ID   TRXH_RICCO              Reviewed;         118 AA.
AC   Q43636;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Thioredoxin H-type;
DE            Short=Trx-H;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sanguineus; TISSUE=Cotyledon;
RA   Szederkenyi J., Dolgener E., Schobert C.;
RL   Submitted (APR-1996) 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; Z70677; CAA94534.1; -; mRNA.
DR   PIR; T10170; T10170.
DR   RefSeq; XP_002534131.1; XM_002534085.2.
DR   AlphaFoldDB; Q43636; -.
DR   SMR; Q43636; -.
DR   STRING; 3988.XP_002534131.1; -.
DR   GeneID; 8266412; -.
DR   KEGG; rcu:8266412; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   OrthoDB; 1482186at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..118
FT                   /note="Thioredoxin H-type"
FT                   /id="PRO_0000120060"
FT   DOMAIN          2..114
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            41
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            42
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   118 AA;  13053 MW;  B5BD7ABB6601741B CRC64;
     MAAEEGQVIG CHTVEAWNEQ LQKGNDTKGL IVVDFTASWC GPCRFIAPFL AELAKKLPNV
     TFLKVDVDEL KTVAHEWAVE SMPTFMFLKE GKIMDKVVGA KKDELQQTIA KHMATAST