C. Korsgren et Cm. Cohen, CDNA SEQUENCE, GENE SEQUENCE, AND PROPERTIES OF MURINE PALLIDIN (BAND-4.2), THE PROTEIN IMPLICATED IN THE MURINE PALLID MUTATION, Genomics, 21(3), 1994, pp. 478-485
Band 4.2, which plays an important but poorly understood role in eryth
rocyte function and survival, is a major component of erythrocyte memb
ranes. Recently, it has been shown that the gene for murine protein ba
nd 4.2 colocalizes on chromosome 2 with the murine pallid mutation, wh
ich affects the formation or function of intracellular storage granule
s in melanocytes and platelets and lysosomes in kidney. As a first ste
p in identifying the mutation responsible for the pallid phenotype, we
have sequenced the entire normal murine band 4.2 gene. Our results sh
ow that the gene for murine band 4.2 is approximately 22 kb in size, w
ith 13 exons and 12 intervening introns. The organization of the mouse
band 4.2 gene is identical to that of the human band 4.2 gene and sim
ilar to that of the genes for the transglutaminase enzymes, reiteratin
g the membership of protein band 4.2 in the transglutaminase gene supe
rfamily. We also present 3.5 kb of normal murine erythroid band 4.2 cD
NA sequence containing an open reading frame of 2073 bp and coding for
691 amino acids. This is the same size as the human erythrocyte prote
in, with which the murine protein shares a 72% amino acid identity. (C
) 1994 Academic Press, Inc.