v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | ERp44 is an endoplasmic reticulum (ER)-resident protein that retrieves some ER-resident enzymes and immature oligomers of secretory proteins from the Golgi [ ]. It is composed of three thioredoxin (Trx)-like domains (a, b,and b'), followed by a C-terminal extension (C tail). Domain a contains a rather unique CRFS motif. The cysteine in this motif (Cys29) is known to form mixed disulfide bonds with client proteins to promote their thiol-dependent retention. Domain a is followed by two redox inactive Trx-like domains, b and b' []. Interestingly, the interactions between ERp44 and client proteins are pH-dependent []. This entry represents domain b', the second redox inactive TRX-like domain of ERp44. |
| Short Name | ERp44_PDI_b' |