ArticleJournal of biomedical science2024
Characterization of the genetic variation and evolutionary divergence of the CLEC18 family.
Article in Journal of biomedical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Partitioned polygenic scores show mechanistic heterogeneity in type 2 diabetes and hypertension comorbidity.Nature communications · 2026Article
- CLEC18A interacts with sulfated glycosaminoglycans and controls clear cell renal cell carcinoma progression.The FEBS journal · 2026Article
- Genetic mutations in lymphocytic variant of hypereosinophilic syndrome: study of five siblings.Frontiers in medicine · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
backgroundThe C-type lectin family 18 (CLEC18) with lipid and glycan binding capabilities is important to metabolic regulation and innate immune responses against viral infection. However, human CLEC18 comprises three paralogous genes with highly similar sequences, making it challenging to distinguish genetic variations, expression patterns, and biological functions of individual CLEC18 paralogs. Additionally, the evolutionary relationship between human CLEC18 and its counterparts in other species remains unclear.
methodsTo identify the sequence variation and evolutionary divergence of human CLEC18 paralogs, we conducted a comprehensive analysis using various resources, including human and non-human primate reference genome assemblies, human pangenome assemblies, and long-read-based whole-genome and -transcriptome sequencing datasets.
resultsWe uncovered paralogous sequence variants (PSVs) and polymorphic variants (PVs) of human CLEC18 proteins, and identified distinct signatures specific to each CLEC18 paralog. Furthermore, we unveiled a novel segmental duplication for human CLEC18A gene. By comparing CLEC18 across human and non-human primates, our research showed that the CLEC18 paralogy probably occurred in the common ancestor of human and closely related non-human primates, and the lipid-binding CAP/SCP/TAPS domain of CLEC18 is more diverse than its glycan-binding CTLD. Moreover, we found that certain amino acids alterations at variant positions are exclusive to human CLEC18 paralogs.
conclusionsOur findings offer a comprehensive profiling of the intricate variations and evolutionary characteristics of human CLEC18.
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