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THIOT_DROME
ID   THIOT_DROME             Reviewed;         157 AA.
AC   Q8IFW4; Q9W4D6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Thioredoxin-T;
DE            Short=ThioredoxinT;
GN   Name=TrxT; ORFNames=CG3315;
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Testis;
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).
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).
CC   -!- FUNCTION: Probably 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. Its tissue specificity
CC       suggests a regulatory role in the germline.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14579129}. Chromosome
CC       {ECO:0000269|PubMed:14579129}. Note=Specifically associated with the Y
CC       chromosome loops.
CC   -!- TISSUE SPECIFICITY: Testis specific. Not expressed in the embryo.
CC       Becomes progressively more strongly expressed during larval and pupal
CC       development. In testis, it is strongly expressed in young
CC       spermatocytes, and postmeiotic spermatid stages, then expression
CC       decreases at the nuclear elongation stage. Strongly expressed in the
CC       waste bag, in which material no longer needed for the mature sperm is
CC       eliminated. Not expressed in the stem cells and spermatogonial cells.
CC       {ECO:0000269|PubMed:14579129}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed maternally.
CC       {ECO:0000269|PubMed:14579129}.
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; AJ507731; CAD45644.1; -; mRNA.
DR   EMBL; AE014298; AAF46018.2; -; Genomic_DNA.
DR   RefSeq; NP_001284881.1; NM_001297952.1.
DR   RefSeq; NP_572212.1; NM_131984.1.
DR   PDB; 6Z7O; X-ray; 2.33 A; A=1-157.
DR   PDBsum; 6Z7O; -.
DR   AlphaFoldDB; Q8IFW4; -.
DR   SMR; Q8IFW4; -.
DR   BioGRID; 57953; 1.
DR   IntAct; Q8IFW4; 18.
DR   STRING; 7227.FBpp0070722; -.
DR   PaxDb; Q8IFW4; -.
DR   DNASU; 31443; -.
DR   GeneID; 31443; -.
DR   KEGG; dme:Dmel_CG3315; -.
DR   CTD; 31443; -.
DR   FlyBase; FBgn0029752; TrxT.
DR   VEuPathDB; VectorBase:FBgn0029752; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_7_0_1; -.
DR   InParanoid; Q8IFW4; -.
DR   PhylomeDB; Q8IFW4; -.
DR   BioGRID-ORCS; 31443; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; TrxT; fly.
DR   GenomeRNAi; 31443; -.
DR   PRO; PR:Q8IFW4; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   ExpressionAtlas; Q8IFW4; baseline and differential.
DR   Genevisible; Q8IFW4; DM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000806; C:Y chromosome; IDA:UniProtKB.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISS:FlyBase.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IDA: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   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; Chromosome; Disulfide bond; Electron transport; Nucleus;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..157
FT                   /note="Thioredoxin-T"
FT                   /id="PRO_0000120036"
FT   DOMAIN          2..107
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          132..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        32..35
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        47..48
FT                   /note="HE -> QQ (in Ref. 2; AAF46018)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..17
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   HELIX           33..48
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   HELIX           64..69
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   STRAND          74..82
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:6Z7O"
FT   HELIX           95..104
FT                   /evidence="ECO:0007829|PDB:6Z7O"
SQ   SEQUENCE   157 AA;  17499 MW;  5D8EAB28344BFA6B CRC64;
     MVYPVRNKDD LDQQLILAED KLVVIDFYAD WCGPCKIIAP KLDELAHEYS DRVVVLKVNV
     DENEDITVEY NVNSMPTFVF IKGGNVLELF VGCNSDKLAK LMEKHAGVYT DEAADVKAVH
     IDGECIVDLT AESSESDNDN NNVNEVSAHD ENAVLEH
 
 
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