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 27-MAR-2024, entry version 83.
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; Agaricineae; 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 CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 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
//
