ID   TRXH_BRACM              Reviewed;         123 AA.
AC   O64432;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Thioredoxin H-type;
DE            Short=Trx-H;
GN   Name=PEC-2;
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Anther;
RX   PubMed=9539157; DOI=10.1016/s0014-5793(98)00174-4;
RA   Toriyama K., Hanaoka K., Okada T., Watanabe M.;
RT   "Molecular cloning of a cDNA encoding a pollen extracellular protein as a
RT   potential source of a pollen allergen in Brassica rapa.";
RL   FEBS Lett. 424:234-238(1998).
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; AB010434; BAA25681.1; -; mRNA.
DR   PIR; T14379; T14379.
DR   RefSeq; NP_001288844.1; NM_001301915.1.
DR   AlphaFoldDB; O64432; -.
DR   SMR; O64432; -.
DR   STRING; 3711.Bra027469.1-P; -.
DR   EnsemblPlants; Bra027469.1; Bra027469.1-P; Bra027469.
DR   GeneID; 103839264; -.
DR   Gramene; Bra027469.1; Bra027469.1-P; Bra027469.
DR   KEGG; brp:103839264; -.
DR   OMA; INTHEEF; -.
DR   OrthoDB; 1482186at2759; -.
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_0000120054"
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;  13587 MW;  8E0A18DB446F0172 CRC64;
     MAATAELIPA GEVIACHTVE DWNNKLKAAK ESNKLIVIDF TAVWCPPCRF IAPIFVELAK
     KHLDVVFFKV DVDELATVAK EFDVQAMPTF VYMKGEEKLD KVVGAAKEEI EAKLLKHSQV
     AAA