ID   TRXH2_BRANA             Reviewed;         119 AA.
AC   Q39362;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Thioredoxin H-type 2;
DE            Short=Trx-H-2;
GN   Name=THL-2;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pistil;
RX   PubMed=8837514; DOI=10.2307/3870256;
RA   Bower M.S., Matias D.D., Fernandes-Carvalho E., Mazzurco M., Gu T.,
RA   Rothstein S.J., Goring D.R.;
RT   "Two members of the thioredoxin-h family interact with the kinase domain of
RT   a Brassica S locus receptor kinase.";
RL   Plant Cell 8:1641-1650(1996).
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   -!- TISSUE SPECIFICITY: Preferentially expressed in floral tissues.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U59380; AAB53695.1; -; mRNA.
DR   PIR; T08142; T08142.
DR   AlphaFoldDB; Q39362; -.
DR   SMR; Q39362; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 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..119
FT                   /note="Thioredoxin H-type 2"
FT                   /id="PRO_0000120052"
FT   DOMAIN          2..115
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   119 AA;  12949 MW;  84A9985C618B1246 CRC64;
     MAAEEGQVIG CHEIDVWAVQ LDTAKQSNKL IVIDFTASWC PPCRMIAPVF ADLAKKFMSS
     AIFFKVDVDE LQNVAQEFGV EAMPTFVLIK DGNVVDKVVG ARKEDLHATI AKHTGVATA