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Protein

Thioredoxin-3, mitochondrial

Gene

TRX3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei49 – 491Deprotonates C-terminal active site CysBy similarity
Active sitei55 – 551NucleophileBy similarity
Sitei56 – 561Contributes to redox potential valueBy similarity
Sitei57 – 571Contributes to redox potential valueBy similarity
Active sitei58 – 581NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: SGD
  • glycerol ether metabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29379-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-3, mitochondrial
Gene namesi
Name:TRX3
Ordered Locus Names:YCR083W
ORF Names:YCR83W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR083W.
SGDiS000000679. TRX3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121MitochondrionSequence analysisAdd
BLAST
Chaini22 – 127106Thioredoxin-3, mitochondrialPRO_0000034155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP25372.
PeptideAtlasiP25372.

Interactioni

Protein-protein interaction databases

BioGridi31056. 32 interactions.
IntActiP25372. 3 interactions.
MINTiMINT-4478665.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi33 – 4210Combined sources
Beta strandi44 – 518Combined sources
Helixi56 – 605Combined sources
Helixi62 – 7110Combined sources
Beta strandi75 – 817Combined sources
Turni82 – 843Combined sources
Helixi86 – 916Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi107 – 1159Combined sources
Helixi117 – 1259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OE0X-ray2.00A/B22-127[»]
2OE1X-ray2.10A/B22-127[»]
2OE3X-ray1.80A/B22-127[»]
ProteinModelPortaliP25372.
SMRiP25372. Positions 22-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25372.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 127106ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
InParanoidiP25372.
KOiK03671.
OMAiIAKECEV.
OrthoDBiEOG71CFZN.

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]
SUPFAMiSSF52833. SSF52833. 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.

P25372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFYKPVMRM AVRPLKSIRF QSSYTSITKL TNLTEFRNLI KQNDKLVIDF
60 70 80 90 100
YATWCGPCKM MQPHLTKLIQ AYPDVRFVKC DVDESPDIAK ECEVTAMPTF
110 120
VLGKDGQLIG KIIGANPTAL EKGIKDL
Length:127
Mass (Da):14,432
Last modified:May 1, 1992 - v1
Checksum:iB55D434B6E5DB28A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42258.1.
BK006937 Genomic DNA. Translation: DAA07553.1.
PIRiS19498.
RefSeqiNP_010006.1. NM_001178789.1.

Genome annotation databases

EnsemblFungiiCAA42258; CAA42258; CAA42258.
YCR083W; YCR083W; YCR083W.
GeneIDi850444.
KEGGisce:YCR083W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42258.1.
BK006937 Genomic DNA. Translation: DAA07553.1.
PIRiS19498.
RefSeqiNP_010006.1. NM_001178789.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OE0X-ray2.00A/B22-127[»]
2OE1X-ray2.10A/B22-127[»]
2OE3X-ray1.80A/B22-127[»]
ProteinModelPortaliP25372.
SMRiP25372. Positions 22-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31056. 32 interactions.
IntActiP25372. 3 interactions.
MINTiMINT-4478665.

Proteomic databases

MaxQBiP25372.
PeptideAtlasiP25372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42258; CAA42258; CAA42258.
YCR083W; YCR083W; YCR083W.
GeneIDi850444.
KEGGisce:YCR083W.

Organism-specific databases

EuPathDBiFungiDB:YCR083W.
SGDiS000000679. TRX3.

Phylogenomic databases

GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
InParanoidiP25372.
KOiK03671.
OMAiIAKECEV.
OrthoDBiEOG71CFZN.

Enzyme and pathway databases

BioCyciYEAST:G3O-29379-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25372.
NextBioi966054.
PROiP25372.

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]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae."
    Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.-A., Wright A.P.H., Spyrou G.
    J. Biol. Chem. 274:6366-6373(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRX3_YEAST
AccessioniPrimary (citable) accession number: P25372
Secondary accession number(s): D6VR84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2, and one mitochondrial, TRX3.
Present with 1010 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.