{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/Pila_proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/Lny_proteinGroups.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR1_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR1_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR2_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR2_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR2_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR2_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/PilaR1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/LnR2_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/Qian120513PVF-Ovo-2.pkl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/Qian120513PVF-Ovo-3.pkl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD070092/Qian120513PVF-Ovo-1.pkl"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jin_sun@ouc.edu.cn"],"submitter":["yufei zhou"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Pvf protein","Pila pesmei","Lanistes nyassanus","Pomacea canaliculata"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070092"],"tissue":["Albumen Gland"],"sample_protocol":["PVF was extracted from approximately 30 eggs using a fine needle in Pila pesmei and Lanistes nyassanus, mixed with 8 M urea, and centrifuged at 12,000×g for 10 min at 4 °C to obtain the protein-containing supernatant. Protein samples were combined with a loading buffer at a 1:3 (v/v) ratio, separated by SDS-PAGE, stained with Coomassie Brilliant Blue, and destained with 1% acetic acid. Each gel was cut into eight slices based on intensity and molecular weight, further destained with 50mM NH4HCO3 in 50% methanol, washed with MilliQ water, dried, and rehydrated twice with 100% acetonitrile and 100mM NH4HCO3. In-gel digestion was performed using sequencing grade trypsin in 50mM NH4HCO3, and peptides were recovered, desalted using Sep-Pak C18 cartridges, and dried in a vacuum concentrator.The dried fraction from each biological sample was reconstituted with 0.1% formic acid and analyzed twice using an LTQ-Orbitrap Elite coupled with an Easy-nLC (Thermo Fisher, Bremen, Germany). Peptides were separated on a C18 capillary column (Michrom BioResources, CA) over a 90-min gradient. Mass spectrometry scans were performed in the range of 350 to 1600 m/z at a resolution of 60,000 in positive mode. The five most abundant multiple-charged ions with a minimum signal of 500.0 were selected for high-energy collision-induced dissociation (HCD) and fragmentation via collision-induced dissociation (CID), both using an isolation width of 2.0 m/z. HCD had an activation time of 10 ms and a normalised collision energy of 45%, while CID had the same activation time but a normalised collision energy of 35%.And then the MS/MS data was identified and quantified via MaxQuant v1.5.3.30 , searching two reference (host and symbiont) databases plus their reversed sequences, which served as the “decoy” database, respectively.A false discovery rate threshold of < 0.01 was also applied in each replicate for final protein identification. Only proteins that were identified in at least two biological replicates, contained at least 2 unique peptides were retained.  To further confirm the number of PV1 subunit, MSGFPlus searches were performed for the ovorubin MS data of Pomacea canaliculata, with following parameters: ±20 ppm parent mass tolerance; isotope error range (-ti ‘-1,2’); fully tryptic enzyme settings (-e 1 -ntt 2); conducting a parallel search against a decoy protein database (-tda 1) for calculating the false discovery rate (FDR). Only proteins that were identified in three biological replicates and contained at least 3 unique peptides were retained."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For the MaxQuant, a false discovery rate threshold of < 0.01 was also applied in each replicate for final protein identification and only proteins that were identified in at least two biological replicates, contained at least 2 unique peptides were retained. For the Ovorubin, only proteins that were identified in three biological replicates and contained at least 3 unique peptides were retained."],"omics_type":["Proteomics"],"labhead":["Jin Sun"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Ocean University of China"],"species":["Pomacea Canaliculata","Lanistes Nyassanus","Pila Pesmei"],"publication":["42227959 Zhou Y, Mu H, Nie X, Gao Y, Wang H, Fang L, Luan T, Ganmanee M, Qiu JW, Sun J, Ip JC. Two Routes to Land: Genomic Underpinnings of Parallel Aerial Egg Deposition in Aquatic Old-World Pila and New-World Pomacea (Ampullariidae). Adv Sci (Weinh). 2026 13(48):e22371 10.1002/advs.202522371"],"submitter_mail":["yufeizhou0906@163.com"],"submitter_affiliation":["ocean university of China"],"submitter_country":["China"],"pubmed_abstract":["The evolution of aerial oviposition in Old-World Pila and New-World Pomacea apple snails-diverged since the Gondwanan breakup-offers a powerful model for probing genomic adaptations underpinning key evolutionary innovations. We generate a chromosomal-level genome for Pila celebensis and a scaffold-level genome for Pila pesmei, revealing a genus-specific doubling in genome size driven by transposable element expansions. Analyses of macrosynteny and topologically associating domains (TAD) identified lineage-specific chromosomal rearrangements associated with positive selection in gene blocks enriched for environmental sensing, metabolism, and stress response. Breakpoints in aerial egg layers preferentially are localized within TADs, suggesting convergent rewiring of gene regulation. Gene family evolution revealed parallel expansions in cellulases, β-D-xylosidases, and immune genes, alongside convergent positive selection in aquaporins critical for aerial osmoregulation. Perivitelline fluid (PVF) proteomics uncovered the central role of PVF1, likely acquired via ancient horizontal gene transfer (HGT) from viruses in the Ampullariidae ancestor in the Jurassic. Subsequent duplications enabled lineage-specific adaptation; PVF1 in aerial eggs shows parallel increases in hydrophobicity and aromatic residues (notably phenylalanine), enhancing desiccation resistance. Collectively, these convergent genomic mechanisms-structural rearrangement, gene family dynamics, and HGT-driven innovation-underpin the independent evolution of aerial oviposition in Pila and Pomacea, providing a multi-layered blueprint for understanding key ecological transitions."],"pubmed_title":["Two Routes to Land: Genomic Underpinnings of Parallel Aerial Egg Deposition in Aquatic Old-World Pila and New-World Pomacea (Ampullariidae)."],"pubmed_authors":["Zhou Yufei Y, Mu Huawei H, Nie Xueying X, Gao Yue Y, Wang Hui H, Fang Ling L, Luan Tiangang T, Ganmanee Monthon M, Qiu Jian-Wen JW, Sun Jin J, Ip Jack Chi-Ho JC"],"additional_accession":[]},"is_claimable":false,"name":"PVF proteome of three Ampullariidae snails","description":"Egg PVF proteins have been the primary focus in the water-to-land transition of ampullariids over the last three decades, but there is a lack of PVF data in Old-World species. To better understand the function and evolutionary history of PVF proteins, we generated Old-World Pila and Lanistes PVF proteomes. It also supplements the data on Ovorubin of Pomacea canaliculata, further helping to confirm the subunit of PV1 in PVF 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