ID   TRXH_BRAOL              Reviewed;         123 AA.
AC   P68176; Q42388;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Thioredoxin H-type;
DE            Short=Trx-H;
DE   AltName: Full=Pollen coat protein;
GN   Name=BOPC17;
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ruiter R.K., Mettenmeyer T., Doughty J., van Eldik G.J., Van Herpen M.M.A.,
RA   Dickinson H.G., Schrauwen J.A.M., Wullems G.J.;
RT   "The pollen coat of Brassica oleracea contains a thioredoxin h-like
RT   protein.";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of the active center dithiol to a disulfide. The H
CC       form is known to activate a number of cytosolic enzymes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X89759; CAA61908.1; -; mRNA.
DR   AlphaFoldDB; P68176; -.
DR   SMR; P68176; -.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:EnsemblPlants.
DR   GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR   GO; GO:0010286; P:heat acclimation; IEA:EnsemblPlants.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:EnsemblPlants.
DR   GO; GO:0006457; P:protein folding; IEA:EnsemblPlants.
DR   GO; GO:0010188; P:response to microbial phytotoxin; IEA:EnsemblPlants.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; 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   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..123
FT                   /note="Thioredoxin H-type"
FT                   /id="PRO_0000120053"
FT   DOMAIN          2..119
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        45..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   123 AA;  13573 MW;  2E0A02C6735BDEC4 CRC64;
     MAATAEVIPA GEVIACHTVE DWNNKLKAAK ESNKLIVIDF TAVWCPPCRF IAPIFVELAK
     KHLDVVFFKV DVDELATVAQ EFDVQAMPTF VYMKGEEKLD KVVGAAKEEI EAKLLKHSQV
     AAA