THIO1_DROYA
ID THIO1_DROYA Reviewed; 107 AA.
AC P60226; B4PZR8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Thioredoxin-1;
DE Short=Trx-1;
DE AltName: Full=Protein deadhead;
GN Name=dhd; Synonyms=Trx-1; ORFNames=GE16391;
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]
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17701050; DOI=10.1007/s00427-007-0175-y;
RA Svensson M.J., Stenberg P., Larsson J.;
RT "Organization and regulation of sex-specific thioredoxin encoding genes in
RT the genus Drosophila.";
RL Dev. Genes Evol. 217:639-650(2007).
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.
CC Required for female meiosis and early embryonic development (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in testes and ovaries.
CC {ECO:0000269|PubMed:17701050}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AY231790; AAR09813.1; -; mRNA.
DR EMBL; CM000162; EDX01135.1; -; Genomic_DNA.
DR RefSeq; XP_002100027.1; XM_002099991.2.
DR AlphaFoldDB; P60226; -.
DR SMR; P60226; -.
DR STRING; 7245.FBpp0261401; -.
DR EnsemblMetazoa; FBtr0403990; FBpp0362727; FBgn0233920.
DR GeneID; 6524164; -.
DR KEGG; dya:Dyak_GE16391; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR OMA; CIAKQHA; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P60226; -.
DR Proteomes; UP000002282; Chromosome X.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0007143; P:female meiotic nuclear division; IEA:EnsemblMetazoa.
DR GO; GO:0035042; P:fertilization, exchange of chromosomal proteins; IEA:EnsemblMetazoa.
DR GO; GO:0060322; P:head development; 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 PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Electron transport; Nucleus; Redox-active center;
KW Transport.
FT CHAIN 1..107
FT /note="Thioredoxin-1"
FT /id="PRO_0000120033"
FT DOMAIN 2..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 8..10
FT /note="TDF -> NDY (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="N -> T (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="D -> E (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="T -> S (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> Q (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..90
FT /note="AFS -> SFA (in Ref. 1; AAR09813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 12354 MW; 58712AAD66B8E534 CRC64;
MASVRTMTDF HKRIEAADDK LIVLDFYANW CGPCKDMEST VKSLARKYST KAVVLKIDVD
KFEELTERYK VRSMPTFVFL RNNRRLAAFS GADEHKLTNM MAKLVKA
