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Table 1 Identified proteins from Daphnia pulex acclimated to 10°C or 20°C

From: Acclimatory responses of the Daphnia pulex proteome to environmental changes. II. Chronic exposure to different temperatures (10 and 20°C) mainly affects protein metabolism

Spot no. Specificity N10: N20 Matched peptide sequences Sequence coveragea) Mascot scoreb) Mrgel/Mrpredicted pI gel/pI predicted SP Length PP Length Putative function (symbolic name)
Proteolytic enzymes
36 0.3* 1. VVAGEHSLR
2. SVDVPVVDDDTCNR
8.9% 149 30/26–29 4.4/4.4–4.8 15 27 Trypsin (TRY5L)
   1. LTAAEEPTRVEIR
2. IRNDVALIK
7.5% 80 30/25–30 4.4/4.5–5.3 18 48 Chymotrypsin (CHY1A)
37 0.2* 1. GVTDLTIFR
2. VVAGEHSLR
3. VVAGEHSLRTDSGLEQNR
9.8% 159 29/26–29 4.4/4.4–4.8 15 27 Trypsin (TRY5F)
   1. VVAGEHSLR
2. SVDVPVVDDDTCNR
8.9% 149 29/26–29 4.4/4.4–4.8 15 27 Trypsin (TRY5L)
38 0.5* 1. GLADADIAVFK
2. LIWMGQYNR
3. YYRDELAGK
10.7% 123 29/30 4.5/4.5 19   Endoribonuclease-like protein (ERNA)
   1. GLADADIAVFK
2. LIWMGQYNR
3. YYRDELAGK
8.0% 123 29/39 4.5/4.6 20   Endoribonuclease-like protein (ERNB)
   1. VVAGEHSLR
2. SVDVPVVDDDTCNR
8.9% 149 29/26–29 4.5/4.4–4.8 15 27 Trypsin (TRY5L)
   1. GVTDLTIFR
2. VVAGEHSLR
6.5% 80 29/26–29 4.5/4.4–4.8 15 27 Trypsin (TRY5F)
39 0.4* 1. VVAGEHSLR
2. SVDVPVVDDDTCNR
8.9% 149 29/26–29 4.6/4.4–4.8 15 27 Trypsin (TRY5L)
   1. GVTDLTIFR
2. VVAGEHSLR
6.5% 120 29/26–29 4.6/4.4–4.8 15 27 Trypsin (TRY5F)
40 0.6* 1. TTEEYYVSVQK
2. TGGGCYSYIGR
6.5% 112 25/23–27 4.5/4.7–4.6 ? 39 ? Astacin (ACN2)
   1. GVTDLTIFR
2. VVAGEHSLR
6.5% 109 25/26–29 4.5/4.4–4.8 15 27 Trypsin (TRY5F)
41 0.4* 1. LTAAEEPTR
2. LTAAEEPTRVEVR
3. IINDVALIK
9.1% 141 25/25–30 4.7/4.4–5.0 18 47 Chymotrypsin (CHY1C)
28 1.2 see [12]        Peptidase M13
Peptidase M2
Carboxylesterase, type B
Sphingomyelin phosphodiesterase
Sphingomyelin phosphodiesterase
31 0.6 see [12]    30/34–45
30/35–46
29/26–29
4.8/4.9–4.8
4.8/5.1–4.9
4.4/4.4–4.8
16
16
15
92
93
27
Carboxypeptidase A (CPA1A)
Carboxypeptidase A (CPA1B)
Trypsin (TRY5F)
32 0.3 see [12]    23/24–27 5.0/5.2–5.4 17 24 Trypsin (TRY4B)
Egg yolk proteins & precursors
43 7.3* see Figure 2    /190–220 /6.4–6.7 17–20   Vitellogenin (VTG1, VTG2, VTG4)
44 7.1* see Figure 3
see Figure 2
15.7%
2.8%
271 25/42
25/220
5.8/5.3
5.8/6.7
17
17
  Actin
Vitellogenin (VTG1)
45 5.9* see Figure 2 2.2% 132 21/190 5.2/6.4 20   Vitellogenin (VTG4)
46 5.2* see Figure 2 2.9% 361 21/220 5.9/6.7 17   Vitellogenin (VTG1)
47 4.9* see Figure 3
see Figure 2
9.6%
2.0%
  25/42
25/220
5.6/5.3
5.6/6.7
17   Actin
Vitellogenin (VTG1, VTG2)
   1. EDQMDYLEEK
2. LLVEKER
3. YSVDEELNK
3.6%   25/83 5.6/4.7    HSP90
49 4.4* see Figure 2 ?.?% ??? 21/190–220 4.8/6.4–6.7 17–20   Vitellogenin (VTG1, VTG2, VTG4)
50 4.2* see Figure 2 2.2% 163 20/220 5.7/6.7 17   Vitellogenin (VTG1)
52 3.7 see Figure 2 3.0% 344 18/220 5.1/6.7 17   Vitellogenin (VTG1, VTG2)
Cytoskeleton & muscle proteins
48 4.5* see Figure 2
see Figure 3
?.?% ??? 27/42 5.2/5.3    Actin
Vitellogenin (VTG4)
   1. EQLDEESEAK
2. AEELEDAKR
3. ATVLANQMEK
   27/220 5.2/5.9    Myosin heavy chain (MHC-1)
   1. LTTDPAFLEK
2. NAAAVHEIR
3. GDLGIEIPPEK
   27/?? 5.2/?    Pyruvate kinase
51 3.6* see Figure 3 ?.?% ??? 36/42 5.7/5.3    Actin
ATPase
42 9.8* 2. GNEDLSTAILK
3. MDELQLFK
4. GDIFIVR
5. KQLALIK
6. EMVELPLR
5.1% 214 16/89 5.3/5.0    AAA+ ATPase
Carbohydrate-modifying enzymes
35 1.2 see [12]        α-Amylase (AMY)
34 1.0 see [12]        Exo-β-1,3-Glucanase (EXG5)
1 0.4 see [12]        Cellubiohydrolase (CEL7A)
29 0.3 see [12]        Endo-β-1,4-Glucanase (CEL9A)
Paramyosin (PMY)
30 0.6 see [12]        Endo-β-1,4-Mannanase (MAN5A)
β-1,3-Glucan-binding protein
19 0.6 see [12]        Enolase (ENO)
  1. Identification was based on 2D gel electrophoresis and nano-HPLC-ESI-MS/MS analysis of trypsin-digested proteins matched against the "Frozen Gene Catalog" of the D. pulex protein database [2]. The compiled information includes the spot number (Figure 1A, B), the 10-to-20°C expression ratio, the number and sequences of matched peptides, the sequence coverage, the Mascot score as a statistical measure of identification probability, the experimental and theoretical molecular weight (Mr) and isolectric point (pI) of the mature protein (without signal peptide), the predicted length of the N-terminal signal peptide (SP) in secretory proteins, as well as the putative function and symbolic name of the protein. The length of the putative pro-peptide (PP) is additionally provided for proteolytic enzymes that are secrected as inactive precursors (zymogens). The predicted Mr and pI values of zymogens and the mature enzymes are given as value ranges. The amino acid sequences of the identified proteins were derived from the gene models listed in Table 2. a)percentage of predicted protein sequence covered by matched peptides. b)Probability-based MOWSE score: -10*Log(P), where P is the probability that the observed match is a random event. Scores >38 indicate identity or extensive homology (p < 0.05). Protein scores are derived from ions scores as a non-probabilistic basis for ranking protein hits. The Mascot-score calculation was performed using whole-protein sequence (including the N-terminal signal peptide in case of extracellular proteins). *p < 0.05 (t-Test).