Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin-1

Gene

TRX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei24 – 241Deprotonates C-terminal active site Cys
Active sitei30 – 301Nucleophile
Sitei31 – 311Contributes to redox potential value
Sitei32 – 321Contributes to redox potential value
Active sitei33 – 331Nucleophile

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 folding Source: GO_Central
  • protein transport Source: UniProtKB-KW
  • retrograde vesicle-mediated transport, Golgi to ER Source: SGD
  • sulfate assimilation Source: GO_Central
  • vacuole fusion, non-autophagic Source: SGD
  • vacuole inheritance Source: SGD
Complete GO annotation...

Keywords - Biological processi

Deoxyribonucleotide synthesis, Electron transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32200-MONOMER.
ReactomeiR-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-499943. Synthesis and 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

GO - Cellular componenti

  • cytosol Source: SGD
  • fungal-type vacuole Source: SGD
  • Golgi membrane Source: UniProtKB-SubCell
  • mitochondrial intermembrane space Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 103102Thioredoxin-1PRO_0000120044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 33Redox-activePROSITE-ProRule annotation1 Publication
Cross-linki54 – 54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki66 – 66Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki96 – 96Glycyl 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.
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

Protein-protein interaction databases

BioGridi31318. 41 interactions.
IntActiP22217. 4 interactions.
MINTiMINT-2786449.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi8 – 158Combined sources
Beta strandi17 – 193Combined sources
Beta strandi21 – 266Combined sources
Helixi31 – 4616Combined sources
Beta strandi50 – 567Combined sources
Turni57 – 593Combined sources
Helixi61 – 666Combined sources
Beta strandi71 – 799Combined sources
Beta strandi82 – 909Combined sources
Helixi92 – 10211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I9HNMR-A1-103[»]
2N5ANMR-A1-103[»]
2N5BNMR-A1-103[»]
3F3QX-ray1.76A1-103[»]
3F3RX-ray1.80A/B1-103[»]
ProteinModelPortaliP22217.
SMRiP22217. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 103102ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
InParanoidiP22217.
KOiK03671.
OMAiVHTADQI.
OrthoDBiEOG092C4AE3.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I9HNMR-A1-103[»]
2N5ANMR-A1-103[»]
2N5BNMR-A1-103[»]
3F3QX-ray1.76A1-103[»]
3F3RX-ray1.80A/B1-103[»]
ProteinModelPortaliP22217.
SMRiP22217. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31318. 41 interactions.
IntActiP22217. 4 interactions.
MINTiMINT-2786449.

PTM databases

iPTMnetiP22217.

Proteomic databases

MaxQBiP22217.
TopDownProteomicsiP22217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR043C; YLR043C; YLR043C.
GeneIDi850732.
KEGGisce:YLR043C.

Organism-specific databases

EuPathDBiFungiDB:YLR043C.
SGDiS000004033. TRX1.

Phylogenomic databases

GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
InParanoidiP22217.
KOiK03671.
OMAiVHTADQI.
OrthoDBiEOG092C4AE3.

Enzyme and pathway databases

BioCyciYEAST:G3O-32200-MONOMER.
ReactomeiR-SCE-2559580. Oxidative Stress Induced Senescence.
R-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-SCE-5628897. TP53 Regulates Metabolic Genes.
R-SCE-5676934. Protein repair.
R-SCE-844456. The NLRP3 inflammasome.

Miscellaneous databases

EvolutionaryTraceiP22217.
PROiP22217.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRX1_YEAST
AccessioniPrimary (citable) accession number: P22217
Secondary accession number(s): D6VY45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.