Red lines indicate ZP proteins with EGF-like domains in four lophotrochozoans ( C. Branch lengths are proportional to the expected number of substitutions per site, as indicated by the scale bar. The maximum likelihood tree was inferred from 128 ZP proteins sequences under the WAG + Z model (221 positions, 1000 bootstrap replicates). ( B) Molecular phylogeny of lophotrochozoan ZP proteins. Adi, Acropora digitifera Bfl, Branchiostoma floridae Cgi, Crassostrea gigas Cin, Ciona intestinalis Cte, Capitella teleta Dme, Drosophila melanogaster Dre, Danio rerio Gga, Gallus gallus Hsa, Homo sapiens Lan, Lingula anatina Lgi, Lottia gigantea Mye, Mizuhopecten yessoensis Nge, Notospermus geniculatus Obi, Octopus bimaculoides Pau, Phoronis australis Pfu, Pinctada fucata Spu, Strongylocentrotus purpuratus. Numbers indicate the number of both EGF-like and ZP domains-containing genes (EGF + ZP). ( A) Numbers of EGF-like and/or ZP domains-containing genes in 17 animal genomes. Pmarg, Pinctada margaritifera Pmax, Pinctada maxima Pma, Pecten maximus Rph, Ruditapes philippinarum Sc, Scaphopoda Vli, Villosa lienosa VEZP, Viteline envelope ZP protein.Įvolution of EGF-like and ZP domains-containing proteins in animals. Ama, Archivesica marissinica Ape, Atrina pectinata Bi, Bivalvia BZP, Bivalve ZP protein Ce, Cephalopoda CGI, Crassostrea gigas Cvi, Crassostrea virginica Eco, Elliptio complanata Ga, Gastropoda LZP, lophotrochozoan ZP protein Med, Mytilus edulis Mga, Mytilus galloprovincialis Mye, Mizuhopecten yessoensis MZP, molluscan ZP protein Obi, Octopus bimaculoides Ovu, Octopus vulgaris Pfu, Pinctada fucata. Asterisks indicate 100% bootstrap support. ( B) Details of the clade contain EGFZP and EGFL proteins in bivalves in ( A). Numbers on nodes indicate the bootstrap values. ( A) The maximum likelihood tree was inferred from 137 ZP proteins sequences under the WAG + Г model (196 positions, 1000 bootstrap replicates). Molecular phylogeny of molluscan ZP proteins. DIO1-like, type I iodothyronine deiodinase-like. Gray box in the exon structure of PfuEGFL1 indicate the missing coding region in genome data (poly-N part). Asterisks indicate conserved cysytein residues. Black, blue, red, and pink boxes indicate signal peptide, EGF-like domain, ZP domain, and transmembrane, respectively. ( D) The boundary of exons of EGFL and EGFZP. Arrows indicate the direction of the transcript ( B), and black boxes represent exons ( C). ( B, C) Genomic organization of EGFL and EGFZP in P. The Asterisks indicate the conserved Cys residues. Yellow arrowheads indicate the potential cleavage sites by furin enzyme (amino acid sequences are "RRRR" and "RKRR"). However, they undoubtedly have one ZP domain and an additional TMD in their C-termini. fucata (PfuEGFZP) and Lottia gigantea (LUSP-17) are similar to EGFL proteins of P. ( A) Three EGFL proteins of Pinctada fucata (PfuEGFL1, 2A, and 2B) consist of a signal peptide (black box), two EGF-like domains, and one ZP-like domain. Schematic representation of EGFL and EGFZP proteins. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. The data suggest that the ZP domain can interact with other SMPs, and EGFL evolution in pterimorph bivalves represents an example of neo-functionalization that involves the acquisition of a novel protein through gene duplication.īiomineralization Neo-functionalization Organic complex Tandem duplication Zona pellucida. fucata, the ZP domain interacts with eight SMPs that have various functions in the nacreous shell mineralization. Furthermore, our analysis showed that in P. fucata and the limpet Nipponacmea fuscoviridis, EGFZP genes were expressed in the inner part of the mantle epithelial cells are related to aragonitic shell formation. fucata, EGFL genes were expressed in the outer part of mantle epithelial cells are related to the calcitic shell formation. Phylogenetic analysis and genomic arrangement studies showed that EGFL and EGFZP formed a clade in bivalves, and their encoding genes were localized in tandem repeats on the same scaffold. In contrast, only EGFZP was identified in the gastropods. Two types of the proteins (EGF-like protein (EGFL) and EGF-like and ZP domains containing protein (EGFZP)) were found in the pearl oyster, Pinctada fucata. In this study, we investigated the evolutionary process EGF-like and zona pellucida (ZP) domains containing SMPs. However, the evolutionary origin of most SMPs remains unclear. Their diversity is the consequence of various molecular processes, including domain shuffling and gene duplication. Several types of shell matrix proteins (SMPs) have been identified in molluskan shells.
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