Fig. 2.
Fig. 2. CD109 cDNA and predicted protein sequences. / The K1 and K1-H7 CD109 cDNAs and the corresponding 1445 aa protein sequence are shown (GenBank accession number AF410459). Nucleotides are numbered relative to the translation initiation codon, with the corresponding aa numbering shown in parentheses. K1 and K1-H7 3′UTRs, and the positions of the corresponding poly(A) tails [(a)n)] are shown. Peptides identified by immuno-affinity purification–microsequencing of CD109 are singly underlined. Potential sites of N-linked glycosylation, the thioester signature sequence (aa residues 918-924), and the corresponding downstream thioester reactivity-defining hexapeptide motif (aa residues 1030-1035) are marked by open boxes. Additionally, the amino-terminal leader peptide (double underline), the bait region (dotted underline), the translation stop (*), and the GPI anchor cleavage–addition site (open triangle) are shown.

CD109 cDNA and predicted protein sequences.

The K1 and K1-H7 CD109 cDNAs and the corresponding 1445 aa protein sequence are shown (GenBank accession number AF410459). Nucleotides are numbered relative to the translation initiation codon, with the corresponding aa numbering shown in parentheses. K1 and K1-H7 3′UTRs, and the positions of the corresponding poly(A) tails [(a)n)] are shown. Peptides identified by immuno-affinity purification–microsequencing of CD109 are singly underlined. Potential sites of N-linked glycosylation, the thioester signature sequence (aa residues 918-924), and the corresponding downstream thioester reactivity-defining hexapeptide motif (aa residues 1030-1035) are marked by open boxes. Additionally, the amino-terminal leader peptide (double underline), the bait region (dotted underline), the translation stop (*), and the GPI anchor cleavage–addition site (open triangle) are shown.

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