ID   THIO_GEOCY              Reviewed;         106 AA.
AC   O96952;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=THIO;
OS   Geodia cydonium (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=6047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wiens M., Koziol C., Hassanein H.M.A., Batel R., Mueller W.E.G.;
RT   "Expression of the chaperones 14-3-3 and HSP70 induced by PCB 118
RT   (2,3',4,4'5-pentachlorobiphenyl) in the marine sponge Geodia cydonium.";
RL   Mar. Ecol. Prog. Ser. 165:247-257(1998).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; Y17147; CAA76654.1; -; mRNA.
DR   AlphaFoldDB; O96952; -.
DR   SMR; O96952; -.
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   PIRSF; PIRSF000077; 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..106
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120026"
FT   DOMAIN          2..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            26
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   106 AA;  11992 MW;  A7D1C5D2D44DBA19 CRC64;
     MVNFLKTKAD FDQALKDAGD KLVVIDFTAS WCGPCQRIAP KYVEMAKEFP DVIFYKVDVD
     ENDETAEAEK IQAMPTFKFY KSGKALSDYV QGANEAGLRE KIKKNK