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Protein

Thioredoxin H2

Gene

TRX2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei53 – 531Deprotonates C-terminal active site CysBy similarity
Active sitei59 – 591NucleophileBy similarity
Sitei60 – 601Contributes to redox potential valueBy similarity
Sitei61 – 611Contributes to redox potential valueBy similarity
Active sitei62 – 621NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciARA:AT5G39950-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H2
Short name:
AtTrxh2
Alternative name(s):
Thioredoxin 2
Short name:
AtTRX2
Gene namesi
Name:TRX2
Ordered Locus Names:At5g39950
ORF Names:MYH19.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G39950.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133Thioredoxin H2PRO_0000120047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 62Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ38879.
PRIDEiQ38879.

Expressioni

Gene expression databases

GenevisibleiQ38879. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G39950.1.

Structurei

3D structure databases

ProteinModelPortaliQ38879.
SMRiQ38879. Positions 47-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 133128ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
InParanoidiQ38879.
KOiK03671.
OMAiLHFNEIK.
PhylomeDBiQ38879.

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.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGALSTVFG SGEDATAAGT ESEPSRVLKF SSSARWQLHF NEIKESNKLL
60 70 80 90 100
VVDFSASWCG PCRMIEPAIH AMADKFNDVD FVKLDVDELP DVAKEFNVTA
110 120 130
MPTFVLVKRG KEIERIIGAK KDELEKKVSK LRA
Length:133
Mass (Da):14,676
Last modified:November 2, 2001 - v2
Checksum:iBC034E2BCD4D3CA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71T → I in AAC49353 (PubMed:8642611).Curated
Sequence conflicti22 – 221S → SS in AAC49353 (PubMed:8642611).Curated
Sequence conflicti127 – 1271K → Q in AAC49353 (PubMed:8642611).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35475 mRNA. Translation: CAA84612.1.
U35826 Genomic DNA. Translation: AAC49353.1.
AB010077 Genomic DNA. Translation: BAB10219.1.
CP002688 Genomic DNA. Translation: AED94495.1.
AY048235 mRNA. Translation: AAK82498.1.
AY113052 mRNA. Translation: AAM47360.1.
PIRiS58123.
RefSeqiNP_198811.1. NM_123358.3.
UniGeneiAt.10806.
At.27173.
At.30316.
At.70939.

Genome annotation databases

EnsemblPlantsiAT5G39950.1; AT5G39950.1; AT5G39950.
GeneIDi833992.
GrameneiAT5G39950.1; AT5G39950.1; AT5G39950.
KEGGiath:AT5G39950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35475 mRNA. Translation: CAA84612.1.
U35826 Genomic DNA. Translation: AAC49353.1.
AB010077 Genomic DNA. Translation: BAB10219.1.
CP002688 Genomic DNA. Translation: AED94495.1.
AY048235 mRNA. Translation: AAK82498.1.
AY113052 mRNA. Translation: AAM47360.1.
PIRiS58123.
RefSeqiNP_198811.1. NM_123358.3.
UniGeneiAt.10806.
At.27173.
At.30316.
At.70939.

3D structure databases

ProteinModelPortaliQ38879.
SMRiQ38879. Positions 47-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G39950.1.

Proteomic databases

PaxDbiQ38879.
PRIDEiQ38879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G39950.1; AT5G39950.1; AT5G39950.
GeneIDi833992.
GrameneiAT5G39950.1; AT5G39950.1; AT5G39950.
KEGGiath:AT5G39950.

Organism-specific databases

TAIRiAT5G39950.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
InParanoidiQ38879.
KOiK03671.
OMAiLHFNEIK.
PhylomeDBiQ38879.

Enzyme and pathway databases

BioCyciARA:AT5G39950-MONOMER.

Miscellaneous databases

PROiQ38879.

Gene expression databases

GenevisibleiQ38879. 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.
TIGRFAMsiTIGR01068. thioredoxin. 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. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [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. "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.
  7. "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.
  8. "A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication."
    Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B.
    Proc. Natl. Acad. Sci. U.S.A. 107:3900-3905(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTRXH2_ARATH
AccessioniPrimary (citable) accession number: Q38879
Secondary accession number(s): Q39240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 2, 2001
Last modified: May 11, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.