ID   THIO2_DROYA             Reviewed;         106 AA.
AC   Q6XHI1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Thioredoxin-2;
DE            Short=Trx-2;
GN   Name=Trx-2;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:AAR10225.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14525923; DOI=10.1101/gr.1311003;
RA   Domazet-Loso T., Tautz D.;
RT   "An evolutionary analysis of orphan genes in Drosophila.";
RL   Genome Res. 13:2213-2219(2003).
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. As a reducing substrate
CC       of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1 (By
CC       similarity). {ECO:0000250|UniProtKB:P47938}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000255}.
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DR   EMBL; AY232202; AAR10225.1; -; mRNA.
DR   AlphaFoldDB; Q6XHI1; -.
DR   SMR; Q6XHI1; -.
DR   STRING; 7245.FBpp0263867; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblMetazoa.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..106
FT                   /note="Thioredoxin-2"
FT                   /id="PRO_0000120035"
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:0000250|UniProtKB:P47938,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   106 AA;  11725 MW;  6CEA2DFF096F2F50 CRC64;
     MVYQIKDKAD LNGQLTKASG KLVVLDFFAT WCGPCKMISP KLAELSTQYA DTVVVLKVDV
     DECEDIAMEY NISSMPTFVF LKNGVKVEEF AGANAQRLED VIKANI