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Protein

Thioredoxin H3

Gene

TRX3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-disulfide oxidoreductase that possesses disulfide reductase and insulin disulfide bonds reducing activities. Heat shock causes oligomerization and formation of high molecular weight (HMW) complexes with concomitant functional switching from a disulfide reductase to chaperone.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei39 – 391NucleophileSequence analysis
Active sitei42 – 421NucleophileSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: GO_Central
  • cellular response to oxidative stress Source: GO_Central
  • defense response to fungus Source: TAIR
  • glycerol ether metabolic process Source: InterPro
  • heat acclimation Source: UniProtKB
  • protein folding Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • response to cytokinin Source: TAIR
  • response to heat Source: UniProtKB
  • response to microbial phytotoxin Source: TAIR
  • sulfate assimilation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H3
Short name:
AtTrxh3
Alternative name(s):
Thioredoxin 3
Short name:
AtTRX3
Gene namesi
Name:TRX3
Ordered Locus Names:At5g42980
ORF Names:MBD2.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G42980.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: UniProtKB
  • Golgi apparatus Source: TAIR
  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

High sensitivity to heat shock.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391C → S: Loss of disulfide reductase activity. 1 Publication
Mutagenesisi42 – 421C → S: Loss of disulfide reductase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 118117Thioredoxin H3PRO_0000120048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Disulfide bondi39 ↔ 42Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiQ42403.
PRIDEiQ42403.

PTM databases

SwissPalmiQ42403.

Expressioni

Gene expression databases

GenevisibleiQ42403. AT.

Interactioni

Protein-protein interaction databases

BioGridi19563. 19 interactions.
IntActiQ42403. 50 interactions.
STRINGi3702.AT5G42980.1.

Structurei

3D structure databases

ProteinModelPortaliQ42403.
SMRiQ42403. Positions 2-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 113112ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiQ42403.
KOiK03671.
OMAiVVFFKVD.
PhylomeDBiQ42403.

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.

Q42403-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEGEVIAC HTVEDWTEKL KAANESKKLI VIDFTATWCP PCRFIAPVFA
60 70 80 90 100
DLAKKHLDVV FFKVDVDELN TVAEEFKVQA MPTFIFMKEG EIKETVVGAA
110
KEEIIANLEK HKTVVAAA
Length:118
Mass (Da):13,109
Last modified:November 1, 1996 - v1
Checksum:i7AFCE291C3EB8FE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35474 mRNA. Translation: CAA84611.1.
U35640 Genomic DNA. Translation: AAC49351.1.
AB008264 Genomic DNA. Translation: BAB09200.1.
CP002688 Genomic DNA. Translation: AED94897.1.
AY059870 mRNA. Translation: AAL24352.1.
AY065098 mRNA. Translation: AAL38274.1.
AY093318 mRNA. Translation: AAM13317.1.
AY114566 mRNA. Translation: AAM47885.1.
AY085117 mRNA. Translation: AAM61671.1.
Z35335 mRNA. Translation: CAA84560.1.
PIRiS58118.
RefSeqiNP_199112.1. NM_123664.3.
UniGeneiAt.24175.

Genome annotation databases

EnsemblPlantsiAT5G42980.1; AT5G42980.1; AT5G42980.
GeneIDi834313.
GrameneiAT5G42980.1; AT5G42980.1; AT5G42980.
KEGGiath:AT5G42980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35474 mRNA. Translation: CAA84611.1.
U35640 Genomic DNA. Translation: AAC49351.1.
AB008264 Genomic DNA. Translation: BAB09200.1.
CP002688 Genomic DNA. Translation: AED94897.1.
AY059870 mRNA. Translation: AAL24352.1.
AY065098 mRNA. Translation: AAL38274.1.
AY093318 mRNA. Translation: AAM13317.1.
AY114566 mRNA. Translation: AAM47885.1.
AY085117 mRNA. Translation: AAM61671.1.
Z35335 mRNA. Translation: CAA84560.1.
PIRiS58118.
RefSeqiNP_199112.1. NM_123664.3.
UniGeneiAt.24175.

3D structure databases

ProteinModelPortaliQ42403.
SMRiQ42403. Positions 2-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19563. 19 interactions.
IntActiQ42403. 50 interactions.
STRINGi3702.AT5G42980.1.

PTM databases

SwissPalmiQ42403.

Proteomic databases

PaxDbiQ42403.
PRIDEiQ42403.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G42980.1; AT5G42980.1; AT5G42980.
GeneIDi834313.
GrameneiAT5G42980.1; AT5G42980.1; AT5G42980.
KEGGiath:AT5G42980.

Organism-specific databases

TAIRiAT5G42980.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiQ42403.
KOiK03671.
OMAiVVFFKVD.
PhylomeDBiQ42403.

Miscellaneous databases

PROiQ42403.

Gene expression databases

GenevisibleiQ42403. AT.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Callus.
  2. "Intron position as an evolutionary marker of thioredoxins and thioredoxin domains."
    Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.
    J. Mol. Evol. 42:422-431(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-105.
    Strain: cv. Columbia.
  8. "Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana."
    Yamazaki D., Motohashi K., Kasama T., Hara Y., Hisabori T.
    Plant Cell Physiol. 45:18-27(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa."
    Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.
    Mol. Plant 2:308-322(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  10. "Heat-shock and redox-dependent functional switching of an h-type Arabidopsis thioredoxin from a disulfide reductase to a molecular chaperone."
    Park S.K., Jung Y.J., Lee J.R., Lee Y.M., Jang H.H., Lee S.S., Park J.H., Kim S.Y., Moon J.C., Lee S.Y., Chae H.B., Shin M.R., Jung J.H., Kim M.G., Kim W.Y., Yun D.J., Lee K.O., Lee S.Y.
    Plant Physiol. 150:552-561(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-39 AND CYS-42.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRXH3_ARATH
AccessioniPrimary (citable) accession number: Q42403
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The active site contains a CPPC motif wich differs from the conserved CGPC motif.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.