The sequence of human retinal S‐antigen reveals similarities with α‐transducin

FEBS Letters

Tsuda, Masahiko¹  Shinohara, Toshimichi¹  Yamaki, Kunihiko¹ 

[1] Molecular Biology Section, Laboratory of Immunology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA

关键词: S-antigen;    48-kDa protein;    Human cDNA;    Amino acid sequence;    Uveitis;    Visual process;    NBRF;    National Biomedical Research Foundation;    EAU;    experimental autoimmune uveitis;    R*;    photoactivated rhodopsin;    R*P;    phosphorylated photoactivated rhodopsin;    CD;    circular dichroism;    Td;    transducin;    PDE;    phosphodiesterase;    cGMP;    cyclic guanosine monophosphate;   

DOI  :  10.1016/0014-5793(88)81298-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of human retinal S-antigen (48 kDa protein), a retinal protein involved in the visual process has been determined by cDNA sequencing. The largest cDNA was 1590 base pairs (bp) and it contained an entire coding sequence. The similarity of nucleotide sequence between the human and bovine is approximately 80%. The predicted amino acid sequence indicates that human S-antigen has 405 residues and its molecular mass is 45050 Da. The amino acid sequence homology between human and bovine is 81%. There is no overall sequence similarity between S-antigen and other proteins listed in the National Biomedical Research Foundation (NBRF) protein data base. However, local regions of sequence homology with α-transducin (Tα) are apparent including the putative rhodopsin binding and phosphoryl binding sites. In addition, human S-antigen has sequences identical to bovine uveitopathogenic sites, indicating that some types of human uveitis may in part be related to the animal model of experimental autoimmune uveitis (EAU).

【 授权许可】

Unknown