Supplemental Data
Files in this Data Supplement:
- Supplemental figure 1 - Abundances of peptides from a) transepithelial ion transport proteins, b) molecular chaperones, and c) mitochondrial proteins. Heat maps depict targeted EIC integrals of peptides identified for the corresponding proteins. Three technical replicates are shown for 34ppt, 70 ppt, and 90 ppt salinity acclimation experiments (from left to right). Heat maps were generated with Gene-E (BROAD Institute). Peptide abundances are shown as arbitrary units (AU) corresponding to a FW handling control mean of 1. Each peptide is labeled on the right hand side with the UniProtKB accession number (AC), annotated protein name, mass to charge ratio (m/z), retention time (Rt), charge (z), and peptide sequence.
- Supplemental table 1 - Peptide identification data for all proteins identified in this study. These data were exported from PRIDE accession # 28628. Peptides are sorted by protein ID (UniProtKB accession number) in alphabetical order. Rows containing peptides shared by multiple protein IDs (e.g. isoforms) are shaded grey. The position of amino acid modifications is indicated in brackets following the amino acid that is modified, [16.0] = oxidation / hydroxylation and [57.0] = carbamidomethylation. The number of modifications per peptide is indicated in column 6.
- Supplemental table 2 - Protein identification data for all proteins identified in this study. These data were exported from PRIDE accession # 28628. Only a single peptide to protein mapping is kept in PRIDE data and no protein groupings are shown. Each protein ID is identified by the corresponding UniProtKB accession number (UniProt AC) and includes at least one distinct peptide mapping that is unique for that protein and not found in any of the other proteins.
- Supplemental table 3 - Detailed two-factorial ANOVA results for targeted quantitation of salinity effects on A) ion transport proteins, B) molecular chaperones, and C) mitochondrial proteins.