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Table 3 Characteristics of the wheat PDI-like proteins.

From: The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)

Name

Length

Mw

pI

N-glycisilation sites (putative)

Domain compositiona

Active site sequence

Conserved charge pair sequenceb

Conserved arginineb

TaPDIL1-1a

515

56.59

4.99

1: N283

a-b-b'-a'

CGHC, CGHC

E62-K96, E406-K439

R136, R475

TaPDIL1-1b

512

56.44

5.03

1: N283

a-b-b'-a'

CGHC, CGHC

E62-K96, E406-K439

R136, R475

TaPDIL1-1c

515

56.63

4.96

1: N283

a-b-b'-a'

CGHC, CGHC

E62-K96, E406-K439

R136, R475

TaPDIL2-1

588

63.80

4.61

2: N109, N212

c-a-b-b'-a'

CGHC, CGHC

E123-K157, E464-K497

R193, R535

TaPDIL3-1

541

59.61

4.95

1: N150

c-a-b-b'-a'

CERS, CVDC

L90-K124, E429-R462

R160, O492

TaPDIL4-1a

367

40.27

6.17

0

a°-a-D

CGHC, CGHC

E54-K87, E173-K211

R125, R244

TaPDIL4-1b

367

40.26

6.17

0

a°-a-D

CGHC, CGHC

E54-K87, E173-K211

R125, R244

TaPDIL5-1a

440

47.15

5.12

1: N170

a°-a-b

CGHC, CGHC

E51-K89, E188-K226

R119, R257

TaPDIL5-1b

440

47.22

5.36

1: N170

a°-a-b

CGHC, CGHC

E51-K89, E188-K226

R119, R257

TaPDIL6-1a

151

16.99

4.96

0

a

CKHC

Q56-S95

R126

TaPDIL6-1b

149

16.65

5.30

0

a

CKHC

Q54-S93

R124

TaPDIL7-1a

413

46.30

4.91

1: N275

a-b-b'-t

CGHC

D56-K90

R126

TaPDIL7-1b

417

46.62

4.91

2: N176, N279

a-b-b'-t

CGHC

D60-K94

R130

TaPDIL7-1c

413

46.32

4.87

2: N172, N275

a-b-b'-t

CGHC

D56-K90

R126

TaPDIL7-2a

418

46.40

5.12

0

a-b-b'-t

CGHC

D64-K98

R134

TaPDIL7-2b

418

46.34

5.03

1: N384

a-b-b'-t

CGHC

D64-K98

R134

TaPDIL8-1

485

54.41

6.90

ND

t-a-t

CYWS

N164-K203

R249

  1. a a = active site containing thioredoxin-like domain; b = inactive thioredoxin-like domain (note that the superscript are included to distinguish between domains of proteins containing more than one a and b domain on the basis of their position and not on the basis of sequence homology); c = acidic segment; D = Erp29c domain; t = transmembrane domain. b The position of conserved charge pair sequence and arginine residues that are considered important for the catalytic activity of different members of the human PDI family are determined on the basis of multiple alignments of the atype domains of wheat PDI-like proteins and human classical PDI [Accession number P07237] (Figure 3). ND = not determined because TaPDIL8-1 lacks a putative N-terminal signal peptide. Proteins without signal peptides are unlikely to be exposed to N-glycosilation machinery and thus may not be glycosylated in vivo even though they contain potential motifs.