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Cloning and sequence analysis of brain cDNA encoding a Xenopus D 2 dopamine receptor
Author(s) -
Martens Gerard J.M.,
Molhuizen Henri O.F.,
Gröneveld Diet,
Roubos Eric W.
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)80364-9
Subject(s) - xenopus , biology , receptor , transmembrane domain , gabbr1 , complementary dna , microbiology and biotechnology , peptide sequence , 5 ht5a receptor , biochemistry , gene , protease activated receptor 2
A D 2 dopamine receptor pharmacologically different from the mammalian D 2 receptor has previously been characterized in the amphibian Xenopus laevis . Here we report the cloning of a Xenopus D 2 receptor which revealed about 75% amino acid sequence identity with its mammalian counterpart and the presence of an additional 33 amino acid sequence in the 3rd cytoplasmic loop instead of the additional 29 residues in the large form of the mammalian D 2 receptor, All 7 predicted transmembrane domains are highly conserved between the Xenopus and mammalian D 2 receptors, as are the 1st and 2nd intracellular loop, the 1st and 3rd extracellular loop and the carboxy‐terminal portion of the receptors. The amino‐terminal portion, the 2nd extracellular loop and the middle portion of the 3rd intracellular loop of these receptors, however, differ considerably, Knowledge of the locations of these regions of conservation and divergence within the D 2 receptors or Xenopus and mammals will help to delineate portions of the receptor molecule that are functionally important. Interestingly, the 5‐untranslated region of the Xenopus D 2 receptor mRNA contains 4 small open reading frames which may affect translational efficiency.