Acyl-coenzyme A thioesterase 13, also known as Thioesterase superfamily member 2, ACOT13, THEM2 and PNAS-27, is a member of the thioesterase PaaI family. Acyl-CoA thioesterases catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. THEM2 is a cytoplasmic protein and exsis in a homotetramer. THEM2 has been identified as an interacting protein of phosphatidylcholine transfer protein. THEM2 also regulates hepatic lipid and glucose metabolism.
Thioredoxin-2 (TXN2) is a mitochondrial member of the thioredoxin family. Thioredoxin-2 is extensively expressed in adult and fetal tissues. Thioredoxin-2 contains an N-terminal 59 amino acid transit peptide; which is cleaved before translocating to mitochondria. Mitochondrial thioredoxin play important roles in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. Thioredoxin-2 could be involved in the resistance to anti-tumor agents and possesses a dithiol-reducing activity. In addition; Thioredoxin-2 is important at low oxidative stress conditions.
Thioredoxin-2; also known as TXN2; MTRX and TRX2; is a member of the thioredoxin family. Tryparedoxins (TXN) are thioredoxin-related proteins which; as trypanothione:peroxiredoxin oxidoreductases; constitute the trypanothione-dependent antioxidant defense and may also serve as substrates for ribonucleotide reductase in trypanosomatids. Thioredoxin-2 / TXN2 contains onethioredoxin domain. It is widely expressed in adult (at protein level) and fetal tissues. Human Thioredoxin-2 / TXN2 is a small redox protein important in cellular antioxidant defenses; as well as in the regulation of apoptosis. Thioredoxin-2 / TXN2 has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Thioredoxin-2 / TXN2 could be involved in the resistance to anti-tumor agents. It possesses a dithiol-reducing activity. Thioredoxin-2 / TXN2 plays an important role in protecting the mitochondria against oxidative stress and in sensitizing the cells to ROS-induced apoptosis. Mammalian Thioredoxin-2 / TXN2 is a mitochondrial isoform of highly evolutionary conserved thioredoxins. Thioredoxins are small ubiquitous protein-disulfide oxidoreductases implicated in a large variety of biological functions.
Thioredoxin; also known as ATL-derived factor; Surface-associated sulphydryl protein; SASP and TXN; is a nucleus; cytoplasm and secreted protein which belongs to thethioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins; and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO); and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
Thioredoxin (TXN) is a member of the Thioredoxin family. Thioredoxin exists as a disulfide-linked homodimer and contains one Thioredoxin domain. Thioredoxin is up-regulated by ionizing radiation. Thioredoxin participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin also plays a role in the reversible S-nitrosylation of cysteine residues in target proteins; and thereby contributes to the response to intracellular nitric oxide.
Thimet Oligopeptidase (THOP1) belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.
Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability (Probable). May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF.Facilitates neutrophil migration across renal epithelia.
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