ID   THIO_COPCM              Reviewed;         106 AA.
AC   Q9UW02;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
DE   AltName: Allergen=Cop c 2;
OS   Coprinus comatus (Shaggy mane).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Coprinus.
OX   NCBI_TaxID=56187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Brander K.A., Crameri R., Schuermann P., Pichler W.J., Helbling A.;
RT   "Coprinus thioredoxin as inhalative allergen and cross-reactive human
RT   autoantigen.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AJ242791; CAB52130.1; -; mRNA.
DR   AlphaFoldDB; Q9UW02; -.
DR   SMR; Q9UW02; -.
DR   Allergome; 226; Cop c 2.
DR   Allergome; 3210; Cop c 2.0101.
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   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..106
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120038"
FT   DOMAIN          2..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        30
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            24
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            31
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..33
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   106 AA;  11773 MW;  05A2155B210E8C69 CRC64;
     MVQVISNLDE FNKLTNSGKI IIIDFWATWC GPCRVISPIF EKFSEKYGAN NIVFAKVDVD
     TASDISEEAK IRAMPTFQVY KDGQKIDELV GANPTALESL VQKSLA