Fig. 1.
Fig. 1. The predicted amino acid sequence of human Sn shows a high degree of similarity to mouse Sn. / The hydrophobic leader peptide (amino acids 1-19) and transmembrane region (1642-1662) are underlined. Potential N-linked glycosylation sites are boxed in black. The conserved cysteine residues in domains 1 and 2 characteristic of Siglecs are boxed in gray. Residues in domain 1 that interact with sialic acid are boxed in white. The Ig domain boundaries, deduced from the exon-intron boundaries of the mouse Sn gene,63 are indicated. Residues that are identical with the mouse ortholog are indicated by stars; residues that are similar are indicated by dashes; and residues that are not represented in mouse Sn are indicated by open circles. The cDNA sequence of human Sn has been assigned the GenBank accession number AF230073.

The predicted amino acid sequence of human Sn shows a high degree of similarity to mouse Sn.

The hydrophobic leader peptide (amino acids 1-19) and transmembrane region (1642-1662) are underlined. Potential N-linked glycosylation sites are boxed in black. The conserved cysteine residues in domains 1 and 2 characteristic of Siglecs are boxed in gray. Residues in domain 1 that interact with sialic acid are boxed in white. The Ig domain boundaries, deduced from the exon-intron boundaries of the mouse Sn gene,63 are indicated. Residues that are identical with the mouse ortholog are indicated by stars; residues that are similar are indicated by dashes; and residues that are not represented in mouse Sn are indicated by open circles. The cDNA sequence of human Sn has been assigned the GenBank accession number AF230073.

Close Modal

or Create an Account

Close Modal
Close Modal