ID   THIO2_DICDI             Reviewed;          88 AA.
AC   P29446;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Thioredoxin-2;
DE            Short=Trx-2;
DE   Flags: Fragment;
GN   Name=trxB; Synonyms=trx2; ORFNames=DDB_G0294491;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX3;
RX   PubMed=1577820; DOI=10.1016/s0021-9258(19)50177-6;
RA   Wetterauer B., Jacquot J.-P., Veron M.;
RT   "Thioredoxins from Dictyostelium discoideum are a developmentally regulated
RT   multigene family.";
RL   J. Biol. Chem. 267:9895-9904(1992).
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}.
CC   -!- CAUTION: Has not been found in the genome sequence, yet it seems to be
CC       really from D.discoideum. {ECO:0000305}.
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DR   EMBL; M91382; AAA33259.1; -; mRNA.
DR   PIR; B46264; B46264.
DR   AlphaFoldDB; P29446; -.
DR   SMR; P29446; -.
DR   OMA; VTFTFVH; -.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISS:dictyBase.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:dictyBase.
DR   GO; GO:0045454; P:cell redox homeostasis; ISS:dictyBase.
DR   GO; GO:0006457; P:protein folding; ISS:dictyBase.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..>88
FT                   /note="Thioredoxin-2"
FT                   /id="PRO_0000120030"
FT   DOMAIN          2..>88
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        31
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            25
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   NON_TER         88
SQ   SEQUENCE   88 AA;  10103 MW;  CEC73BCEFACB607C CRC64;
     MSRVIHISSN EELDKHLQAE RLVIDFSAAW CGPCRAISPV FEKLSNEFVT FTFVHVDIDK
     LSGHPIVKEI RSVPTFYFYR NGAKVSEF