Amino acid sequences around exofacial proteolytic cleavage sites of band 3 from bovine and porcine erythrocytes.
1. Amino acid sequences of bovine and porcine band 3, an erythrocyte anion transporter, were determined. 2. The sequence of bovine band 3 was positioned to residues 519-599 (the numbering is based on human band 3), in which probably 6 residues were unidentified. 3. Binding site of DIDS (4,4'-diisothiocyanostilbene-2,2'-disulfonate), a potent anion transport inhibitor, was identified as Lys-539 in the bovine case. 4. A loop (residues 551-567), which provides exofacial proteolytic cleavage sites, contains only 53% homology between human and bovine, whereas the residues flanking it on either side are > 84% homologous. 5. Furthermore, the loop of porcine band 3 was indicated to consist of a 6 or 7-residues short peptide as compared with those of other species.
Moriyama
R
R
Department of Applied Bioscience, Faculty of Agriculture, Nagoya University, Japan.
Nagatomi
Y
Y
Hoshino
F
F
Makino
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D002417:Cattle; D002918:Chymotrypsin; D004912:Erythrocytes / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013552:Swine; D014357:Trypsin
D001457:Anion Exchange Protein 1, Erythrocyte; D002918:Chymotrypsin; D014357:Trypsin