Thioredoxin-like protein 1 (TXNL1)

Thioredoxin-like protein 1 (TXNL1) is a cytosolic, evolutionarily conserved protein with a thioredoxin fold that displays two documented functions: a redox-active disulfide reductase (akin to classical thioredoxins) and an ATP-independent chaperone activity[1][7]. As a thioredoxin-fold protein, TXNL1 supports disulfide reduction in proteins (including insulin, cystine, glutathione disulfide) via reactions coupled to thioredoxin reductase (TrxR1) and NADPH, although its catalytic efficacy is lower than canonical thioredoxin 1 (TXN)[1][7]. Uniquely, TXNL1 also performs chaperone functions independently of its redox capacity, including preventing protein aggregation and stabilizing denatured proteins, an activity not requiring ATP or its active site cysteine residues[1]. TXNL1 is expressed in all human tissues, highest in the thyroid gland, and interacts directly with proteasomal subunits for ubiquitin-independent degradation, highlighting its role in protein homeostasis[2][5]. It is genetically associated with susceptibility to certain infections (notably Ehrlichiosis), but no drugs are known to directly target TXNL1, nor is it an established biomarker or therapeutic target at this time[3][6][7].

Other names

Thioredoxin-like protein 1TXNL1TRP32TXLTXNLTxl32 kDa thioredoxin-related proteinthioredoxin-like, 32kDHEL-S-114TXL-1epididymis secretory protein Li 114thioredoxin-related protein 1