Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/TMT_channel_detail.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/checksum.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/BG_miP100_WCP_20231115.msfftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F12.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F21.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F08.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F03.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F16.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F11.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F13.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F20.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F04.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F09.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F17.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F10.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F01.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F14.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F05.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F18.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F24.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F22.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F15.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F07.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F02.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F19.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F06.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/20231115_AS_LC4_GT_BG_miP100_WCP_400ng_F23.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/miP100_miRFP.fastaftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077152/BG_miP100_WCP_20231115-2.4.0.305.pdResultprimaryOK200ch.muench@em.uni-frankfurt.deSüleyman BozkurtData-dependent acquisitionMass SpectrometryBottom-up proteomicsEndothelial cellSenescenceMicroproteinSmorfProteasomeProtein ubiquitinationhttps://www.ebi.ac.uk/pride/archive/projects/PXD077152Primary CellCell CultureSample preparation for mass spectrometry The samples were lysed and denatured with 2% SDS, 50 mM Tris-HCl pH 8, 150 mM NaCl, 10 mM TCEP, 40 mM chloroacetamide and protease inhibitor cocktail tablet (EDTA-free, Roche) at 95 °C for 5 min, then sonicated for 1 min (1s ON/ 1s OFF pulse, 45% amplitude) and boiled again for 5 min at 95 °C. Pure proteins were obtained with methanol/chloroform precipitation. Protein pellets were then resuspended in 8M urea solution containing 10mM EPPS. 100 μg of protein per samples were digested overnight at 37oC with LysC (Wako Chemicals) at 1:50 (w/w) ratio and Trypsin (Promega, V5113) at 1:100 (w/w) ratio. Digested peptides are purified using Sep-Pak tC18 cartridges (Waters, WAT054955). Peptide concentrations were determined with a μBCA assay (ThermoFisher Scientific, 23235) and 10 μg of peptide per sample was labeled with TMTpro 18-plex reagents (ThermoFisher Scientific, A52045) in a 1:2.5 (w/w) ratio (2.5µg TMT reagent per 1µg peptide). TMT labeled samples were adjusted to equal amounts and pooled. Then the pool was fractionated using High pH micro-flow fractionation. High pH micro-flow fractionation Peptides were fractionated using high-pH reversed-phase liquid-chromatography on a micro-flow HPLC (Dionex U3000 RSLC, Thermo Scientific). 45µg of pooled and purified TMT labelled peptides resuspended in Solvent A (5mM ammonium-bicarbonate, 5%ACN) were separated on a C18 column (XSelect CSH, 1mm x 150mm, 3.5 µm particle size; Waters) using a multistep gradient from 3-60% Solvent B (5mM ammonium-bicarbonate, 90% ACN) over 65 minutes at a flow rate of 30 µl/min. Eluting peptides were collected every 43 seconds from minute 2 for 69 minutes into a total of 96 fractions, which were cross-concatenated into 24 fractions. Pooled fractions were dried in a vacuum concentrator and resuspended in 2% ACN, 0.1% TFA for LC-MS analysis. Mass spectrometry (LC-MS3) Tryptic peptides were analyzed on an Orbitrap Ascend Tribrid Mass Spectrometer (ThermoFisher Scientific) coupled to a Vanquish Neo UHPLC (ThermoFisher Scientific) using a 35 cm long, 75 µm ID fused-silica column packed in house with 1.9 µm C18 particles (Reprosil pur, Dr. Maisch), and kept at 50°C using an integrated column oven (Sonation). HPLC solvents consisted of 0.1% Formic acid in water (Buffer A) and 0.1% Formic acid, 80% acetonitrile in water (Buffer B). Assuming equal amounts in each fraction, 400 ng of peptides were eluted by a non-linear gradient from 7 to 40% B over 90 minutes followed by a step-wise increase to 95% B in 6 minutes which was held for another 9 minutes. A synchronous precursor selection (SPS) multi-notch MS3 method was used in order to minimize ratio compression as previously described (1). Full scan MS spectra (350–1400 m/z) were acquired with a resolution of 120,000 at m/z 200, maximum injection time of 50 ms and AGC target value of 4 × 10⁵. The most intense precursors with a charge state between 2 and 6 per full scan were selected for fragmentation ("Top Speed" with a cycle time of 1.2 seconds) and isolated with a quadrupole isolation window of 0.7 Th. MS2 scans were performed in the Ion Trap (Turbo) using a maximum injection time of 35 ms, AGC target value of 10,000 and fragmented using CID with a normalized collision energy (NCE) of 35%. SPS-MS3 scans for quantification were triggered only after successful Real-time search against the human canonical reference proteome from SwissProt supplemented with a custom sequence database containing the miP-FERMT3 (miP100) and miRFP670nano protein sequences, with the same search parameters as stated below for data processing in Proteome Discoverer. Criteria for passing the search were Xcorr: 1, dCn: 0.1 and precursor mass accuracy: 10 ppm. Maximum search time was 35 ms. MS3 acquisition was performed on the 10 most intense MS2 fragment ions with an isolation window of 0.7 Th (MS) and 2 m/z (MS2). Ions were fragmented using HCD with an NCE of 55% and analysed in the Orbitrap with a resolution of 45,000 at m/z 200, scan range of 100–200 m/z, AGC target value of 100,000 and a maximum injection time of 91 ms. Repeated sequencing of already acquired precursors was limited by setting a dynamic exclusion of 60 seconds and 7 ppm and advanced peak determination was deactivated. All spectra were acquired in centroid mode. 1. McAlister GC, Nusinow DP, Jedrychowski MP, Wühr M, Huttlin EL, Erickson BK, Rad R, Haas W, Gygi SP (2014). "MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes." Analytical Chemistry. doi:10.1021/ac502040v.PrideNot availableProteomics data analysis Raw data were analyzed with Proteome Discoverer (PD) 2.4 (ThermoFisher Scientific) using a TMTpro SPS-MS3 quantification workflow. Acquired MS2 spectra were searched using SequestHT against the human reference proteome from UniProt/SwissProt (one sequence per gene; HoSP_OSPG_20230214.fasta; 20,531 sequences), supplemented with a custom sequence database containing the miP-FERMT3 and miRFP670nano protein sequences, and a collection of common contaminants (MQ_contaminants.fasta). Trypsin (full) was specified as the digestion enzyme allowing a maximum of 1 missed cleavage site. Peptide length was constrained between 6 and 144 amino acids with a maximum of 10 peptides reported per spectrum. TMTpro (+304.207 Da) at peptide N-termini and lysine residues, and carbamidomethylation (+57.021 Da) at cysteine residues were set as static modifications. Methionine oxidation (+15.995 Da) was set as a dynamic modification. Precursor mass tolerance was set to 7 ppm and fragment mass tolerance to 0.5 Da, after recalibration of mass errors using the Spectra RC node with default settings. False discovery rates were controlled using Percolator with a concatenated target-decoy strategy (< 1% FDR at both PSM and protein level; q-value based). Reporter ion intensities were extracted from MS3 spectra using an integration tolerance of 20 ppm (Most Confident Centroid method). Only PSMs with an average reporter signal-to-noise ratio above 10 and an SPS ion purity above 50% were used for protein quantification. Protein abundances were calculated from unique peptides and normalized to total peptide amount. Only high-confidence proteins (combined q-value < 0.01) were exported for downstream analyses. Differential abundance analysis was performed using the NormalyzerDE package (2) version 1.9.1 with limma as the statistical framework. Proteins were considered significantly regulated at an FDR-adjusted p-value < 0.05 and an absolute log₂ fold change > 0.58 (corresponding to a 1.5-fold change). 2 - Willforss J, Chawade A, Levander F (2018). “NormalyzerDE: Online Tool for Improved Normalization of Omics Expression Data and High-Sensitivity Differential Expression Analysis.” Journal of Proteome Research. doi:10.1021/acs.jproteome.8b00523.ProteomicsChristian MünchPARTIALInstitute of Molecular Systems Medicine, Faculty of Medicine, Goethe University, Frankfurt am Main, Germany. The Center for Functional Proteomics, Faculty of Medicine, Goethe University, Frankfurt am Main, Germany. Frankfurt Cancer Institute, Frankfurt am Main, Germany. Cardio-Pulmonary Institute, Frankfurt am Main, Germany.Homo Sapiens (human)42343301 Raheja M, Güven B, Szymanski W, Günther S, Kuenne C, Rakultsev V, Segarra M, Bozkurt S, Münch C, Kaulich M, Graumann J, Fleming I, Siragusa M. A microprotein encoded by FERMT3 modulates endothelial cell protein catabolism and induces cell cycle arrest and senescence. Cell Commun Signal. 2026 24(1):372 10.1186/s12964-026-03019-3bozkurt@med.uni-frankfurt.deInstitute of Biochemistry II, Goethe University Frankfurt, Theodor-Stern-Kai 7, Haus 75 60590 Frankfurt am MainGermany<h4>Background</h4>Endothelial cells express numerous microproteins (miPs) encoded by small open reading frames (smORFs), yet the biological function of most remains unknown. This study set out to characterize a novel 69 amino acid miP encoded within the FERM domain containing kindlin-3 transcript (miP-FERMT3), which is upregulated under inflammatory conditions.<h4>Methods</h4>Confocal microscopy was used to determine miP-FERMT3 localization, and its interaction partners were determined by mass spectrometry and immunoblotting. RNA sequencing and quantitative mass spectrometry were performed to assess transcriptional and proteomic alterations. Cell proliferation and cell cycle progression were examined by live cell imaging, EdU incorporation and flow cytometry, while senescence was determined by β-galactosidase staining, live cell imaging and RT-qPCR-based analysis of telomere length.<h4>Results</h4>In endothelial cells, miP-FERMT3 localized mainly to centriole subdistal appendages, where it colocalized with ninein and CEP170 and induced centrosome amplification. The expression of miP-FERMT3 caused cell cycle arrest and DNA damage, evidenced by γ-H2AX foci and nuclear p53 accumulation. Consistent with this, miP-FERMT3-expressing endothelial cells exhibited downregulation of genes required for cell-cycle progression and upregulation of genes involved in cell cycle inhibition and senescence. However, canonical p53 target genes were not induced and cell cycle arrest occurred independently of p53. Mechanistically, miP-FERMT3 interacted with proteins involved in ubiquitin/proteasome-dependent protein catabolism, including PSMD9, CUL2 and TRIM8, and its expression increased protein ubiquitination, centrosomal neddylation and proteasomal activity. Notably, enhanced proteasomal turnover of p21 in miP-FERMT3-expressing endothelial cells resulted in replication stress, as evidenced by increased CHK1 phosphorylation. These alterations culminated in rapid induction of cellular senescence, characterized by enlarged cell size, β-galactosidase activity, telomere shortening and a paracrine pro-inflammatory activation of naïve endothelial cells. Analyses of independent murine and human transcriptomic and proteomic aging datasets further revealed that FERMT3 expression and protein abundance increase with age.<h4>Conclusions</h4>miP-FERMT3 is a novel regulator of protein catabolism that promotes p21 degradation, replication stress and p53-independent cell cycle arrest and senescence in endothelial cells. Given the aging-associated upregulation of FERMT3 in mouse and human endothelial cells, increased miP-FERMT3 expression may contribute to the onset of vascular senescence as a hallmark of aging.A microprotein encoded by FERMT3 modulates endothelial cell protein catabolism and induces cell cycle arrest and senescence.Raheja Manav M, Güven Beyza B, Szymanski Witold W, Günther Stefan S, Kuenne Carsten C, Rakultsev Vladislav V, Segarra Marta M, Bozkurt Süleyman S, Münch Christian C, Kaulich Manuel M, Graumann Johannes J, Fleming Ingrid I, Siragusa Mauro MfalseA microprotein encoded by FERMT3 modulates endothelial cell protein catabolism and induces cell cycle arrest and senescenceBackground: Endothelial cells express numerous microproteins (miPs) encoded by small open reading frames (smORFs), yet the biological functions of most remain unknown. This study set out to characterize a novel 69 amino acid miP encoded within the FERM domain containing kindlin-3 transcript (miP-FERMT3), which is upregulated under inflammatory conditions. Methods: Confocal microscopy was used to determine miP-FERMT3 localization and its interaction partners were determined by mass spectrometry and immunoblotting. RNA sequencing and mass spectrometry were performed to assess transcriptional and proteomic alterations. Cell proliferation and cell cycle progression were examined by live cell imaging, EdU incorporation and flow cytometry, while senescence was determined by β-galactosidase staining, live cell imaging and RT-qPCR-based analysis of telomere length. Results: In endothelial cells miP-FERMT3 localized mainly to centriole subdistal appendages, where it colocalized with ninein and CEP170 and induced centrosome amplification. The expression of miP-FERMT3 caused cell cycle arrest and DNA damage, evidenced by γ-H2AX foci and nuclear p53 accumulation. Consistent with this, miP-FERMT3-expressing endothelial cells exhibited downregulation of genes required for cell-cycle progression and upregulation of genes involved in cell cycle inhibition and senescence. However, canonical p53 target genes were not induced and cell cycle arrest occurred independently of p53. Mechanistically, miP-FERMT3 interacted with proteins involved in ubiquitin/proteasome-dependent protein catabolism, including PSMD9, CUL2 and TRIM8, and its expression increased protein ubiquitination, centrosomal neddylation and proteasome activity. Notably, enhanced proteasomal turnover of p21 in miP-FERMT3-expressing endothelial cells resulted in replication stress, as evidenced by increased CHK1 phosphorylation. These alterations culminated in rapid induction of cellular senescence, characterized by enlarged cell size, β-galactosidase activity, telomere shortening and a paracrine pro-inflammatory activation of naïve endothelial cells. Analyses of independent murine and human transcriptomic and proteomic aging datasets further revealed that FERMT3 expression and protein abundance increase with age. Conclusions: miP-FERMT3 is a novel regulator of protein catabolism that promotes p21 degradation, replication stress and p53-independent cell cycle arrest and senescence in endothelial cells. Given the aging-associated upregulation of FERMT3 in mouse and human endothelial cells, increased miP-FERMT3 expression may contribute to the onset of vascular senescence as a hallmark of aging.2026-06-292026-04-14PXD077152NEWT:3555NEWT:71647NEWT:330879NEWT:35554NCBITaxon:12939NEWT:32046NEWT:544496NEWT:2042546NEWT:32049NEWT:1392696NEWT:259447NEWT:295546NEWT:45351NEWT:445974NEWT:43179NEWT:180454NEWT:5722NCBITaxon:1280NEWT:1129NEWT:309807NEWT:10245NEWT:55153NEWT:309800NEWT:281395NEWT:1211601NEWT:876138NEWT:44271NEWT:193516NEWT:351581NEWT:43186NEWT:428146NEWT:498257NEWT:10036NEWT:1590NEWT:498019NEWT:1351NEWT:1438992NEWT:1352NEWT:2649997NEWT:1147161NEWT:661410NEWT:638632NEWT:263737NEWT:224326NEWT:1333499NCBITaxon:79857NEWT:1096976NEWT:5702NEWT:95648NEWT:1589NEWT:135622NEWT:1349NEWT:35786NEWT:1580NEWT:399784NEWT:96731NEWT:383379NEWT:1401257NEWT:418106NEWT:10029NEWT:913645NEWT:44491NEWT:641809NEWT:27933NEWT:556484NEWT:317447NEWT:4688NEWT:7955NEWT:7719NEWT:7959NEWT:2261NEWT:868565NEWT:31156NEWT:3112NEWT:79329NEWT:4442NEWT:192875NEWT:1214915NEWT:12637NEWT:59729NEWT:2164133NEWT:295105NEWT:108061NEWT:60711NEWT:1316931NEWT:224308NEWT:3347NEWT:511145NEWT:160621NEWT:212790NEWT:931281NEWT:4432NEWT:5762NEWT:5763NEWT:658457NEWT:1310161NEWT:77133NEWT:295358NEWT:145481NCBITaxon:79824NEWT:2246NEWT:2652724NEWT:1912919NEWT:5757NCBITaxon:4563NEWT:5755NEWT:44689NEWT:44447NEWT:752555NEWT:498211NEWT:5759NEWT:347256NEWT:1736231NEWT:5518NEWT:398007NEWT:1527468NEWT:1392NEWT:498217NEWT:498216NEWT:2242NEWT:11320NEWT:286NEWT:391619NEWT:246196NEWT:287NEWT:246197NEWT:1367269NEWT:145458NEWT:633149NEWT:1149786NEWT:10239NEWT:68895NEWT:44685NEWT:161934NEWT:4897NEWT:1148NEWT:5744NEWT:5508NEWT:3329NEWT:5507NEWT:410661NEWT:55571NEWT:35500NEWT:1235816NEWT:1140NCBITaxon:2157NEWT:1143NEWT:4896NEWT:1287689NEWT:1390NEWT:11557NEWT:1094343NEWT:1462472NEWT:1336795NEWT:644042NEWT:294NEWT:1773NEWT:1182590NEWT:3712NEWT:82380NEWT:3711NEWT:935293NEWT:375146NEWT:2065263NEWT:1772NEWT:118698NEWT:1616117NEWT:263NEWT:118696NEWT:52283NEWT:11988NEWT:284812NEWT:8175NEWT:400667NEWT:43330NEWT:1603293NEWT:408169NEWT:44664NEWT:47946NEWT:459758NEWT:3702NEWT:1245466NEWT:243277NEWT:1246791NEWT:7067NEWT:118694NEWT:586722NEWT:2850NEWT:118691NEWT:33548NEWT:274NEWT:7070NCBITaxon:287NEWT:408172NEWT:408170NEWT:96794NEWT:3708NEWT:332648NEWT:44670NEWT:536231NEWT:376219NEWT:219813NEWT:1510NEWT:1436733NEWT:460519NEWT:1247411NEWT:1515NEWT:572307NEWT:1432138NEWT:1424507NEWT:1194599NEWT:272844NEWT:9483NEWT:333760NEWT:56636NEWT:1513458NEWT:1233681NCBITaxon:40559NEWT:506599NEWT:2853422NEWT:81077NEWT:84588NEWT:1679718NEWT:480NEWT:65349NEWT:67767NEWT:46835NEWT:109757NEWT:582580NEWT:300852NEWT:1502NEWT:128017NEWT:376686NEWT:95486NEWT:508771NEWT:1883446NEWT:253NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:93062NEWT:34613NCBITaxon:4932NEWT:109760NEWT:943274NEWT:644223NEWT:235443NEWT:108458NEWT:5936NEWT:272623NEWT:272624NEWT:320637NEWT:886559NEWT:55521NEWT:983964NEWT:118499NEWT:11706NEWT:32644NEWT:527796NEWT:1130798NEWT:55529NEWT:499175NEWT:109779NEWT:3745NEWT:1715989NCBITaxon:4751NEWT:476272NEWT:3747NEWT:195051NEWT:3988NEWT:1116234NEWT:1255228NEWT:649908NEWT:410289NEWT:373153NEWT:3983NEWT:203696NEWT:352472NEWT:1071661NEWT:1202532NEWT:360094NEWT:470NEWT:41364NEWT:5911NEWT:1313NEWT:1218097NCBITaxon:50557NEWT:39251NEWT:39491NEWT:212142NCBITaxon:5811NEWT:29491NEWT:101841NEWT:2014887NEWT:33952NEWT:153009NEWT:261756NEWT:571256NEWT:40483NEWT:63366NEWT:63367NEWT:688333NEWT:215402NCBITaxon:548681NEWT:318586NCBITaxon:5820NEWT:1547NEWT:272634NEWT:198107NEWT:9031NEWT:1872122NEWT:1308NEWT:7091NEWT:1034015NEWT:760568NEWT:141262NEWT:108931NEWT:1055524NEWT:4087NEWT:9778NEWT:306NEWT:150475NEWT:303NEWT:267872NEWT:97477NEWT:7111NEWT:347515NEWT:172269NEWT:9534NEWT:6269NEWT:5180NEWT:256737NEWT:4090NEWT:4092NEWT:9541NEWT:8694NEWT:4093NEWT:4096NEWT:8692NEWT:2903NEWT:185579NEWT:941442NEWT:536088NEWT:13076NEWT:1226408NEWT:7108NEWT:40479NEWT:43989NEWT:4076NEWT:142615NEWT:317NEWT:1006581NEWT:885318NEWT:39488NEWT:550NEWT:4081NEWT:273068NEWT:554NEWT:98334NEWT:451516NEWT:552NEWT:4084NEWT:63577NEWT:36185NEWT:1225786NEWT:7574NEWT:1715256NEWT:30640NEWT:575412NEWT:929793NEWT:29204NEWT:28112NEWT:114155NEWT:6494NEWT:6491NEWT:507601NEWT:520NEWT:186441NEWT:634955NEWT:643680NEWT:214092NCBITaxon:6157NEWT:6239NEWT:13095NEWT:162425NEWT:216257NEWT:102169NEWT:208893NEWT:9986NEWT:4054NEWT:8654NEWT:8658NEWT:1268063NEWT:8657NEWT:8655NEWT:5147NEWT:98351NEWT:1263854NEWT:118503NEWT:2059687NEWT:160488NEWT:28104NEWT:207559NEWT:407821NCBITaxon:2NEWT:85057NEWT:985076NEWT:568708NEWT:1215323NEWT:986NEWT:52641NEWT:7159NEWT:267671NEWT:28532NEWT:353152NEWT:8496NEWT:7165NEWT:1257118NEWT:27448NEWT:40674NEWT:1194669NEWT:51329NEWT:243230NEWT:443906NEWT:1080772NEWT:519NEWT:8479NEWT:8485NEWT:6063NEWT:49240NEWT:1328388NEWT:104395NEWT:9557NEWT:9315NEWT:6289NEWT:377586NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:9554NEWT:118562NEWT:725NEWT:7137NEWT:469008NEWT:256318NEWT:9321NEWT:206411NCBITaxon:6191NEWT:596153NEWT:229533NEWT:1836NEWT:214053NCBITaxon:10298NEWT:80863NEWT:90675NEWT:105231NEWT:104385NEWT:74649NEWT:52638NEWT:57075NEWT:206672NEWT:4097NEWT:8697NEWT:8695NEWT:884204NEWT:71139NEWT:9785NEWT:6279NEWT:1123869NEWT:9544NEWT:9545NEWT:7370NEWT:9793NEWT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