Cloning and sequencing of the cDNA encoding for a Na+/H+ exchanger from Xenopus laevis oocytes (X1-NHE).
We have cloned and sequenced the cDNA for a Na+/H+ exchanger (NHE) from Xenopus laevis oocytes. This cDNA contains an open reading frame encoding a protein of 782 amino acids with 12 putative transmembrane domains and a long cytoplasmic tail. The protein exhibits a strong homology at the amino acid level to the human NHE-1 as well as to the beta NHE from trout red blood cells: 69% and 58% respectively. Two potential N-linked glycosylation sites at Asn56 and Asn351 were identified. Three potential protein kinase C phosphorylation sites at the cytoplasmic tail were identified at Ser494, Thr726 and Ser747. RT-PCR revealed the expression of the X1-NHE in Xenopus heart, reticulocytes and skeletal muscle.
Busch
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Institut für Pharmakologie, Universitätsklinikum Essen, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D008969:Molecular Sequence Data; D009865:Oocytes / Q000502:physiology*; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D017923:Sodium-Hydrogen Exchangers / Q000235:genetics*; D014982:Xenopus laevis
D018076:DNA, Complementary; D017923:Sodium-Hydrogen Exchangers