{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/sample_description.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/1011-20.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/eneo-braker3-manual_annot-Znev-250110_edit.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070647/txt.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jitka.stafkova@uochb.cas.cz"],"submitter":["Karel Harant"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Terpen  biosynthesis","Neoisoptera","Termites"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070647"],"tissue":["Whole Body"],"sample_protocol":["Each sample was homogenized in 500 µL of homogenization buffer consisting of 100 mM triethylammonium bicarbonate buffer (TEAB; Sigma-Aldrich) and 2% sodium deoxycholate (SDC; Sigma-Aldrich) in a 1.5-mL Eppendorf tube using FastPrep-24 homogenizer (MP Biomedicals). The homogenate was centrifuged to remove cell debris and the supernatant was used for analysis. Further sample processing and MS analysis were performed as previously described (Štáfková et al. 2018). Briefly, protein concentration was determined using a BCA protein assay kit (Thermo Fisher Scientific). Cysteines were reduced with Tris(2-carboxyethyl) phosphine hydrochloride (TCEP) and blocked with methyl methanethiosulfonate (MMTS). The samples were digested with porcine trypsin. Then, the samples were acidified with trifluoroacetic acid to a final concentration of 1%. SDC was removed by extraction to ethylacetate and subsequently to hexane. Peptides were desalted using a Michrom C18 column. Dried peptides were resuspended in 25 µL of water containing 2% acetonitrile and 0.1% trifluoroacetic acid. Peptides were separated by nanoliquid chromatography (nanoLC) on a Dionex Ultimate 3000 system and analyzed on an Orbitrap Fusion Tribrid mass spectrometer (both Thermo Fisher Scientific)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The data were evaluated with MaxQuant version 2.2.0.0 using LFQ algorithms (Cox and Mann 2008; Cox et al. 2014) and the Andromeda search engine (Cox et al. 2011). The key criteria used in the data analysis were a false discovery rate (FDR) of 0.01 for proteins and peptides, a minimum length of seven amino acids, a fixed modification (methylthio), and variable modifications of N-terminal protein acetylation and methionine oxidation. The data were locally evaluated against selected databases of nonredundant protein sequences that were downloaded from NCBI on February 13, 2023. The in-house database of E. neotenicus protein sequences was based on protein models generated by BRAKER (see E. neotenicus draft genome assembly and annotation) complemented by a set of manually annotated IDS genes. The local database is available along with the raw data and result files in MassIVE (see Data availability). The data were processed in Perseus version 2.0.7.0 (Tyanova et al. 2016). Results representing standard contaminants, reverse sequences (decoys), and sequences identified only with modified peptides were discarded. The dataset containing proteins with at least two valid LFQ values in at least one experimental group was further analyzed. The dataset was log2 transformed. Missing LFQ values were replaced from the normal distribution (width 0.3; downshift 1.8) and histograms before and after the data imputation were examined. Heatmap with hierarchical clustering was used to check the uniformity of the sample proteomes between the two subgroups. Significant differences were determined by a permutation-based two-sided t-test with an error-corrected p-value (FDR = 0.05; S0 = 0.1). The number of randomizations in the analysis was 1,000."],"omics_type":["Proteomics"],"labhead":["Robert Hanus"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic"],"species":["Embiratermes Neotenicus"],"publication":["10.1371/JOURNAL.PBIO.3003648"],"submitter_mail":["harant@natur.cuni.cz"],"submitter_affiliation":["Charles University"],"submitter_country":["Czech Republic"],"additional_accession":[]},"is_claimable":false,"name":"Evolutionary origin of terpenoid biosynthesis in termites","description":"Termites produce the most diverse array of terpenoids among metazoans, comprising over 200 structures involved in chemical communication and defense described to date, some of which are exclusive to termites. However, their biosynthesis has not yet been elucidated, and the responsible terpene synthases remain unknown. Here, we draw lessons from discoveries in other insects which showed that terpene synthases can originate through duplications and neofunctionalizations of isoprenyl diphosphate synthase genes, occurring independently in individual clades. We identify a novel gene family which arose through the duplication of geranylgeranyl pyrophosphate synthase (GGPPS) in the common ancestor of Neoisoptera, the modern terpene-producing termite lineage. This family subsequently expanded into multiple paralogs and has been retained in neoisopteran genomes throughout 100 million years of diversification. We functionally characterized several GGPPS-like enzymes from two neoisopteran species and demonstrated that they indeed act as terpene synthases generating biologically relevant sesqui- and diterpenes. In Embiratermes neotenicus, EneoC produces enantiomerically pure (3R,6E)-nerolidol, known as the queen pheromone, and EneoE produces (E,E,E)-neocembrene, another queen-specific compound. In Nasutitermes takasagoensis, NtGGPPS6 synthesizes (E,E,E)-neocembrene, the precursor of polycyclic diterpenes characteristic of this genus. We explore the evolutionary transition from isoprenyl diphosphate synthase to terpene synthase activity in these enzymes in terms of structural features and selection pressures, and highlight the potential role of transposable elements in the evolution of the GGPPS-like family. We conclude that we have identified an enzyme family underlying the remarkable richness of termite terpenoids, which likely contributed to the ecological success of 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