[No authors listed]
cDNA clones encoding a glutamic acid-rich protein were isolated from a bovine retina cDNA expression library. The cDNA sequence contained an open reading frame of 1770 base pairs encoding a protein of 590 amino acids (64,509 Da) and untranslated regions of 60 and 490 base pairs at the 5' and 3' ends, respectively. The cDNA hybridized to a 2.4-kilobase retinal mRNA. The amino acid sequence derived from the cDNA sequence contains a glutamic acid-rich domain in which 68 of 109 amino acids are glutamic acid. In addition, this domain contains four repeats of a peptide of 11 amino acids and two repeats of a peptide of 26 amino acids. A polyclonal antibody raised against a decapeptide corresponding to the undecapeptide repeat sequence reacted with a protein in an extract of bovine rod outer segments, whose molecular mass, 65 kDa, corresponded to that of the above glutamic acid-rich protein. The retinal glutamic acid-rich protein showed homology with glutamic acid-rich proteins from bovine brain and the C-terminal region of mammalian neurofilaments.
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