TRX3_YEAST
ID TRX3_YEAST Reviewed; 127 AA.
AC P25372; D6VR84;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Thioredoxin-3, mitochondrial;
DE Flags: Precursor;
GN Name=TRX3; OrderedLocusNames=YCR083W; ORFNames=YCR83W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10037727; DOI=10.1074/jbc.274.10.6366;
RA Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.-A.,
RA Wright A.P.H., Spyrou G.;
RT "Identification and functional characterization of a novel mitochondrial
RT thioredoxin system in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:6366-6373(1999).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2,
CC and one mitochondrial, TRX3.
CC -!- MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; X59720; CAA42258.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07553.1; -; Genomic_DNA.
DR PIR; S19498; S19498.
DR RefSeq; NP_010006.1; NM_001178789.1.
DR PDB; 2OE0; X-ray; 2.00 A; A/B=22-127.
DR PDB; 2OE1; X-ray; 2.10 A; A/B=22-127.
DR PDB; 2OE3; X-ray; 1.80 A; A/B=22-127.
DR PDB; 5YKW; X-ray; 2.08 A; A=22-127.
DR PDBsum; 2OE0; -.
DR PDBsum; 2OE1; -.
DR PDBsum; 2OE3; -.
DR PDBsum; 5YKW; -.
DR AlphaFoldDB; P25372; -.
DR SMR; P25372; -.
DR BioGRID; 31056; 83.
DR IntAct; P25372; 3.
DR STRING; 4932.YCR083W; -.
DR iPTMnet; P25372; -.
DR MaxQB; P25372; -.
DR PaxDb; P25372; -.
DR PRIDE; P25372; -.
DR EnsemblFungi; YCR083W_mRNA; YCR083W; YCR083W.
DR GeneID; 850444; -.
DR KEGG; sce:YCR083W; -.
DR SGD; S000000679; TRX3.
DR VEuPathDB; FungiDB:YCR083W; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000163988; -.
DR HOGENOM; CLU_090389_14_5_1; -.
DR InParanoid; P25372; -.
DR OMA; MFAPTYG; -.
DR BioCyc; YEAST:G3O-29379-MON; -.
DR ChiTaRS; TRX3; yeast.
DR EvolutionaryTrace; P25372; -.
DR PRO; PR:P25372; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25372; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
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 PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Mitochondrion;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..127
FT /note="Thioredoxin-3, mitochondrial"
FT /id="PRO_0000034155"
FT DOMAIN 22..127
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 49
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2OE3"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2OE3"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2OE3"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:2OE3"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:2OE3"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2OE3"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2OE3"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:2OE3"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2OE3"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2OE3"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:2OE3"
SQ SEQUENCE 127 AA; 14432 MW; B55D434B6E5DB28A CRC64;
MLFYKPVMRM AVRPLKSIRF QSSYTSITKL TNLTEFRNLI KQNDKLVIDF YATWCGPCKM
MQPHLTKLIQ AYPDVRFVKC DVDESPDIAK ECEVTAMPTF VLGKDGQLIG KIIGANPTAL
EKGIKDL
