<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Xin Zhan</submitter><species>Pteria Penguin</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0013762000</full_dataset_link><submitter_email>zhanxinuni@163.com</submitter_email><submitter_affiliation>School of Marine Biology and Fisheries, Hainan University, Haikou 570228, China</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>The proteomic analysis of byssus in Pteria penguin</name><description>Byssus, a unique external structure in bivalves, facilitates robust attachment in complex underwater environments.The byssus of P. penguin are different from other bivalves, as their byssus is merged together. We employed proteomic analysis to investigate the protein profiles of the foot and byssus in Pteria penguin, complemented by phosphoproteomic validation and molecular docking simulations. Through the foot proteomics, 155 differential expressed proteins (DEPs), 124 DEPs, 216 DEPs, 120 DEPs, 128 DEPs, and 98 DEPs were identified in SA vs SC, SC vs ST, SA vs ST, SC vs MA, ST vs MA, and SA vs MA, respectively. Byssus proteomics identified a total of 364,152 secondary maps, 1,805 peptide segments, and 308 proteins. We identified 33 different expressed proteins in SB(single byssus) vs MB (merged byssus). A total of 30 DUPs and 13 DDPs proteins were identified between SB and MB. In individuals secreting a single byssus and individuals secreting merged byssus, functional enrichment analysis demonstrated that the upregulated proteins were primarily associated with ion binding, energy metabolism. In contrast, the downregulated proteins were enriched in pathways related to Internal and external environment. Notably, individuals with single byssus exhibited heightened activity in ion transport pathways, elevated energy expenditure, and increased secretory activity for organic matter, suggesting a continuous and dynamic byssus secretion process. Conversely, those with merged byssus displayed a greater emphasis on maintaining internal and external environmental equilibrium, reflecting a shift toward physiological stability rather than active byssus secretion. The results of phosphoproteomics and molecular docking simulations also support this conclusion. These findings provide valuable insights for further investigation into the characteristics of different byssus morphologies and byssal proteins.</description><dates><publication>Mon Oct 13 00:00:00 BST 2025</publication></dates><accession>PXD069385</accession><cross_references><TAXONOMY>113549</TAXONOMY></cross_references></HashMap>