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Protein

Thioredoxin-1

Gene

TRX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.8 Publications

Miscellaneous

Present with 8579 molecules/cell in log phase SD medium.1 Publication
Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2, and one mitochondrial, TRX3.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei24Deprotonates C-terminal active site Cys1
Active sitei30Nucleophile1
Sitei31Contributes to redox potential value1
Sitei32Contributes to redox potential value1
Active sitei33Nucleophile1

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • deoxyribonucleotide biosynthetic process Source: UniProtKB-KW
  • ER to Golgi vesicle-mediated transport Source: SGD
  • glycerol ether metabolic process Source: InterPro
  • protein deglutathionylation Source: SGD
  • protein transport Source: UniProtKB-KW
  • retrograde vesicle-mediated transport, Golgi to ER Source: SGD
  • vacuole fusion, non-autophagic Source: SGD
  • vacuole inheritance Source: SGD

Keywordsi

Biological processDeoxyribonucleotide synthesis, Electron transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-46
ReactomeiR-SCE-2559580 Oxidative Stress Induced Senescence
R-SCE-3299685 Detoxification of Reactive Oxygen Species
R-SCE-499943 Interconversion of nucleotide di- and triphosphates
R-SCE-5628897 TP53 Regulates Metabolic Genes
R-SCE-5676934 Protein repair
R-SCE-844456 The NLRP3 inflammasome

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-1
Alternative name(s):
Thioredoxin I
Short name:
TR-I
Thioredoxin-2
Gene namesi
Name:TRX1
Synonyms:TRX2
Ordered Locus Names:YLR043C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR043C
SGDiS000004033 TRX1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001200442 – 103Thioredoxin-1Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 33Redox-activePROSITE-ProRule annotation1 Publication
Cross-linki54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki66Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

Reversible disulfide bond formation between Cys-30 and Cys-33, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.

Keywords - PTMi

Disulfide bond, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP22217
PaxDbiP22217
PRIDEiP22217
TopDownProteomicsiP22217

PTM databases

iPTMnetiP22217

Interactioni

Subunit structurei

Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. Most of the thioredoxin of yeast is in this complex rather than the well-studied monomer. LMA1 binds to the ATPase SEC18.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDIT4LQ96D033EBI-19607,EBI-742054From Homo sapiens.

Protein-protein interaction databases

BioGridi31318, 58 interactors
IntActiP22217, 19 interactors
MINTiP22217
STRINGi4932.YLR043C

Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi8 – 15Combined sources8
Beta strandi17 – 19Combined sources3
Beta strandi21 – 26Combined sources6
Helixi31 – 46Combined sources16
Beta strandi50 – 56Combined sources7
Turni57 – 59Combined sources3
Helixi61 – 66Combined sources6
Beta strandi71 – 79Combined sources9
Beta strandi82 – 90Combined sources9
Helixi92 – 102Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I9HNMR-A1-103[»]
2N5ANMR-A1-103[»]
2N5BNMR-A1-103[»]
3F3QX-ray1.76A1-103[»]
3F3RX-ray1.80A/B1-103[»]
ProteinModelPortaliP22217
SMRiP22217
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22217

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 103ThioredoxinPROSITE-ProRule annotationAdd BLAST102

Sequence similaritiesi

Belongs to the thioredoxin family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00530000063008
HOGENOMiHOG000292977
InParanoidiP22217
KOiK03671
OMAiDANQEFA
OrthoDBiEOG092C4AE3

Family and domain databases

InterProiView protein in InterPro
IPR005746 Thioredoxin
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain
PANTHERiPTHR10438 PTHR10438, 1 hit
PfamiView protein in Pfam
PF00085 Thioredoxin, 1 hit
PIRSFiPIRSF000077 Thioredoxin, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
TIGRFAMsiTIGR01068 thioredoxin, 1 hit
PROSITEiView protein in PROSITE
PS00194 THIOREDOXIN_1, 1 hit
PS51352 THIOREDOXIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTQFKTASE FDSAIAQDKL VVVDFYATWC GPCKMIAPMI EKFSEQYPQA
60 70 80 90 100
DFYKLDVDEL GDVAQKNEVS AMPTLLLFKN GKEVAKVVGA NPAAIKQAIA

ANA
Length:103
Mass (Da):11,235
Last modified:January 23, 2007 - v3
Checksum:i87A19FBBBDB20CF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59169 Genomic DNA Translation: AAA35171.1
M62647 Genomic DNA Translation: AAA35177.1
Z73215 Genomic DNA Translation: CAA97572.1
AY558203 Genomic DNA Translation: AAS56529.1
BK006945 Genomic DNA Translation: DAA09361.1
PIRiS15048 TXBY2
RefSeqiNP_013144.1, NM_001181930.1

Genome annotation databases

EnsemblFungiiYLR043C; YLR043C; YLR043C
GeneIDi850732
KEGGisce:YLR043C

Similar proteinsi

Entry informationi

Entry nameiTRX1_YEAST
AccessioniPrimary (citable) accession number: P22217
Secondary accession number(s): D6VY45
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 177 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health