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Protein

Thioredoxin-2

Gene

TRX2

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. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.9 Publications

Miscellaneous

Present with 17237 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
Sitei25Deprotonates C-terminal active site Cys1
Active sitei31Nucleophile1
Sitei32Contributes to redox potential value1
Sitei33Contributes to redox potential value1
Active sitei34Nucleophile1

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: GO_Central
  • deoxyribonucleotide biosynthetic process Source: UniProtKB-KW
  • ER to Golgi vesicle-mediated transport Source: SGD
  • glutathione metabolic process 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
  • sulfate assimilation 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-68
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-2
Alternative name(s):
Thioredoxin II
Short name:
TR-II
Thioredoxin-1
Gene namesi
Name:TRX2
Synonyms:TRX1
Ordered Locus Names:YGR209C
ORF Names:G7746
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR209C
SGDiS000003441 TRX2

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, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001200452 – 104Thioredoxin-2Add BLAST103

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 34Redox-activePROSITE-ProRule annotation1 Publication
Modified residuei62PhosphoserineCombined sources1
Cross-linki67Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

Reversible disulfide bond formation between Cys-31 and Cys-34, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP22803
PaxDbiP22803
PRIDEiP22803
TopDownProteomicsiP22803

PTM databases

CarbonylDBiP22803
iPTMnetiP22803

Expressioni

Inductioni

Strongly induced by hydrogen peroxide and diamide stress in a YAP1- and SKN7-dependent manner. Also induced by reducing stress by DTT.

Interactioni

Subunit structurei

Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. LMA1 binds to the ATPase SEC18.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi33462, 164 interactors
DIPiDIP-5552N
IntActiP22803, 26 interactors
MINTiP22803
STRINGi4932.YGR209C

Structurei

Secondary structure

1104
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi8 – 15Combined sources8
Beta strandi19 – 27Combined sources9
Helixi32 – 47Combined sources16
Beta strandi51 – 57Combined sources7
Turni58 – 60Combined sources3
Helixi62 – 67Combined sources6
Beta strandi72 – 80Combined sources9
Beta strandi83 – 91Combined sources9
Helixi93 – 101Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FA4X-ray2.38A/B1-104[»]
2HSYNMR-A1-104[»]
3PINX-ray2.70A1-104[»]
4DSSX-ray2.10B1-104[»]
ProteinModelPortaliP22803
SMRiP22803
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22803

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 104ThioredoxinPROSITE-ProRule annotationAdd BLAST103

Sequence similaritiesi

Belongs to the thioredoxin family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00530000063008
HOGENOMiHOG000292977
InParanoidiP22803
KOiK03671
OMAiKIKICKF
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.

P22803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTQLKSASE YDSALASGDK LVVVDFFATW CGPCKMIAPM IEKFAEQYSD
60 70 80 90 100
AAFYKLDVDE VSDVAQKAEV SSMPTLIFYK GGKEVTRVVG ANPAAIKQAI

ASNV
Length:104
Mass (Da):11,204
Last modified:January 23, 2007 - v3
Checksum:i071503762C90D451
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59168 Genomic DNA Translation: AAA35170.1
M62648 Genomic DNA Translation: AAA35178.1
U40843 Genomic DNA Translation: AAA85584.1
Z49133 Genomic DNA Translation: CAA89002.1
Z72994 Genomic DNA Translation: CAA97236.1
AY557817 Genomic DNA Translation: AAS56143.1
BK006941 Genomic DNA Translation: DAA08303.1
PIRiS15049 TXBY1
RefSeqiNP_011725.3, NM_001181338.3

Genome annotation databases

EnsemblFungiiYGR209C; YGR209C; YGR209C
GeneIDi853123
KEGGisce:YGR209C

Similar proteinsi

Entry informationi

Entry nameiTRX2_YEAST
AccessioniPrimary (citable) accession number: P22803
Secondary accession number(s): D6VUZ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 186 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