{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/sdrf.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_008_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_001_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_006_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_021_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_017_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_007_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_011_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_004_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_010_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_003_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_012_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_019_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_016_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_018_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_015_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_014_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_002_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_009_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_013_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_005_02_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_020_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_023_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_022_01_10pto.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_024_01_10pto.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_extendedDB_SemiTryp.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD060293/2019LZ011_TOMA_extendedDB.pdResult"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["joseluis.riechmann@cragenomica.es"],"submitter":["José Luis Riechmann"],"technology_type":["Data-dependent acquisition","Proteogenomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060293"],"tissue":["Flower Bud"],"sample_protocol":["Peptide extraction by ultrafiltration: For each sample, ~0.5 g of blended tissue distributed in two 2 mL microcentrifuge tubes were used. A total of 1.2 mL of extraction buffer (phosphate-buffered saline (PBS) 1x, urea 1.5M, DTT 10mM, acetonitrile 2% v/v, trifluoroacetic acid (TFA) 0.5%, MG-132 10µM, Proteinase Inhibitor cocktail cOmplete 1x, and PMSF 1mM) were added to the tissue, mixed by vortexing and incubated the samples with continuous shaking for 1 h at 4 °C. Samples were spined twice for 1 min at 4 °C (max speed) to precipitate cellular debris and solid particles in suspension. All the supernatant of each sample was filtered in 30K- or 100K- Amicon ® Ultra-0.5 Centrifugal Filter devices as indicated by the manufacturer (~500 µL of supernatant at a time were centrifuged at 14,000 x g for 10 min at 4 °C). Filtrates containing the smallest peptides depending on the weight limit of the filter device were kept for reverse phase chromatography.  Reverse phase chromatography: Samples obtained with both previous methods were mixed with sample buffer (2% TFA in 20% ACN) in 3:1 sample:sample buffer proportion. Final samples contained 0.5% TFA in 5% ACN. C18 resin columns (Pierce, Thermo Scientific) were prepared as indicated by the manufacturer before loading the samples on top of the resin beds (150 µL at a time). Samples were centrifuged at 1500 x g for 1 min as many times as needed to pass all the sample volume through the resin. Peptides were eluted from the column by adding 21 µL of elution buffer on top (0.1% formic acid in 70% ACN) and centrifuge at 1500 x g for 1 min (this step was repeated twice to increment the final concentration of the samples). The concentration (270 – 830 µg/mL) and amount of total protein (15 – 40 µg) in each sample were quantified using a Qubit Protein Assay Kit.  Sample preparation for LC-MS/MS: Samples (1 mg) were reduced with dithiothreitol (30 nmol, 37 ºC, 60 min) and alkylated in the dark with iodoacetamide (60 nmol, 25 ºC, 30 min). The resulting protein extract was first diluted to 2M urea with 200 mM ammonium bicarbonate for digestion with endoproteinase LysC (1:10 w:w, 37ºC, o/n, Wako), and then diluted 2-fold with 200 mM ammonium bicarbonate for trypsin digestion. After digestion, peptide mix was acidified with formic acid and desalted with a MicroSpin C18 column (The Nest Group, Inc) prior to LC-MS/MS analysis. Chromatographic and mass spectrometric analysis. Samples were analysed using a LTQ-Orbitrap Velos Pro mass spectrometer (Thermo Fisher Scientific, San Jose, CA, USA) coupled to an EASY-nLC 1000 (Thermo Fisher Scientific (Proxeon), Odense, Denmark). Peptides were loaded onto the 2-cm Nano Trap column with an inner diameter of 100 μm packed with C18 particles of 5 μm particle size (Thermo Fisher Scientific) and were separated by reversed-phase chromatography using a 25-cm column with an inner diameter of 75 μm, packed with 1.9 μm C18 particles (Nikkyo Technos Co., Ltd. Japan). Chromatographic gradients started at 93% buffer A and 7% buffer B with a flow rate of 250 nl/min for 5 minutes and gradually increased 65% buffer A and 35% buffer B in 60 min. After each analysis, the column was washed for 15 min with 10% buffer A and 90% buffer B. Buffer A: 0.1% formic acid in water. Buffer B: 0.1% formic acid in acetonitrile. The mass spectrometer was operated in positive ionization mode with nanospray voltage set at 2.1 kV and source temperature at 300°C. Ultramark 1621 for the was used for external calibration of the FT mass analyzer prior the analyses, and an internal calibration was performed using the background polysiloxane ion signal at m/z 445.1200.   The acquisition was performed in data-dependent acquisition (DDA) mode and full MS scans with 1 micro scans at resolution of 60,000 were used over a mass range of m/z 350-2000 with detection in the Orbitrap. Auto gain control (AGC) was set to 1E6, dynamic exclusion (60 seconds) and charge state filtering disqualifying singly charged peptides was activated. In each cycle of DDA analysis, following each survey scan, the top twenty most intense ions with multiple charged ions above a threshold ion count of 5000 were selected for fragmentation. Fragment ion spectra were produced via collision-induced dissociation (CID) at normalized collision energy of 35% and they were acquired in the ion trap mass analyzer. AGC was set to 1E4, isolation window of 2.0 m/z, an activation time of 10 ms and a maximum injection time of 100 ms were used. All data were acquired with Xcalibur software v2.2. Digested bovine serum albumin (New England Biolabs cat # P8108S) was analyzed between each sample to avoid sample carryover and to assure stability of the instrument and QCloud has been used to control instrument longitudinal performance during the project."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data analysis: Acquired spectra were analysed using the Proteome Discoverer software suite (v2.3, Thermo Fisher Scientific) and the Mascot search engine (v2.6, Matrix Science). The data were searched against two different databases (see below), plus a list of common contaminants and all the corresponding decoy entries. For peptide identification a precursor ion mass tolerance of 7 ppm was used for MS1 level, trypsin was chosen as enzyme, and up to three missed cleavages were allowed. The fragment ion mass tolerance was set to 0.5 Da for MS2 spectra. Oxidation of methionine and N-terminal protein acetylation were used as variable modifications whereas carbamidomethylation on cysteines was set as a fixed modification. False discovery rate (FDR) in peptide identification was set to a maximum of 5%. Peptide quantification data were retrieved from the “Precursor ion area detector” node from Proteome Discoverer (v2.0) using 2 ppm mass tolerance for the peptide extracted ion current (XIC). Protein abundance in each condition was estimated using the average of the three most intense peptides per protein group (TOP3).  Reference database: The LC-MS/MS data were searched with a tryptic analysis against a database (DB1) containing 40,798 non-redundant Araport11 protein coding genes (downloaded October 2019, Araport11_genes.201606.pep.fasta), 1,684 short Open Reading Frames (sORFs) identified in root and shoot by RiboTaper, and 7,016 putative sORFs identified in intergenic regions plus a list of common contaminants and all the corresponding decoy entries. For the final peptide identification, a second database (DB2) containing (i) those proteins (with more than 100 aa) and peptides (≤ 100 aa) that had been identified in the LC-MS/MS spectra using DB1 (6124 proteins and peptides) plus (ii) all peptide sequences (of ≥10 aa) derived from a three-frame translation of lncRNAs (CNTdb2.0) and TUFs (other RNA, lncRNA, antisense lncRNA, antisense RNA, novel transcribed region and uORF genes in Araport11) (TAIR ‘nc’). Sequence redundancy at amino acid sequence level was removed by grouping into clusters each subset using CD-HIT (https://www.bioinformatics.org/cd-hit/). The priority order that was used to remove redundancy was: Araport11 > Hsu et al. > Hanada et al. > CNTdb 2.0 > TAIR ‘nc’.  MS spectra were matched with the peptides in DB2 in a tryptic and semi-tryptic manner (DB2T, DB2ST). For the final peptide quantification, all the information obtained for the three analyses was kept. The most reliable quantifications were those from the first analysis (DB1T), then the information of those new detections in DB2T and the new peaks in DB2ST were added. For the final dataset, the origin of the information was annotated (DB1T, DB2T, DB2ST or a combination of more than one analysis). Finally, two lists of data were analyzed: one with the average abundance of the top three aminoacidic sequences for each accession (ID of peptides or proteins, TOP3) and one with all the aminoacidic partial sequences quantified for each accession (sequences). To each dataset, median normalization was performed by subtracting from each logged value the sample median and adding the global dataset median."],"omics_type":["Proteomics"],"labhead":["José Luis"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB, 08193 Cerdanyola del Vallès, Barcelona, Spain.  Institució Catalana de Recerca i Estudis Avançats (ICREA), 08010 Barcelona, Spain."],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["10.1093/PLPHYS/KIAG047"],"submitter_mail":["joseluis.riechmann@cragenomica.es"],"submitter_affiliation":["Centre for Research in Agricultural Genomics (CRAG)"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"The non-conventional peptidome of Arabidopsis flower development","description":"Our study is focused on the characterization of the Arabidopsis flower peptidome, using the floral homeotic mutants apetala1, apetala2, apetala3, pistillata, and agamous in comparison to the wild type. For peptide identification by LC-MS/MS, an extensive database of hypothetical novel Arabidopsis peptides was created. It comprised putative sORF-encoded peptides (SEPs) from intergenic regions, UTRs, ‘non-coding’ RNAs and other transcripts.","dates":{"publication":"2026-03-31","submission":"2025-01-28"},"accession":"PXD060293","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NCBITaxon:10090","NEWT:1006581","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NCBITaxon:10088","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEW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