{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/gi_proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/ar_proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/22072905_WS_BURONG-AR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/22072905_WS_BURONG-GI.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/22072905_WS_kerong-GI.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD053708/22072905_WS_kerong-AR.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["wangshentong@qdio.ac.cn"],"submitter":["shentong wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Shell matrix proteins","Oysters"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD053708"],"tissue":["Exoskeleton"],"sample_protocol":["Proteomic analyses of SMPs were conducted on the shells of C. ariakensis and C. gigas, respectively. Each shell was soaked overnight in 5–10% sodium hypochlorite solution to eliminate organic impurities and the periostracum. A mortar and pestle were used to grind the air-dried shell pieces into a powder. The shell powder was decalcified with 0.5 M ethylenediaminetetraacetic acid (EDTA)-2Na (pH 8.0; Solarbio, Beijing, China) at 4°C, and the EDTA-soluble matrix was separated from the EDTA-insoluble matrix by centrifuging at 12,000 g for 30 min at 4°C. The EDTA-soluble matrix was concentrated and washed with water using Amicon Ultra-4 Centrifugal Filter Units (10 kDa NMWL; Millipore, Billerica, MA, USA) for protein analysis. The EDTA-insoluble matrix fractions were rinsed with distilled water and subsequently dissolved in a buffer solution containing 9 M urea and 2% (v/v) Triton X-100 for 5 minutes at 100°C. Following centrifugation at 12,000 g for 20 minutes at 4°C, the supernatant was collected as the EDTA-insoluble matrix. Each matrix was subjected to protein analysis using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) and liquid chromatography–tandem mass spectrometry (LC-MS/MS). SDS–PAGE was performed on a 15% polyacrylamide gel (Bio-Rad, Hercules, CA, USA) and detected via silver staining."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["We employed a shotgun approach to characterize the matrix proteins via LC-MS/MS.  Briefly, the bands were cut into pieces and subjected to cysteine reduction and alkylation using dithiothreitol and iodoacetamide, respectively. The following day, 300 μl of the extract solution was added; the mixture was then sonicated for 10 min, centrifuged, and the supernatant was collected. This process was repeated twice, the obtained extracts were pooled and vacuum dried. Samples were acidified with 0.2% trifluoroacetic acid, and the digested peptides were desalted. The peptide samples were diluted to 1 μg/μl in a buffer and analyzed by a Triple TOF 5600 plus mass spectrometer coupled with an Eksigent nanoLC system (AB Sciex, Framingham, MA, USA). The original MS/MS files were uploaded to ProteinPilot v4.5 (AB Sciex) for data analysis. The Paragon algorithm in ProteinPilot was employed to identify proteins through querying the C. ariakensis and C. gigas protein databases. The parameters were set as follows: cysteine was modified with iodoacetamide and biological modification was selected as the ID focus. For the identified proteins, peptides with an unused score >1.3 (credibility >95%) were considered credible and proteins containing at least one unique peptide were retained. Cysteine was modified with iodoacetamide, and biological modification was chosen as the identification focus. For the identified proteins, peptides with an unused score greater than 1.3 (credibility above 95%) were considered credible, and proteins containing at least one unique peptide were retained."],"omics_type":["Proteomics"],"labhead":["shentong wang"],"instrument_platform":[""],"labhead_affiliation":["Institute of Oceanology, Chinese Academy of Sciences"],"submission_type":["PARTIAL"],"species":["Crassostrea Ariakensis","Crassostrea Gigas (pacific Oyster) (crassostrea Angulata)"],"publication":["10.1016/J.ENVPOL.2025.126411"],"submitter_mail":["wangshentong@qdio.ac.cn"],"submitter_affiliation":["Institute of Oceanology, Chinese Academy of Sciences"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"shell matrix protein of estuarine oyster (Crassostrea ariakensis) and Pacific oyster (Crassostrea gigas)","description":"Studying the adaptive divergence of shellfish inhabiting different environments is crucial to predict the resilience of marine organisms to rapid climate change. Although the shell serves as the primary physical barrier against environmental change, the evolutionary adaptation of biomineralization in shellfish remains poorly understood. In this study, we using common garden designs to investigate the shell matrix proteome of estuarine (Crassostrea ariakensis) and Pacific (Crassostrea gigas) oysters inhabiting estuarine and open coastal zones, respectively. Shell matrix proteome analyses revealed extensive domain expansion of classical pathway secretomes, which likely contribute to the enhanced biomineralization capacity of estuarine oysters. Furthermore, two-thirds of the 27 C. ariakensis-specific shell matrix-secreted proteins (SMSPs) lacked homology with known proteins in the Swiss-Prot and nr databases, indicating rapid evolution. Our findings suggest that intensified classical pathway secretomes and rapid evolution of species-specific SMSPs are key factors shaping the defense of shells to enhance their adaptive potential to climate 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