Human Erythroid Membrane-Associated Protein (ERMAP) is a cell surface transmembrane protein that belongs to the immunoglobulin superfamily. It is hghly expressed in bone marrow and to a lower extent in leukocytes, thymus, lymph node and spleen. ERMAP contains 1 B30.2/SPRY domain and 1 Ig-like V-type (immunoglobulin-like) domain. It may serve as an erythroid cell receptor, possibly as a mediator of cell adhesion. ERMAP is responsible for the Scianna/Radin blood group system. Two transcript variants encoding the same protein have been found for this gene ERMAP.
Trypsin-3; also known as Trypsin III; brain trypsinogen; Serine protease 3 and PRSS3; is a secreted protein which belongs to thepeptidase S1 family. Trypsin-3 / PRSS3 is expressed is in pancreas and brain. It contains onepeptidase S1 domain. Trypsin-3 / PRSS3 can degrade intrapancreatic trypsin inhibitors that protect against CP. Genetic variants that cause higher mesotrypsin activity might increase the risk for chronic pancreatitis (CP). A sustained imbalance of pancreatic proteases and their inhibitors seems to be important for the development of CP. The trypsin inhibitor-degrading activity qualified PRSS3 as a candidate for a novel CP susceptibility gene. Trypsin-3 / PRSS3 has been implicated as a putative tumor suppressor gene due to its loss of expression; which is correlated with promoter hypermethylation; in esophageal squamous cell carcinoma and gastric adenocarcinoma.
The encoded protein contains two functional catalytic domains; a serine/threonine-protein kinase domain and an endoribonuclease domain. This protein functions as a sensor of unfolded proteins in the endoplasmic reticulum (ER) and triggers an intracellular signaling pathway termed the unfolded protein response (UPR). The UPR is an ER stress response that is conserved from yeast to mammals and activates genes involved in degrading misfolded proteins; regulating protein synthesis and activating molecular chaperones. This protein specifically mediates the splicing and activation of the stress response transcription factor X-box binding protein 1.
ERO1-Like Protein α (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It associates with ERP44, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport.
ERP27 contains 1 thioredoxin domain and is a noncatalytic member of the protein disulfide isomerase family. Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation; reduction; or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones; and are; therefore; part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization; as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. ERP27 is a widely expressed protein which localizes to the ER and may act as a protease; protein disulfide isomerase; thiol-disulfide oxidase or phospholipase. ERP27 doesn't contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.
Endoplasmic reticulum resident protein 27; also known as ER protein 27; C12orf46 and ERP27; is an endoplasmic reticulum luminal protein which is a member of the protein disulfide isomerase family. ERP27 contains one thioredoxin domain and does not contain a CXXC active site motif. ERP27 is widely expressed in many tissues; it has highest expression in pancreas; with lower levels in spleen; lung; kidney; thymus; and bone marrow. ERP27 interacts with PDIA3 and binds somatostatin-14 via hydrophobic interactions. ERP27 may act as a protease; protein disulfide isomerase; thiol-disulfide oxidase or phospholipase.
Endoplasmic reticulum resident protein 44 (TXNDC4) is is a 406 amino acid protein that contains one thioredoxin domain. TXNDC4 mediates thiol-dependent retention in the early secretory pathway and forms mixed disulfides with substrate proteins through its conserved CRFS motif.It can inhibit the calcium channel activity of ITPR1.It may have a role in the control of oxidative protein folding in the endoplasmic reticulum.
PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
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