caa a22 4500 47712044X CHVBK 20180405111635.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF00229478 doi (NATIONALLICENCE)springer-10.1007/BF00229478 Structure and analysis of the mouse Na+/H+ exchanger (NHE1) gene: Homology and conservation of splice sites [Elektronische Daten] [H. Wang, D. Singh, W. Yang, J. Dyck, L. Fliegel] The Na+/H+ exchanger is a widely distributed integral membrane protein that is responsible for pH regulation in mammalian tissues. We have cloned and analyzed the NHE1 isoform of the mouse genomic Na+/H+exchanger. A clone from a mouse genomic library contained the NHE1 promoter region and the 5′-untranslated region. It also contained the first 121 amino acids of the coding region of the Na+/H+ exchanger. A splice site occurred after amino acid 121, at the same region as in the human NHE1 gene. The deduced amino terminal coding sequence was 76 and 88% identical to the human and rat NHE1 sequences respectively. The 5′-untranslated region was highly homologous to that of other species and two minicistrons contained in the human Na+/H+ exchanger were present in the mouse sequence. The results show that the deduced protein sequence of the mouse NHE1 gene has a high level of homology with other species and that the splice site of the first intron is conserved. These results suggest that the first large intron may play an important role in the NHE1 gene expression. Kluwer Academic Publishers, 1996 sodium-hydrogen exchange nationallicence mouse nationallicence gene sequence nationallicence Wang H. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut Singh D. Department of Anatomy, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut Yang W. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut Dyck J. Department of Biochemistry, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut Fliegel L. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/2(1996-12-01), 155-159 0300-8177 165:2<155 1996 165 11010 https://doi.org/10.1007/BF00229478 text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00229478 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Wang H. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Singh D. Department of Anatomy, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Yang W. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Dyck J. Department of Biochemistry, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut NATIONALLICENCE 700 1- Fliegel L. Department of Pediatrics, Faculty of Medicine, University of Alberta, 417 Heritage Medical Research Center, Edmonton, Alberta, Canada aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/2(1996-12-01), 155-159 0300-8177 165:2<155 1996 165 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer