ArticleInternational journal of molecular sciences2018
The Phylogeny of Osteopontin-Analysis of the Protein Sequence.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- Research progress on the correlation between OPN and immune escape of gastric cancer.Clinical and experimental medicine · 2026Review
- Beyond mutations: Accounting for quantitative changes in the analysis of protein evolution.Computational and structural biotechnology journal · 2024Article
- Immunoregulatory Roles of Osteopontin in Diseases.Nutrients · 2024Review
- Methods to Investigate Thrombin Cleavage of Osteopontin (OPN).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Review
- Osteopontin (OPN)/SPP1: from its biochemistry to biological functions in the innate immune system and the central nervous system (CNS).International immunology · 2023Review
- Osteopontin in autoimmune disorders: current knowledge and future perspective.Inflammopharmacology · 2022Review
- The Role of Dendritic Cells during Physiological and Pathological Dentinogenesis.Journal of clinical medicine · 2021Review
- Structural Constraint of Osteopontin Facilitates Efficient Binding to CD44.Biomolecules · 2021Article
- Quantitative Analysis of Protein Evolution: The Phylogeny of Osteopontin.Frontiers in genetics · 2021Article
- Evolution of the Avian Eggshell Biomineralization Protein Toolkit - New Insights From Multi-Omics.Frontiers in genetics · 2021Review
- Osteopontin in pancreatic cancer: A systematic review.Medicine internationalArticle
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1 author.
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Abstract
Osteopontin (OPN) is important for tissue remodeling, cellular immune responses, and calcium homeostasis in milk and urine. In pathophysiology, the biomolecule contributes to the progression of multiple cancers. Phylogenetic analysis of 202 osteopontin protein sequences identifies a core block of integrin-binding sites in the center of the protein, which is well conserved. Remarkably, the length of this block varies among species, resulting in differing distances between motifs within. The amino acid sequence SSEE is a candidate phosphorylation site. Two copies of it reside in the far N-terminus and are variably affected by alternative splicing in humans. Between those motifs, birds and reptiles have a histidine-rich domain, which is absent from other species. Just downstream from the thrombin cleavage site, the common motif (Q/I)(Y/S/V)(P/H/Y)D(A/V)(T/S)EED(L/E)(-/S)T has been hitherto unrecognized. While well preserved, it is yet without assigned function. The far C-terminus, although very different between Reptilia/Aves on the one hand and Mammals on the other, is highly conserved within each group of species, suggesting important functional roles that remain to be mapped. Taxonomic variations in the osteopontin sequence include a lack of about 20 amino acids in the downstream portion, a small unique sequence stretch C-terminally, a lack of six amino acids just upstream of the RGD motifs, and variable length insertions far C-terminally.
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