S.NO	Uniprot ID	Protein Name	Sequence Length	Thioredoxin Repeated Region	Function
1	P07237	Protein disulfide-isomerase	508	DOMAIN 18 134 Thioredoxin 1 DOMAIN 349 475 Thioredoxin 2	"This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307)".
2	Q15084	Protein disulfide-isomerase A6	440	DOMAIN 20 133 Thioredoxin 1 DOMAIN 154 287 Thioredoxin 2	"May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:12204115). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (PubMed:24508390). May also regulate the UPR via the EIF2AK3 UPR sensor (PubMed:24508390). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (PubMed:15466936)".
3	Q13087	Protein disulfide-isomerase A2	525	DOMAIN 27 152 Thioredoxin 1 DOMAIN 367 496 Thioredoxin 2	Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.
4	Q8IXB1	DnaJ homolog subfamily C member 10	793	DOMAIN 130 232 Thioredoxin 1 DOMAIN 454 553 Thioredoxin 2 DOMAIN 557 662 Thioredoxin 3 DOMAIN 671 778 Thioredoxin 4	"Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress".
5	Q8NBS9	Thioredoxin domain-containing protein 5	432	DOMAIN 36 169 Thioredoxin 1 DOMAIN 170 295 Thioredoxin 2 DOMAIN 304 429 Thioredoxin 3	Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity).
6	Q6PKC3	Thioredoxin domain-containing protein 11	985	DOMAIN 92 214 Thioredoxin 1 DOMAIN 649 799 Thioredoxin 2	May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.

The 6 function of Thioredoxin of the protein