J
GJ
Katial
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Craft
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Shinohara
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D000595:Amino Acid Sequence; D000818:Animals; D000941:Antigens / Q000032:analysis*; D019393:Arrestin; D001483:Base Sequence; D002417:Cattle; D004247:DNA / Q000032:analysis; D019204:GTP-Binding Proteins / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D011994:Recombinant Proteins / Q000032:analysis; D012689:Sequence Homology, Nucleic Acid; D015293:Transducin
D000941:Antigens; D019393:Arrestin; D008565:Membrane Proteins; D011994:Recombinant Proteins; D004247:DNA; D019204:GTP-Binding Proteins; D015293:Transducin