ID   TRXF_BRANA              Reviewed;         182 AA.
AC   O48897;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Thioredoxin F-type, chloroplastic;
DE            Short=Trx-F;
DE   Flags: Precursor;
GN   Name=TRXF;
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=Leaf;
RA   Mora-Garcia S.E.F., Rodriguez-Suarez R.J., Wolosiuk R.A.;
RL   Submitted (AUG-1997) 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 F
CC       form is known to activate a number of enzymes of the photosynthetic
CC       carbon cycle (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC       reductase (FTR) and ferredoxin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF018174; AAC04671.1; -; mRNA.
DR   PIR; T07837; T07837.
DR   AlphaFoldDB; O48897; -.
DR   SMR; O48897; -.
DR   GO; GO:0009507; C:chloroplast; 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   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..182
FT                   /note="Thioredoxin F-type, chloroplastic"
FT                   /id="PRO_0000034158"
FT   DOMAIN          52..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            96
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            103
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            104
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..105
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   182 AA;  19757 MW;  9EE3E6AC7C0F35A6 CRC64;
     MPLSLRLAPS PTALSPTTGG FSPAKKQCRI PSYSGVATTT RRIGLCSLDY VKRGDSSVVR
     CSLQTVNVSV GQVTEVDKDT FWPIVKAAGE KIVVLDMYTQ WCGPCKVIAP KYKALSEKYE
     DVVFLKLDCN PENRPLAKEL GIRVVPTFKI LKDNQVVKEV TGAKYDDLVA AIETARSASS
     SG