S. Busch, CLONING AND SEQUENCING OF THE CDNA-ENCODING FOR A NA+ H+ EXCHANGER FROM XENOPUS-LAEVIS OOCYTES (X1-NHE)/, Biochimica et biophysica acta. Biomembranes, 1325(1), 1997, pp. 13-16
We have cloned and sequenced the cDNA for a Na+/H+ exchanger(NHE) from
Xenopus laevis oocytes. This cDNA contains an open reading frame enco
ding a protein of 782 amino acids with 12 putative transmembrane domai
ns 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 Asn(56) and Asn(351) were identified. T
hree potential protein kinase C phosphorylation sites at the cytoplasm
ic tail were identified at Ser(494), Thr(726) and Ser(747). RT-PCR rev
ealed the expression of the X1-NHE in Xenopus heart, reticulocytes and
skeletal muscle. (C) 1997 Elsevier Science B.V.