THIO1_DROME
ID THIO1_DROME Reviewed; 107 AA.
AC P47938; Q8MSC0; Q9W4D5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Thioredoxin-1;
DE Short=DmTrx-1;
DE AltName: Full=Protein deadhead;
GN Name=dhd; Synonyms=Trx-1; ORFNames=CG4193;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7516301; DOI=10.1093/genetics/136.3.1075;
RA Salz H.K., Flickinger T.W., Mittendorf E., Pellicena-Palle A.,
RA Petschek J.P., Albrecht E.B.;
RT "The Drosophila maternal effect locus deadhead encodes a thioredoxin
RT homolog required for female meiosis and early embryonic development.";
RL Genetics 136:1075-1086(1994).
RN [2]
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]
RP FUNCTION, DEVELOPMENTAL STAGE, DISULFIDE BOND, AND MUTAGENESIS OF CYS-31
RP AND CYS-34.
RX PubMed=9106167; DOI=10.1016/s0925-4773(96)00650-8;
RA Pellicena-Palle A., Stitzinger S.M., Salz H.K.;
RT "The function of the Drosophila thioredoxin homologue encoded by the
RT deadhead gene is redox-dependent and blocks the initiation of development
RT but not DNA synthesis.";
RL Mech. Dev. 62:61-65(1997).
RN [6]
RP FUNCTION.
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14579129; DOI=10.1007/s00412-003-0253-5;
RA Svensson M.J., Chen J.D., Pirrotta V., Larsson J.;
RT "The ThioredoxinT and deadhead gene pair encode testis- and ovary-specific
RT thioredoxins in Drosophila melanogaster.";
RL Chromosoma 112:133-143(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.
CC Required for female meiosis and early embryonic development.
CC {ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:9106167}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14579129}.
CC -!- TISSUE SPECIFICITY: Ovary specific. Expressed present in the nurse
CC cells from stage 9 of ovary development and is transported into the
CC oocyte. Expressed throughout oogenesis. {ECO:0000269|PubMed:14579129}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9106167}.
CC -!- MISCELLANEOUS: The TrxT gene, which encodes an testis specific
CC thioredoxin, is adjacent to the dhd gene and shares some regulatory
CC region with it.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; L27072; AAA28937.1; -; mRNA.
DR EMBL; AE014298; AAF46019.1; -; Genomic_DNA.
DR EMBL; AY118929; AAM50789.1; ALT_SEQ; mRNA.
DR PIR; S47867; S47867.
DR RefSeq; NP_001284882.1; NM_001297953.1.
DR RefSeq; NP_511046.1; NM_078491.3.
DR PDB; 6ZMU; X-ray; 1.95 A; A/B/C/D=1-107.
DR PDBsum; 6ZMU; -.
DR AlphaFoldDB; P47938; -.
DR SMR; P47938; -.
DR BioGRID; 57954; 18.
DR DIP; DIP-21555N; -.
DR IntAct; P47938; 1.
DR STRING; 7227.FBpp0070717; -.
DR PaxDb; P47938; -.
DR DNASU; 31444; -.
DR EnsemblMetazoa; FBtr0070749; FBpp0070717; FBgn0011761.
DR EnsemblMetazoa; FBtr0345745; FBpp0311766; FBgn0011761.
DR GeneID; 31444; -.
DR KEGG; dme:Dmel_CG4193; -.
DR UCSC; CG4193-RA; d. melanogaster.
DR CTD; 31444; -.
DR FlyBase; FBgn0011761; dhd.
DR VEuPathDB; VectorBase:FBgn0011761; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; P47938; -.
DR OMA; CIAKQHA; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P47938; -.
DR SignaLink; P47938; -.
DR BioGRID-ORCS; 31444; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31444; -.
DR PRO; PR:P47938; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011761; Expressed in egg chamber and 18 other tissues.
DR ExpressionAtlas; P47938; baseline and differential.
DR Genevisible; P47938; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:FlyBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0035042; P:fertilization, exchange of chromosomal proteins; IMP:FlyBase.
DR GO; GO:0060322; P:head development; IMP:FlyBase.
DR GO; GO:0035041; P:sperm DNA decondensation; 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 PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Nucleus;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..107
FT /note="Thioredoxin-1"
FT /id="PRO_0000120032"
FT DOMAIN 2..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 31
FT /note="Nucleophile"
FT ACT_SITE 34
FT /note="Nucleophile"
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 SITE 33
FT /note="Contributes to redox potential value"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:9106167"
FT MUTAGEN 31
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:9106167"
FT MUTAGEN 34
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:9106167"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:6ZMU"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6ZMU"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:6ZMU"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:6ZMU"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:6ZMU"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6ZMU"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:6ZMU"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6ZMU"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6ZMU"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6ZMU"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:6ZMU"
SQ SEQUENCE 107 AA; 12384 MW; 6A716FD55690C53B CRC64;
MASVRTMNDY HKRIEAADDK LIVLDFYATW CGPCKEMEST VKSLARKYSS KAVVLKIDVD
KFEELTERYK VRSMPTFVFL RQNRRLASFA GADEHKLTNM MAKLVKA
