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Harant"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Embiratermes neotenicus"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077402"],"sample_protocol":["Tissue samples were cryogenically milled using a RETSCH CryoMill in 2 mL microcentrifuge tubes containing a 5 mm zirconium bead. Pulverization was performed in three cycles at 25 Hz for 3 minutes per cycle under liquid nitrogen cooling. The resulting tissue powder was solubilized in 2% sodium deoxycholate (SDC) prepared in 100 mM triethylammonium bicarbonate (TEAB) buffer. Protein concentration was determined using bicinchoninic acid assay. For digestion, 20 µg of total protein was used when sufficient material was available; otherwise, the entire sample was processed. Samples were diluted in 100 µL of 100 mM TEAB containing 2% SDC. Disulfide bonds were reduced with tris(2-carboxyethyl)phosphine (TCEP) in a final concentration of 10 mM, followed by alkylation with 40 mM chloroacetamide at 60 °C for 30 minutes. Proteins were digested with 1 µg of sequencing-grade trypsin at 37 °C overnight. Samples were acidified with trifluoroacetic acid to a final concentration of 1%. Sodium deoxycholate was removed by phase-transfer extraction with ethyl acetate, as described by {Masuda, 2008 #12861}. Peptides were subsequently desalted using in-house packed C18 StageTips (Empore disks) following the protocol described by {Rappsilber, 2007 #12862}.  LC separation was performed on Dionex Ultimate 3000 nano HPLC system online connected with the MS instrument. Samples were loaded onto the trap column (C18 PepMap100, 5 μm particle size, 300 μm x 5 mm, Thermo Scientific) for 2 min at 17.5 μl/min. Loading buffer was composed 2% acetonitrile and 0.1% trifluoroacetic acid in water. Peptides were eluted with Mobile phase B gradient from 4.0% to 35.0% B in 118.0 min. Mobile phase buffer A was 0.1% formic acid in water, Mobile phase B was 0.1% formic acid in acetonitrile. A nano reversed-phase column (Aurora Ultimate TS, 25 cm x 75 μm ID, 1.7 μm particle size, Ion Opticks) was used for LC/MS analysis.  For the two independent datasets analyzed, distinct MS acquisition strategies were employed. In the first dataset, protein abundances were compared across queen and nymph heads, abdominal soma, and ovaries using an Orbitrap Fusion Tribrid (Thermo Scientific) operated in a data-dependent acquisition mode, as described in detail by Horáček et al. {Horáček, 2026 #12858}. In the second dataset, a data-independent acquisition (DIA) approach was applied to enable a more in-depth, peptide-level quantification of EneoC protein abundances across queen tissues. The DIA workflow and instrument settings are described below."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For DIA analysis, peptide mixtures were analyzed on Thermo Scientific Orbitrap Ascend. Eluting peptide cations were converted to gas-phase ions by electrospray ionization in positive mode. Spray voltage was set to 2000 V and ion transfer tube temperature to 275 °C. MS1 scans of peptide precursors were analyzed in the Orbitrap in the range of 400-1000 m/z at 60K resolution and with following settings: RF Lens 60%, maximum injection time 123 ms, AGC target 100%. DIA scans were performed in Orbitrap at 30K resolution. AGC target was set to 1000% and maximum injection time mode to Auto. Precursor mass range 400-1000 m/z was covered by 40 windows, 15 Da wide. Activation type was set to HCD with 28% collision energy.  The DIA dataset was analyzed using Spectronaut version 19.5.241126 {Bruderer, 2015 #12863}. The analysis workflow employed was directDIA+(Deep) with normalization. The analysis was performed using an in-house database of E. neotenicus along with common contaminants. Search parameters were as follows: trypsin enzyme specificity, with Carbamidomethyl (C) as a fixed modification, and Acetyl (protein N-term) and Oxidation (M) as variable modifications. The thresholds for peptide spectrum match and protein false discovery rate (FDR) were set to 0.01. Further statistical and bioinformatic analyses were conducted using Perseus software, version 1.6.15.0 {Tyanova, 2016 #12864}. Quantitative profiles for EneoC were initially evaluated across all proteotypic peptides. As peptide-level quantification showed highly consistent trends, a single representative peptide (ILQPFTYVLK(2+)) was selected for visualization of relative protein abundance across sample types. Quantitative data for all detected peptides are provided in the Supplementary Material."],"omics_type":["Proteomics"],"labhead":["Robert Hanus"],"instrument_platform":[""],"labhead_affiliation":["Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic"],"submission_type":["PARTIAL"],"species":["Embiratermes Neotenicus"],"publication":["Not available"],"submitter_mail":["harant@uochb.cas.cz"],"submitter_affiliation":["Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague, Czech Republic"],"submitter_country":["Czechia"],"additional_accession":[]},"is_claimable":false,"name":"EneoC, a queen-specific terpene synthase, produces the queen pheromone in epidermal secretory cells of Embiratermes neotenicus queens","description":"Queen primer pheromones regulate reproduction and social organization in termites and are thought to function as honest signals of queen fertility. In Embiratermes neotenicus, the sesquiterpene (3R,6E)-nerolidol (RNERO) serves as a queen primer pheromone. We previously identified EneoC, a queen-specific terpene synthase, as a candidate enzyme for RNERO biosynthesis. Here, we provide in vivo functional evidence that EneoC is responsible for QPP production and characterize its spatial organization. Using integrated genome and transcriptome resources, RNA interference, proteomics, immunofluorescence, and electron microscopy, we show that EneoC is strongly upregulated in mature neotenic queens at both transcript and protein levels and represents a highly abundant protein, indicating a substantial physiological investment into pheromone production. Consistent with this, RNERO signaling likely constitutes an energetically costly and thus honest signal of reproductive status. Localization analyses reveal that RNERO biosynthesis occurs in the epidermis, where cells are extensively modified into secretory class I and class III cells. Within class I cells, immunogold labeling localizes EneoC to vesicular structures consistent with mitochondria. Notably, the upstream enzyme EneoB (farnesyl diphosphate synthase) is also abundantly localized in these mitochondria, suggesting co-localization of the final biosynthetic steps and an efficient metabolic organization. In contrast, EneoC is absent from eggs, although RNERO is present, indicating queen marking rather than embryonic synthesis. Together, our findings establish EneoC as the key enzyme underlying queen pheromone production and show that this process is confined to specialized epidermal secretory cells, with pathway organization and high protein investment consistent with the evolution of honest chemical signaling.","dates":{"publication":"2026-06-29","submission":"2026-04-20"},"accession":"PXD077402","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:35554","NEWT:32046","NEWT:544496","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:1129","NEWT:309807","NEWT:55153","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:96731","NEWT:383379","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:3112","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:108061","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:931281","NEWT:4432","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NCBITaxon:79824","NEWT:2246","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:633149","NEWT:10239","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:2065263","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:3702","NEWT:243277","NEWT:7067","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:33548","NEWT:274","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:9483","NEWT:333760","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NCBITaxon:4932","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:352472","NEWT:1071661","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:2014887","NEWT:33952","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:272634","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:141262","NEWT:108931","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT:303","NEWT:267872","NEWT:7111","NEWT:347515","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:4090","NEWT:4092","NEWT:9541","NEWT:8694","NEWT:4093","NEWT:4096","NEWT:8692","NEWT:185579","NEWT:941442","NEWT:13076","NEWT:1226408","NEWT:7108","NEWT:40479","NEWT:43989","NEWT:4076","NEWT:317","NEWT:1006581","NEWT:885318","NEWT:39488","NEWT:550","NEWT:4081","NEWT:273068","NEWT:554","NEWT:98334","NEWT:451516","NEWT:4084","NEWT:63577","NEWT:36185","NEWT:1225786","NEWT:7574","NEWT:1715256","NEWT:30640","NEWT:575412","NEWT:929793","NEWT:29204","NEWT:28112","NEWT:114155","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:6239","NEWT:162425","NEWT:216257","NEWT:102169","NEWT:9986","NEWT:4054","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8655","NEWT:1263854","NEWT:118503","NEWT:2059687","NEWT:160488","NEWT:28104","NEWT:207559","NEWT:407821","NCBITaxon:2","NEWT:985076","NEWT:1215323","NEWT:986","NEWT:52641","NEWT:7159","NEWT:28532","NEWT:353152","NEWT:8496","NEWT:27448","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:243230","NEWT:1080772","NEWT:519","NEWT:8479","NEWT:8485","NEWT:6063","NEWT:49240","NEWT:104395","NEWT:6289","NEWT:6287","NEWT:300641","NEWT:727","NEWT:9796","NEWT:725","NEWT:469008","NEWT:256318","NEWT:9321","NEWT:206411","NCBITaxon:6191","NEWT:596153","NEWT:229533","NEWT:1836","NEWT:214053","NEWT:80863","NEWT:105231","NEWT:52638","NEWT:57075","NEWT:4097","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:9785","NEWT:6279","NEWT:1123869","NEWT:9544","NEWT:7370","NEWT:83906","NCBITaxon:780","NCBITaxon:1502","NEWT:6282","NEWT:1134506","NEWT:387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