Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:16910770, PubMed:22355694). As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells (PubMed:19536257). May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function (PubMed:19536257). Monomer (PubMed:25475729). Component of the Plasmodium translocon of exported proteins (PTEX) complex composed of HSP101, EXP2, PTEX150, PTEX88 and TRX2 (PubMed:19536257). Appears to localize to other uncharacterized organelles. Expressed during the parasite blood stage, including in rings, trophozoites, schizonts and merozoites (at protein level). The disulfide bond between Cys-82 and Cys-85 acts as a redox-active center and is reduced by thioredoxin reductase TRXR. Belongs to the thioredoxin family.