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Protein

Thioredoxin H1

Gene

TRXH

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-disulfide oxidoreductase involved in the redox regulation of MAP kinases. Under reducing conditions, inhibits MPK1 and MPK5 kinase activities. Mediates its own transport from cell-to-cell through plasmodesmata. Possesses insulin disulfide bonds reducing activity.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei34Deprotonates C-terminal active site CysBy similarity1
Active sitei40NucleophileBy similarity1
Sitei41Contributes to redox potential valueBy similarity1
Sitei42Contributes to redox potential valueBy similarity1
Active sitei43NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: GO_Central
  • cellular response to oxidative stress Source: GO_Central
  • glycerol ether metabolic process Source: InterPro
  • negative regulation of catalytic activity Source: UniProtKB
  • plasmodesmata-mediated intercellular transport Source: UniProtKB
  • protein folding Source: GO_Central
  • response to cold Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
  • sulfate assimilation Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H1
Short name:
OsTrxh1
Alternative name(s):
Phloem sap 13 kDa protein 1
Gene namesi
Name:TRXH
Synonyms:RPP13-1
Ordered Locus Names:Os07g0186000, LOC_Os07g08840
ORF Names:OJ1339_B08.1, OsJ_022432, P0506C07.2
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 5Missing : Loss of cell-to-cell movement. 1 Publication5
Mutagenesisi4 – 5EE → AA: Reduces the efficiency of cell-to-cell movement. 1 Publication2
Mutagenesisi14 – 16KDE → AAA: Reduces the efficiency of cell-to-cell movement. 1 Publication3
Mutagenesisi25 – 26KE → AA: Reduces the efficiency of cell-to-cell movement. 1 Publication2
Mutagenesisi55 – 56KK → AA: Reduces the efficiency of cell-to-cell movement. 1 Publication2
Mutagenesisi71 – 72KE → AA: Reduces the efficiency of cell-to-cell movement. 1 Publication2
Mutagenesisi95 – 96DK → AA: Reduces the efficiency of cell-to-cell movement. 1 Publication2
Mutagenesisi101 – 104RKDD → AAAA: Almost loss of cell-to-cell movement. 1 Publication4
Mutagenesisi116 – 122Missing : Reduces the efficiency of cell-to-cell movement. 1 Publication7

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001200571 – 122Thioredoxin H1Add BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 43Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ0D840.
PRIDEiQ0D840.

Expressioni

Tissue specificityi

Expressed in the phloem companion cells of leaf sheaths and stems.2 Publications

Inductioni

By methyl viologen and chilling in roots and shoots.2 Publications

Gene expression databases

GenevisibleiQ0D840. OS.

Interactioni

Protein-protein interaction databases

STRINGi39947.LOC_Os07g08840.1.

Structurei

Secondary structure

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Beta strandi12 – 14Combined sources3
Helixi15 – 25Combined sources11
Turni26 – 28Combined sources3
Beta strandi32 – 34Combined sources3
Beta strandi37 – 39Combined sources3
Beta strandi43 – 46Combined sources4
Helixi47 – 56Combined sources10
Turni67 – 69Combined sources3
Helixi71 – 73Combined sources3
Helixi74 – 77Combined sources4
Turni89 – 92Combined sources4
Turni102 – 104Combined sources3
Helixi105 – 112Combined sources8
Beta strandi114 – 116Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WMJNMR-A1-122[»]
ProteinModelPortaliQ0D840.
SMRiQ0D840.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0D840.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 118ThioredoxinPROSITE-ProRule annotationAdd BLAST117

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
InParanoidiQ0D840.
KOiK03671.
OMAiITIRYNV.
OrthoDBiEOG09360XJ5.

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

Sequencei

Sequence statusi: Complete.

Q0D840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEEGVVIA CHNKDEFDAQ MTKAKEAGKV VIIDFTASWC GPCRFIAPVF
60 70 80 90 100
AEYAKKFPGA VFLKVDVDEL KEVAEKYNVE AMPTFLFIKD GAEADKVVGA
110 120
RKDDLQNTIV KHVGATAASA SA
Length:122
Mass (Da):13,156
Last modified:October 17, 2006 - v1
Checksum:iE595C3FDC0EE229E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26547 Genomic DNA. Translation: BAA05546.1.
D21836 mRNA. Translation: BAA04864.1.
AP003753 Genomic DNA. Translation: BAD30186.1.
AP004384 Genomic DNA. Translation: BAC79928.1.
AP008213 Genomic DNA. Translation: BAF20983.1.
AP014963 Genomic DNA. Translation: BAT00373.1.
CM000144 Genomic DNA. Translation: EAZ38949.1.
AK059196 mRNA. Translation: BAG86917.1.
AK121423 mRNA. Translation: BAH00481.1.
PIRiT04090.
RefSeqiXP_015647572.1. XM_015792086.1.
UniGeneiOs.39054.

Genome annotation databases

EnsemblPlantsiOS07T0186000-02; OS07T0186000-02; OS07G0186000.
GeneIDi4342593.
GrameneiOS07T0186000-02; OS07T0186000-02; OS07G0186000.
KEGGiosa:4342593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26547 Genomic DNA. Translation: BAA05546.1.
D21836 mRNA. Translation: BAA04864.1.
AP003753 Genomic DNA. Translation: BAD30186.1.
AP004384 Genomic DNA. Translation: BAC79928.1.
AP008213 Genomic DNA. Translation: BAF20983.1.
AP014963 Genomic DNA. Translation: BAT00373.1.
CM000144 Genomic DNA. Translation: EAZ38949.1.
AK059196 mRNA. Translation: BAG86917.1.
AK121423 mRNA. Translation: BAH00481.1.
PIRiT04090.
RefSeqiXP_015647572.1. XM_015792086.1.
UniGeneiOs.39054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WMJNMR-A1-122[»]
ProteinModelPortaliQ0D840.
SMRiQ0D840.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os07g08840.1.

Proteomic databases

PaxDbiQ0D840.
PRIDEiQ0D840.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOS07T0186000-02; OS07T0186000-02; OS07G0186000.
GeneIDi4342593.
GrameneiOS07T0186000-02; OS07T0186000-02; OS07G0186000.
KEGGiosa:4342593.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
InParanoidiQ0D840.
KOiK03671.
OMAiITIRYNV.
OrthoDBiEOG09360XJ5.

Miscellaneous databases

EvolutionaryTraceiQ0D840.

Gene expression databases

GenevisibleiQ0D840. OS.

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

Entry informationi

Entry nameiTRXH1_ORYSJ
AccessioniPrimary (citable) accession number: Q0D840
Secondary accession number(s): A0A0P0X3K2
, B7E3H0, O04743, Q42443, Q7EZX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  3. 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.