FIG. 1.

Nucleotide sequence of the cDNA for porcine NRAMP1 and a comparison of its predicted amino acid sequence with those of other NRAMP1 proteins. (A) cDNA and predicted 538-amino-acid sequences of porcine NRAMP1. The polyadenylation signal is underlined. The glycine-to-aspartic-acid substitution at position 169, associated with susceptibility of mice, is circled. (B) Comparison of deduced porcine NRAMP1 with its congeners from humans, mice, and cattle. Identical residues throughout the four species are shown in bold type, and the 12 conservative putative transmembrane domains are underlined. The conserved consensus transport motif, proline- and serine-rich putative SH3-binding domain, PKC phosphorylation sites (S/T-X-R/K), and N-linked glycosylation sites (N-X-S/T) are boxed.