Sequence analysis of bovine retinal S-antigen: Relationships with α-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 a-transd...

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Bibliographic Details
Published in:FEBS letters 1986-02, Vol.196 (1), p.23-28
Main Authors: Wistow, Graeme J., Katial, Albine, Craft, Cheryl, Shinohara, Toshimichi
Format: Article
Language:English
Subjects:
ADP-ribosylation
Amino Acid Sequence
Animals
antigen S
Antigens - analysis
Arrestin
Base Sequence
Bovine retina
Cattle
cDNA sequence
DNA - analysis
GTP-Binding Proteins - analysis
Membrane Proteins - analysis
nucleotide sequence
Recombinant Proteins - analysis
retina
S-Antigen
Sequence Homology, Nucleic Acid
Transducin
Uveitis
α-Transducin
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Summary: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 a-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 α-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 β-structure in the C-terminal half of S-antigen, with a monoclonal antibody epitope in a helical region at the C-terminus.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)80207-1