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The Phylogeny of Osteopontin-Analysis of the Protein Sequence.

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.

SUBMITTER: Weber GF

PROVIDER: S-EPMC6164354 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BACKGROUND: Most members of the serpin family of proteins are potent, irreversible inhibitors of specific serine or cysteine proteinases. Inhibitory serpins are distinguished from members of other families of proteinase inhibitors by their metastable structure and unique suicide-substrate mechanism. Animal serpins exert control over a remarkable diversity of physiological processes including blood coagulation, fibrinolysis, innate immunity and aspects of development. Relatively little is known about the complement of serpin genes in plant genomes and the biological functions of plant serpins. RESULTS: A structurally refined amino-acid sequence alignment of the 14 full-length serpins encoded in the genome of the japonica rice Oryza sativa cv. Nipponbare (a monocot) showed a diversity of reactive-centre sequences (which largely determine inhibitory specificity) and a low degree of identity with those of serpins in Arabidopsis (a eudicot). A new convenient and functionally informative nomenclature for plant serpins in which the reactive-centre sequence is incorporated into the serpin name was developed and applied to the rice serpins. A phylogenetic analysis of the rice serpins provided evidence for two main clades and a number of relatively recent gene duplications. Transcriptional analysis showed vastly different levels of basal expression among eight selected rice serpin genes in callus tissue, during seedling development, among vegetative tissues of mature plants and throughout seed development. The gene OsSRP-LRS (Os03g41419), encoding a putative orthologue of Arabidopsis AtSerpin1 (At1g47710), was expressed ubiquitously and at high levels. The second most highly expressed serpin gene was OsSRP-PLP (Os11g11500), encoding a non-inhibitory serpin with a surprisingly well-conserved reactive-centre loop (RCL) sequence among putative orthologues in other grass species. CONCLUSIONS: The diversity of reactive-centre sequences among the putatively inhibitory serpins of rice point to a range of target proteases with different proteolytic specificities. Large differences in basal expression levels of the eight selected rice serpin genes during development further suggest a range of functions in regulation and in plant defence for the corresponding proteins.

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The Phylogeny of Osteopontin-Analysis of the Protein Sequence.

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