TRX1_YEAST
ID TRX1_YEAST Reviewed; 103 AA.
AC P22217; D6VY45;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Thioredoxin-1;
DE AltName: Full=Thioredoxin I;
DE Short=TR-I;
DE AltName: Full=Thioredoxin-2;
GN Name=TRX1; Synonyms=TRX2; OrderedLocusNames=YLR043C;
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 [GENOMIC DNA].
RX PubMed=1988444; DOI=10.1016/s0021-9258(18)52350-4;
RA Gan Z.-R.;
RT "Yeast thioredoxin genes.";
RL J. Biol. Chem. 266:1692-1696(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2026619; DOI=10.1016/s0021-9258(18)31570-9;
RA Muller E.G.D.;
RT "Thioredoxin deficiency in yeast prolongs S phase and shortens the G1
RT interval of the cell cycle.";
RL J. Biol. Chem. 266:9194-9202(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1561834; DOI=10.1002/yea.320080206;
RA Muller E.G.D.;
RT "Thioredoxin genes in Saccharomyces cerevisiae: map positions of TRX1 and
RT TRX2.";
RL Yeast 8:117-120(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PROTEIN SEQUENCE OF 2-13, AND TSA1 DEPENDENCE ON THIOREDOXIN.
RC STRAIN=ATCC 200358 / YNN 295;
RX PubMed=7961686; DOI=10.1016/s0021-9258(18)47038-x;
RA Chae H.Z., Chung S.J., Rhee S.G.;
RT "Thioredoxin-dependent peroxide reductase from yeast.";
RL J. Biol. Chem. 269:27670-27678(1994).
RN [8]
RP PROTEIN SEQUENCE OF 7-19 AND 43-53, FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN A LMA1 COMPLEX.
RX PubMed=8603912; DOI=10.1083/jcb.132.5.787;
RA Xu Z., Wickner W.;
RT "Thioredoxin is required for vacuole inheritance in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 132:787-794(1996).
RN [9]
RP PROTEIN SEQUENCE OF 26-34, AND REDOX-ACTIVE DISULFIDE BOND.
RX PubMed=4945270; DOI=10.1111/j.1432-1033.1971.tb01625.x;
RA Hall D.E., Baldesten A., Holmgren A., Reichard P.;
RT "Yeast thioredoxin. Amino-acid sequence around the active-center disulfide
RT of thioredoxin I and II.";
RL Eur. J. Biochem. 23:328-335(1971).
RN [10]
RP FUNCTION, AND SULFATE ASSIMILATION AND METHIONINE METABOLISM.
RX PubMed=3060034; DOI=10.1007/bf00408300;
RA Schwenn J.D., Krone F.A., Husmann K.;
RT "Yeast PAPS reductase: properties and requirements of the purified
RT enzyme.";
RL Arch. Microbiol. 150:313-319(1988).
RN [11]
RP FUNCTION, AND LMA1 COMPLEX.
RX PubMed=9015301; DOI=10.1083/jcb.136.2.299;
RA Xu Z., Mayer A., Muller E.G.D., Wickner W.;
RT "A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to
RT promote yeast vacuole inheritance.";
RL J. Cell Biol. 136:299-306(1997).
RN [12]
RP FUNCTION, AND INTERACTION WITH SEC18.
RX PubMed=9657146; DOI=10.1016/s0092-8674(00)81457-9;
RA Xu Z., Sato K., Wickner W.;
RT "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a
RT t-SNARE (Vam3p) complex, and is released during fusion.";
RL Cell 93:1125-1134(1998).
RN [13]
RP FUNCTION, AND DOT5 AND TSA2 DEPENDENCE ON THIOREDOXIN.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [14]
RP FUNCTION, AND REDUCTION OF AHP1.
RX PubMed=9988687; DOI=10.1074/jbc.274.8.4537;
RA Lee J., Spector D., Godon C., Labarre J., Toledano M.B.;
RT "A new antioxidant with alkyl hydroperoxide defense properties in yeast.";
RL J. Biol. Chem. 274:4537-4544(1999).
RN [15]
RP FUNCTION, AND PROTECTION AGAINST REDUCING STRESS.
RX PubMed=12410842; DOI=10.1046/j.1365-2958.2002.03216.x;
RA Trotter E.W., Grant C.M.;
RT "Thioredoxins are required for protection against a reductive stress in the
RT yeast Saccharomyces cerevisiae.";
RL Mol. Microbiol. 46:869-878(2002).
RN [16]
RP FUNCTION, AND REGULATION OF HYR1/GPX3.
RX PubMed=12437921; DOI=10.1016/s0092-8674(02)01048-6;
RA Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.;
RT "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene
RT activation.";
RL Cell 111:471-481(2002).
RN [17]
RP REVIEW, AND OXIDATIVE STRESS.
RX PubMed=11018134; DOI=10.1146/annurev.micro.54.1.439;
RA Carmel-Harel O., Storz G.;
RT "Roles of the glutathione- and thioredoxin-dependent reduction systems in
RT the Escherichia coli and Saccharomyces cerevisiae responses to oxidative
RT stress.";
RL Annu. Rev. Microbiol. 54:439-461(2000).
RN [18]
RP REVIEW.
RX PubMed=11169096; DOI=10.1046/j.1365-2958.2001.02283.x;
RA Grant C.M.;
RT "Role of the glutathione/glutaredoxin and thioredoxin systems in yeast
RT growth and response to stress conditions.";
RL Mol. Microbiol. 39:533-541(2001).
RN [19]
RP REVIEW, AND VESICLE FUSION.
RX PubMed=12914955; DOI=10.1016/s0167-4889(03)00086-7;
RA Elazar Z., Scherz-Shouval R., Shorer H.;
RT "Involvement of LMA1 and GATE-16 family members in intracellular membrane
RT dynamics.";
RL Biochim. Biophys. Acta 1641:145-156(2003).
RN [20]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [21]
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).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [23]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-66 AND LYS-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [24]
RP STRUCTURE BY NMR.
RX PubMed=17932921; DOI=10.1002/prot.21693;
RA Pinheiro A.S., Amorim G.C., Netto L.E., Almeida F.C., Valente A.P.;
RT "NMR solution structure of the reduced form of thioredoxin 1 from
RT Saccharomyces cerevisiae.";
RL Proteins 70:584-587(2008).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=19362171; DOI=10.1016/j.bbapap.2009.04.001;
RA Bao R., Zhang Y., Lou X., Zhou C.Z., Chen Y.;
RT "Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin
RT Trx1: implications for the catalytic mechanism of GSSG reduced by the
RT thioredoxin system.";
RL Biochim. Biophys. Acta 1794:1218-1223(2009).
CC -!- FUNCTION: Participates as a hydrogen donor in redox reactions through
CC the reversible oxidation of its active center dithiol to a disulfide,
CC accompanied by the transfer of 2 electrons and 2 protons. It is
CC involved in many cellular processes, including deoxyribonucleotide
CC synthesis, repair of oxidatively damaged proteins, protein folding,
CC sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes
CC include phosphoadenosine-phosphosulfate reductase MET16, alkyl-
CC hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2,
CC alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin
CC is also involved in protection against reducing stress. As part of the
CC LMA1 complex, it is involved in the facilitation of vesicle fusion such
CC as homotypic vacuole and ER-derived COPII vesicle fusion with the
CC Golgi. This activity does not require the redox mechanism.
CC {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12410842,
CC ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:3060034,
CC ECO:0000269|PubMed:8603912, ECO:0000269|PubMed:9015301,
CC ECO:0000269|PubMed:9657146, ECO:0000269|PubMed:9988687}.
CC -!- SUBUNIT: Monomer. Part of the heterodimeric LMA1 complex together with
CC the proteinase inhibitor PBI2. Most of the thioredoxin of yeast is in
CC this complex rather than the well-studied monomer. LMA1 binds to the
CC ATPase SEC18. {ECO:0000269|PubMed:8603912, ECO:0000269|PubMed:9657146}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8603912}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:22984289}; Peripheral membrane
CC protein {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- PTM: Reversible disulfide bond formation between Cys-30 and Cys-33,
CC reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
CC -!- MISCELLANEOUS: Present with 8579 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2,
CC and one mitochondrial, TRX3.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; M59169; AAA35171.1; -; Genomic_DNA.
DR EMBL; M62647; AAA35177.1; -; Genomic_DNA.
DR EMBL; Z73215; CAA97572.1; -; Genomic_DNA.
DR EMBL; AY558203; AAS56529.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09361.1; -; Genomic_DNA.
DR PIR; S15048; TXBY2.
DR RefSeq; NP_013144.1; NM_001181930.1.
DR PDB; 2I9H; NMR; -; A=1-103.
DR PDB; 2N5A; NMR; -; A=1-103.
DR PDB; 2N5B; NMR; -; A=1-103.
DR PDB; 3F3Q; X-ray; 1.76 A; A=1-103.
DR PDB; 3F3R; X-ray; 1.80 A; A/B=1-103.
DR PDBsum; 2I9H; -.
DR PDBsum; 2N5A; -.
DR PDBsum; 2N5B; -.
DR PDBsum; 3F3Q; -.
DR PDBsum; 3F3R; -.
DR AlphaFoldDB; P22217; -.
DR BMRB; P22217; -.
DR SMR; P22217; -.
DR BioGRID; 31318; 80.
DR ComplexPortal; CPX-1278; LMA1 complex, TRX1 variant.
DR IntAct; P22217; 5.
DR MINT; P22217; -.
DR STRING; 4932.YLR043C; -.
DR iPTMnet; P22217; -.
DR MaxQB; P22217; -.
DR PaxDb; P22217; -.
DR PRIDE; P22217; -.
DR TopDownProteomics; P22217; -.
DR EnsemblFungi; YLR043C_mRNA; YLR043C; YLR043C.
DR GeneID; 850732; -.
DR KEGG; sce:YLR043C; -.
DR SGD; S000004033; TRX1.
DR VEuPathDB; FungiDB:YLR043C; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000156170; -.
DR HOGENOM; CLU_090389_14_0_1; -.
DR InParanoid; P22217; -.
DR OMA; KIKICKF; -.
DR BioCyc; YEAST:MON3O-46; -.
DR EvolutionaryTrace; P22217; -.
DR PRO; PR:P22217; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P22217; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120124; C:membrane fusion priming complex; IC:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:SGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:SGD.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0080058; P:protein deglutathionylation; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
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; Cytoplasm; Deoxyribonucleotide synthesis;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Golgi apparatus; Isopeptide bond; Membrane; Mitochondrion; Nucleus;
KW Protein transport; Redox-active center; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7961686"
FT CHAIN 2..103
FT /note="Thioredoxin-1"
FT /id="PRO_0000120044"
FT DOMAIN 2..103
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 30
FT /note="Nucleophile"
FT ACT_SITE 33
FT /note="Nucleophile"
FT SITE 24
FT /note="Deprotonates C-terminal active site Cys"
FT SITE 31
FT /note="Contributes to redox potential value"
FT SITE 32
FT /note="Contributes to redox potential value"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:19362171"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3F3R"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:3F3Q"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:3F3Q"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:3F3Q"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:3F3Q"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3F3Q"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3F3Q"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3F3Q"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:3F3Q"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3F3Q"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:3F3Q"
SQ SEQUENCE 103 AA; 11235 MW; 87A19FBBBDB20CF5 CRC64;
MVTQFKTASE FDSAIAQDKL VVVDFYATWC GPCKMIAPMI EKFSEQYPQA DFYKLDVDEL
GDVAQKNEVS AMPTLLLFKN GKEVAKVVGA NPAAIKQAIA ANA
