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Journal Article

Amino acid sequence of band-3 protein from rainbow trout erythrocytes derived from cDNA

MPS-Authors
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Hübner,  Stefan
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Frank
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Rudloff,  Victor
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Appelhans,  Heribert
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Hübner, S., Michel, F., Rudloff, V., & Appelhans, H. (1992). Amino acid sequence of band-3 protein from rainbow trout erythrocytes derived from cDNA. Biochemical Journal, 285(1), 17-23. doi:10.1042/bj2850017.


Cite as: https://hdl.handle.net/21.11116/0000-0007-CD56-2
Abstract
In this report we present the first complete band-3 cDNA sequence of a poikilothermic lower vertebrate. The primary structure of the anion-exchange protein band 3 (AE1) from rainbow trout erythrocytes was determined by nucleotide sequencing of cDNA clones. The overlapping clones have a total length of 3827 bp with a 5'-terminal untranslated region of 150 bp, a 2754 bp open reading frame and a 3'-untranslated region of 924 bp. Band-3 protein from trout erythrocytes consists of 918 amino acid residues with a calculated molecular mass of 101 827 Da. Comparison of its amino acid sequence revealed a 60-65% identity within the transmembrane spanning sequence of band-3 proteins published so far. An additional insertion of 24 amino acid residues within the membrane-associated domain of trout band-3 protein was identified, which until now was thought to be a general feature only of mammalian band-3-related proteins.