Amino acid sequence of band-3 protein from rainbow trout erythrocytes derived from cDNA.
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.
Hübner
S
S
Max-Planck-Institut für Biophysik, Frankfurt/Main, Germany.
Michel
F
F
Rudloff
V
V
Appelhans
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000235:genetics* / Q000302:isolation & purification; D001483:Base Sequence; D015139:Blotting, Southern; D004247:DNA; D004912:Erythrocytes / Q000737:chemistry*; D051379:Mice; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D016133:Polymerase Chain Reaction; D012689:Sequence Homology, Nucleic Acid; D014337:Trout
D001457:Anion Exchange Protein 1, Erythrocyte; D004247:DNA