Primary structure and expression of the human beta-subunit and related proteins of the rod photoreceptor cGMP-gated channel.

The Journal of Biological Chemistry
C A Colville, R S Molday

Abstract

The full-length cDNA for the beta-subunit of the human rod photoreceptor cyclic nucleotide-gated channel has been shown to encode a 1251-amino acid ( approximately 140 kDa) polypeptide which, like its bovine counterpart, has an unusual bipartite structure. The C-terminal part corresponds to the previously reported "subunit 2" of the human rod channel and contains the structural features of other cyclic nucleotide-gated channel subunits including six putative membrane spanning segments, a cyclic nucleotide binding domain, a voltage-sensor motif, and a pore region. The N-terminal part contains the human homolog of the bovine glutamic acid-rich protein called GARP. Western blots indicate that both the native and heterologously expressed human beta-subunit migrate anomalously as a 220-kDa polypeptide by SDS-gel electrophoresis. Two other GARP variants, full-length GARP (f-GARP) and truncated GARP (t-GARP), are also present in human, bovine, and rat rod outer segments and migrate as 120-140- and 55-62-kDa polypeptides, respectively. The bovine f-GARP and t-GARP cDNAs code for proteins containing 590 amino acids and 299 amino acids, respectively. The first 571 amino acids of f-GARP and the first 291 amino acids of t-GARP are identica...Continue Reading

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