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. 2018 Jan 23;8:1989. doi: 10.3389/fimmu.2017.01989

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Copyright © 2018 Eden, Menzel, Wesolowski, Bergmann, Nissen, Dubberke, Seyfried, Albrecht, Haag and Koch-Nolte.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Amino acid sequence alignments of CD38 and CXCR4 from human, mouse, and alpaca. Amino acid sequence alignments of the CD38 and CXCR4 species orthologs from human, mouse and alpaca (hs, homo sapiens; mm, mus musculus; vp, vicuna pacos). Symbols below the alignments indicate identical amino acid residues (*), conserved substitutions (. and:), and non-conserved substitutions (blank spaces). Cytosolic amino acid residues are indicated in blue, transmembrane residues in red, and extracellular residues in black. Potential asparagine-linked glycosylation sites and potential tyrosine-linked sulfation (SO) sites are highlighted in cyan. Cysteines engaged in intrachain disulfide bonding are highlighted in yellow. In order to access the sequence of the camelid ortholog, we perform a protein BLAST search (https://blast.ncbi.nlm.nih.gov) using the human protein sequence as input and selecting “Non-redundant protein sequences (nr)” as database and “Camelidae (taxid:9835)” as organism from the respective pull down menus.