ID   THIO_ECHGR              Reviewed;         107 AA.
AC   O17486;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=TRX;
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10448109; DOI=10.1006/bbrc.1999.1168;
RA   Chalar C., Martinez C., Agorio A., Salinas G., Soto J., Ehrlich R.;
RT   "Molecular cloning and characterization of a thioredoxin gene from
RT   Echinococcus granulosus.";
RL   Biochem. Biophys. Res. Commun. 262:302-307(1999).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AF034637; AAC14584.1; -; mRNA.
DR   AlphaFoldDB; O17486; -.
DR   SMR; O17486; -.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..107
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120037"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        37
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            28
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            35
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            36
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..37
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   107 AA;  11556 MW;  BE9525588D1E7EA2 CRC64;
     MSVEAVVKQV DGDALEAAIK GDKLLVCDFF ATWCGPCKSL APKLDAMAKE NEKVIFVKLD
     VDECQDVAEK YRVTAMPTLI VFKNGCEIGH VVGANEAGIR ELIQANA