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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.