TXNDC4 Peptide - Middle Region Blocking Peptide

This gene encodes a member of the protein disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins. It has an inferred N-terminal signal peptide, a catalytically active thioredoxin (TRX) domain, two TRX-like domains and a C-terminal ER-retention sequence. This protein functions as a pH-regulated chaperone of the secretory pathway and likely plays a role in protein quality control at the endoplasmic reticulum - Golgi interface. [provided by RefSeq, Dec 2016]

ERP44: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum. Forms mixed disulfides with both ERO1L and ERO1LB and cargo folding intermediates. Directly interacts with ITPR1 in a pH-, redox state- and calcium-dependent manner, but not with ITPR2 or ITPR3. The strength of this interaction inversely correlates with calcium concentration. By endoplasmic reticulum stress.

Protein type: Secreted, signal peptide; Endoplasmic reticulum; Secreted; Isomerase

Chromosomal Location of Human Ortholog: 9q31.1

Cellular Component: endoplasmic reticulum membrane; cell surface; endoplasmic reticulum lumen; ER-Golgi intermediate compartment

Molecular Function: protein binding; protein disulfide isomerase activity

Biological Process: glycoprotein metabolic process; protein folding; cell redox homeostasis; response to unfolded protein