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J. Biol. Chem., Vol. 263, Issue 32, 17092-17099, Nov, 1988
SL Alper, RR Kopito, SM Libresco and HF Lodish
Anion exchange is a nearly ubiquitous cellular transport function which
contributes to the regulation of cell pH and of cell volume. However, the
only plasma membrane anion exchanger of known identity and sequence is
erythroid band 3. Both hybridization and immunologic data support the
presence of band 3-related mRNAs and proteins in nonerythroid tissues. We
have used low stringency hybridization with the murine band 3 cDNA to clone
a band 3-related cDNA from murine kidney and from 70Z/3 pre-B cells. The
cDNA encodes a band 3-related protein (B3RP) of 1237 amino acids, with a
predicted mass of 137 kDa. The carboxyl-terminal hydrophobic domain of B3RP
has an amino acid sequence 67% identical to that of band 3, with a very
similar predicted secondary structure. The amino-terminal hydrophilic
domain of B3RP has two sections. The section adjacent to the putative
membrane-associated segment is 33% identical in amino acid sequence to the
amino-terminal, cytoplasmic domain of band 3. The other, far amino-terminal
section of B3RP has no correspondent in the band 3 sequence. B3RP mRNA is
present in a variety of epithelial and other tissues and probably encodes
an anion exchange protein of wide distribution.
Cloning and characterization of a murine band 3-related cDNA from kidney and from a lymphoid cell line
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142.
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