{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit_phosphoenrich__FDR.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit__FDR.xlsx"],"Wiff":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit_phosphoenrich.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit.wiff.scan","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit_phosphoenrich.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit.wiff","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit.wiff_PEAKSsearch.xls"],"Xls":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD076788/mussel_sperm_PKA_C_subunit_phosphoenrich_PEAKSsearch.xls"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sbbravo@gmail.com"],"submitter":["Susana Bravo"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["phosphoproteomics","Camp-dependent protein kinase; pka; catalytic subunit; lc–ms/ms; phosphoproteomics; phosphorylation sites; tio₂ enrichment; mytilus galloprovincialis; sperm","mytilus galloprovincialis","tio₂ enrichment","pka","phosphorylation sites","sperm","catalytic subunit","lc–ms/ms","Camp-dependent protein kinase"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076788"],"sample_protocol":["Purified PKA C‑subunit protein from Mytilus galloprovincialis spermatozoa was processed for LC–MS/MS analysis using an in‑gel digestion workflow adapted from established protocols. Excised polyacrylamide gel bands were subjected to reduction with 10 mM dithiothreitol in 50 mM ammonium bicarbonate, followed by alkylation with 55 mM iodoacetamide under light protected conditions. After alkylation, gel pieces were sequentially washed with 50% methanol in ammonium bicarbonate, dehydrated in acetonitrile, and dried under vacuum. Proteolytic digestion was conducted overnight at 37 °C using modified porcine trypsin (20 ng/µL in 20 mM ammonium bicarbonate). Resulting peptides were extracted by three consecutive incubations in 60% acetonitrile containing 0.5% formic acid, pooled, and stored at −20 °C until mass spectrometric analysis. Peptide samples were analyzed by nanoLC–MS/MS on a TripleTOF 6600 mass spectrometer operated in data dependent acquisition (DDA) mode. MS/MS spectra were used for protein identification and sequence coverage determination through ProteinPilot™ (SCIEX), searching against a Mytilus‑specific UniProt database and standard search parameters. Post translational modification analysis, including phosphorylation site identification and localization, was performed using PEAKS (Bioinformatics Solutions Inc.), incorporating variable phosphorylation on serine, threonine, and tyrosine residues. To enhance detection of low abundance phosphopeptides, a portion of the digested material was subjected to titanium dioxide (TiO₂)–based phosphopeptide enrichment using the High Select™ TiO₂ Phosphopeptide Enrichment Kit following the manufacturer’s recommendations. Enriched fractions were reanalyzed under identical LC–MS/MS acquisition settings, and data were reprocessed using both ProteinPilot™ and PEAKS to confirm protein identity and validate phosphorylation sites through independent spectral evidence. This multi step workflow ensured high confidence identification of the sperm specific PKA C subunit and robust mapping of its phosphorylation profile."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["LC–MS/MS data were acquired on a TripleTOF 6600 mass spectrometer operated in data dependent acquisition (DDA) mode. MS1 scans were collected over m/z 350–1250, followed by MS/MS of the most intense precursor ions using collision induced dissociation with dynamic exclusion enabled. Peptide and protein identifications were performed using ProteinPilot™ (SCIEX), searching against a Mytilus galloprovincialis UniProt database with tryptic specificity and standard precursor/fragment mass tolerances. Results were filtered at a 1% FDR at both peptide and protein levels using a target–decoy approach. Post translational modification (PTM) analysis was conducted using PEAKS, with phosphorylation on Ser/Thr/Tyr as variable modifications and carbamidomethylation of cysteine as a fixed modification. Phosphopeptide spectrum matches were required to meet stringent quality criteria, including ≤1% peptide level FDR, PEAKS confidence score thresholds, and site localization probability ≥0.75. Phosphosites were further validated by detection in TiO₂ enriched fractions. Together, these workflows yielded high confidence identifications covering ~90% of the protein and enabled robust mapping of phosphorylation sites."],"omics_type":["Proteomics"],"labhead":["Susana B Bravo"],"instrument_platform":[""],"labhead_affiliation":["Instituto de >Investigaciones Sanitarias de Santiago de Compostela"],"submission_type":["PARTIAL"],"species":["Crenomytilus"],"submitter_mail":["sbbravo@gmail.com"],"publication":["42533721 Ibarguren I, Flament-Simon SC, Losada AP, Bravo SB, Villamarín JA. Mussel Spermatozoa Express a Specific Isoform of the Catalytic Subunit of cAMP-Dependent Protein Kinase. Mol Reprod Dev. 2026 93(8):e70139 10.1002/mrd.70139"],"submitter_affiliation":["FIDIS"],"submitter_country":["Spain"],"pubmed_abstract":["cAMP-dependent protein kinase (PKA) plays a central role in regulating sperm motility in both invertebrates and mammals. The sea mussel Mytilus galloprovincialis provides a valuable model for investigating the molecular mechanisms underlying gamete activation in externally fertilizing organisms. In previous work, several catalytic (C) subunit isoforms of PKA were isolated from this species. Here, we report that one of these isoforms appears to be specifically expressed in spermatozoa, indicating the presence of a sperm-specific C-subunit isoform in a non-mammalian species. The protein was purified from male gonadal tissue and identified by LC-MS/MS as the isoform corresponding to UniProt entry A0A8B6GIP6. Sequence analysis revealed that this mussel C-isoform shares strong homology with mammalian sperm-specific Cα2-isoform within the catalytic core but possesses a unique N-terminal region. Whereas mammalian Cα2 contains a short six-residue N-terminal extension, the mussel sperm isoform features a longer acidic extension of 17 amino acids. Moreover, phosphoproteomic analysis reveals the presence of two phosphorylation sites (Ser5 and Thr30) in the N-terminal tail of the mussel C-subunit that are absent in Cα2. These structural differences suggest specific regulatory mechanisms associated with sperm activation in externally fertilizing bivalves. Immunolocalization studies show that the mussel sperm C-subunit is distributed in the acrosomal region, mitochondria, and along the flagellum, where it is predominantly associated with R<sub>myt2</sub>, a type II regulatory subunit previously characterized in the mussel."],"pubmed_title":["Mussel Spermatozoa Express a Specific Isoform of the Catalytic Subunit of cAMP-Dependent Protein Kinase."],"pubmed_authors":["Ibarguren Izaskun I, Flament-Simon Saskia-Camille SC, Losada Ana P AP, Bravo Susana B SB, Villamarín José Antonio JA"],"additional_accession":[]},"is_claimable":false,"name":"Identification and phosphorylation site mapping of a sperm specific PKA C subunit isoform from Mytilus galloprovincialis","description":"This project investigates a sperm-specific isoform of the catalytic (C) subunit of cAMP-dependent protein kinase (PKA) in the marine mussel Mytilus galloprovincialis, an externally fertilizing invertebrate widely used as a model for gamete activation studies. A C-subunit isoform purified from male gonadal tissue was identified by LC–MS/MS as the protein corresponding to UniProt entry A0A8B6GIP6. Sequence analysis revealed high structural conservation with mammalian Cα2 within the catalytic core, but also demonstrated the presence of a markedly extended, acidic N-terminal region unique to mussel sperm. Comprehensive phosphoproteomic profiling identified phosphorylation at Ser5 and Thr30 within the N-terminal extension, as well as a likely regulatory phosphosite at Thr200 located in the activation loop of the kinase catalytic core. Phosphorylation events detected in unenriched samples were independently validated through TiO₂ phosphopeptide enrichment followed by LC–MS/MS. These findings reveal structural and regulatory motifs not present in mammalian sperm PKA isoforms and suggest the existence of molluscan-specific mechanisms controlling sperm activation.","dates":{"publication":"2026-09-07","submission":"2026-04-09"},"accession":"PXD076788","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:77173","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5537","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:33554","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:980415","NEWT:3702","NEWT:66440","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:34878","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:1385720","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:133894","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:367774","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9917","NEWT:95912","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1392997","NEWT:114796","NEWT:1150621","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:89252","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEW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