THIO2_DROME
ID THIO2_DROME Reviewed; 106 AA.
AC Q9V429; A4V0H9; D3DMZ9; Q95SW4;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Thioredoxin-2;
DE Short=DmTrx-2;
GN Name=Trx-2; ORFNames=CG31884;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL25497.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seong K., Horiuchi N., Aigaki T.;
RT "Characterization of Drosophila thioredoxin.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:ADC54215.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ADC54215.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ADC54215.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11877442; DOI=10.1074/jbc.m200636200;
RA Bauer H., Kanzok S.M., Schirmer R.H.;
RT "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin
RT peroxidase-1 from Drosophila melanogaster: isolation and characterization
RT of a second thioredoxin in D.melanogaster and evidence for distinct
RT biological functions of Trx-1 and Trx-2.";
RL J. Biol. Chem. 277:17457-17463(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 9-106, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=15644209; DOI=10.1016/j.jmb.2004.11.004;
RA Wahl M.C., Irmler A., Hecker B., Schirmer R.H., Becker K.;
RT "Comparative structural analysis of oxidized and reduced thioredoxin from
RT Drosophila melanogaster.";
RL J. Mol. Biol. 345:1119-1130(2005).
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 {ECO:0000269|PubMed:11877442}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15644209}.
CC -!- DEVELOPMENTAL STAGE: Larval stages. {ECO:0000269|PubMed:11877442}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25497.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF220362; AAF37263.1; -; mRNA.
DR EMBL; AE014134; AAN10700.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10701.1; -; Genomic_DNA.
DR EMBL; AY060458; AAL25497.1; ALT_SEQ; mRNA.
DR EMBL; BT120324; ADC54215.1; -; mRNA.
DR RefSeq; NP_523526.1; NM_078802.4.
DR RefSeq; NP_723475.1; NM_164863.3.
DR PDB; 1XW9; X-ray; 2.30 A; A/B/C/D=9-106.
DR PDB; 1XWA; X-ray; 2.20 A; A/B/C/D=1-106.
DR PDB; 1XWB; X-ray; 2.20 A; A/B/C/D=9-106.
DR PDB; 1XWC; X-ray; 2.30 A; A=9-106.
DR PDBsum; 1XW9; -.
DR PDBsum; 1XWA; -.
DR PDBsum; 1XWB; -.
DR PDBsum; 1XWC; -.
DR AlphaFoldDB; Q9V429; -.
DR SMR; Q9V429; -.
DR BioGRID; 60380; 56.
DR IntAct; Q9V429; 5.
DR STRING; 7227.FBpp0079436; -.
DR PaxDb; Q9V429; -.
DR PeptideAtlas; Q9V429; -.
DR PRIDE; Q9V429; -.
DR DNASU; 34281; -.
DR EnsemblMetazoa; FBtr0079839; FBpp0079436; FBgn0040070.
DR EnsemblMetazoa; FBtr0079840; FBpp0079437; FBgn0040070.
DR GeneID; 34281; -.
DR KEGG; dme:Dmel_CG31884; -.
DR UCSC; CG31884-RA; d. melanogaster.
DR CTD; 34281; -.
DR FlyBase; FBgn0040070; Trx-2.
DR VEuPathDB; VectorBase:FBgn0040070; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000163988; -.
DR HOGENOM; CLU_090389_14_4_1; -.
DR InParanoid; Q9V429; -.
DR OMA; FPTIFEF; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9V429; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DME-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-5676934; Protein repair.
DR Reactome; R-DME-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 34281; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9V429; -.
DR GenomeRNAi; 34281; -.
DR PRO; PR:Q9V429; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0040070; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR Genevisible; Q9V429; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
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 3D-structure; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..106
FT /note="Thioredoxin-2"
FT /id="PRO_0000120034"
FT DOMAIN 1..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
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,
FT ECO:0000269|PubMed:15644209"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1XWA"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:1XWA"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:1XWA"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:1XWA"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:1XWA"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1XWA"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1XWA"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1XWA"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:1XWA"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1XWA"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1XWA"
SQ SEQUENCE 106 AA; 11737 MW; 255341DD95839FB8 CRC64;
MVYQVKDKAD LDGQLTKASG KLVVLDFFAT WCGPCKMISP KLVELSTQFA DNVVVLKVDV
DECEDIAMEY NISSMPTFVF LKNGVKVEEF AGANAKRLED VIKANI
