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Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase α‐ and β‐subunits, and identification of β′‐, a putative β‐subunit isozyme produced by alternative splicing of the β‐subunit gene
Author(s) -
Wolfgang Baehr,
Mary S. Champagne,
Andrea K. Lee,
Steven J. Pittler
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80095-k
Subject(s) - protein subunit , g alpha subunit , interleukin 10 receptor, alpha subunit , biology , phosphodiesterase , alternative splicing , microbiology and biotechnology , complementary dna , gamma subunit , beta (programming language) , isozyme , rna splicing , interleukin 12 receptor, beta 1 subunit , gene , biochemistry , exon , enzyme , rna , computer science , programming language
We have characterized overlapping cDNA clones encoding cGMP phosphodiesterase (PDE) α‐ and β‐subunits of mouse retinal rod photoreceptors. The open reading frames predict an α‐subunit of 100 kDa (856 residues), and a β‐subunit of 99 kDa (853 residues). Sequence analysis of two of twelve β‐subunit clones predicts the presence in the retina of an additional PDE, termed β, which is generated by alternative splicing of the β‐subunit gene, β differs from β only at the C‐terminus being 55 residues shorter and lacking the Caax motif found at the C‐termini of both the α‐ and β‐subunits. A 300 residue segment thought to contain the active site is present in the C‐terminal half of α, β and β.