Table 3 Primary structures of signal peptides of possible TRAP clients and non-TRAP clients

From: Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import

UniProt ID

Gene name

Signal peptide

TM

N-glyc

GP %

Hph

Q9H173 */**

SIl1

MAPQSLPSSRMAPLGMLLGLLMAACFTFCLS

−

+

16.1

0.992

P27797 */**

CALR

MLLSVPLLLGLLGLAVA

−

+

17.6

2.307

P14625 *

HSP90B1

MRALWVLGLCCVLLTFGSVRA

−

+

9.52

1.446

Q9Y4L1 *

HYOU1

MADKVRRQRPRRRVCWALVAVLLADLLALSDT

−

+

3.12

−0.101

P23284 *

PPIB

MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAA

−

+

12.1

0.961

—

mut-PPIB

MLRLGPRNMKVLLPPALIAGSVFFLLLPGPSAA

−

+

24.2

0.814

Q9Y3A6 */**

TMED5

MGDKIWLPFPVLLLAALPPVLLPGAAG

+

−

29.6

1.074

—

mut-TMED5

MGDKIWLPFPVLLLAALPPVLLAAAAG

+

−

22.2

1.250

  1. Amino acid sequences of signal peptides (SP) are shown together with protein accession number, gene name, presence of transmembrane domains (TM) or N-glycosylation sites (N-glyc), GP content in %, and hydrophobicity (Hph). Signal peptides are divided into N-terminal, hydrophobic, and C-terminal domains according to Phobius prediction (www.phobius.sbc.su.se). *, accession numbers of proteins, which were also negatively affected by Sec61 complex depletion; **, validated proteins. TMED5 was copied from Table 1 for comparison. Mutated variants of TMED5 and PPIB were generated by quick change mutagenesis in one and two steps, respectively, and verified by sequence analysis. The CALR genes codes for Calreticulin, the HSP90B1 gene for Grp94, the HYOU1 gene for Grp170. mut, mutated
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