Fig. 4.
Fig. 4. The nucleotide, deduced amino acid sequence, and hydropathy plot of CD164. (A) The putative signal sequence is underlined. Potential sites of N-linked and O-linked glycan attachment are indicated by (*) asterisks and (#) hatch-markings, respectively. Cysteine residues are indicated by boxes. Nucleotide (and amino acid) sequences that differ from the published sequences of MGC-2455 are in bold. The putative transmembrane domain (amino acid 161 to 180) is italicized. Please note that the nucleotide and amino acid sequence numbering is based on that of Masuzawa et al.55 (B) The hydropathy plot of CD164 polypeptide backbone, according to the method of Kyte and Doolittle.61Various regions are bracketed and identified at the right of the figure. Circled Ns represent potential N-linked glycosylation sites.

The nucleotide, deduced amino acid sequence, and hydropathy plot of CD164. (A) The putative signal sequence is underlined. Potential sites of N-linked and O-linked glycan attachment are indicated by (*) asterisks and (#) hatch-markings, respectively. Cysteine residues are indicated by boxes. Nucleotide (and amino acid) sequences that differ from the published sequences of MGC-2455 are in bold. The putative transmembrane domain (amino acid 161 to 180) is italicized. Please note that the nucleotide and amino acid sequence numbering is based on that of Masuzawa et al.55 (B) The hydropathy plot of CD164 polypeptide backbone, according to the method of Kyte and Doolittle.61Various regions are bracketed and identified at the right of the figure. Circled Ns represent potential N-linked glycosylation sites.

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