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Protein

Thioredoxin H5

Gene

TRX5

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 involved in response to pathogens and oxidative stresses. Required for the response to victorin, a phytotoxin which induces programmed cell death in sensitive plants. Possesses insulin disulfide bonds reducing activity.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
  • protein folding Source: GO_Central
  • response to cadmium ion Source: TAIR
  • response to microbial phytotoxin Source: TAIR
  • response to oxidative stress Source: TAIR
  • sulfate assimilation Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H5
Short name:
AtTrxh5
Alternative name(s):
Protein LOCUS OF INSENSITIVITY TO VICTORIN 1
Thioredoxin 5
Short name:
AtTRX5
Gene namesi
Name:TRX5
Synonyms:LIV1
Ordered Locus Names:At1g45145
ORF Names:F27F5.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G45145.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Insensitivity to victorin phytotoxin.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391C → S: Loss of sensitivity to victorin phytotoxin. 1 Publication
Mutagenesisi42 – 421C → S: No effect on sensitivity to victorin phytotoxin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 118117Thioredoxin H5PRO_0000120050Add
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

PaxDbiQ39241.
PRIDEiQ39241.

PTM databases

SwissPalmiQ39241.

Expressioni

Inductioni

By treatment with salicylic acid (SA), abscisic acid (ABA), iron, copper and UV-C. Induced by wounding, oxidative stress, infection with incompatible P.syringae and treatment with the fungal phytotoxin victorin.2 Publications

Gene expression databases

GenevisibleiQ39241. AT.

Interactioni

Protein-protein interaction databases

BioGridi26307. 76 interactions.
IntActiQ39241. 3 interactions.
STRINGi3702.AT1G45145.1.

Structurei

3D structure databases

ProteinModelPortaliQ39241.
SMRiQ39241. Positions 4-111.
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.
InParanoidiQ39241.
KOiK03671.
OMAiGREHARV.
PhylomeDBiQ39241.

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.

Q39241-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGEGEVIAC HTLEVWNEKV KDANESKKLI VIDFTASWCP PCRFIAPVFA
60 70 80 90 100
EMAKKFTNVV FFKIDVDELQ AVAQEFKVEA MPTFVFMKEG NIIDRVVGAA
110
KDEINEKLMK HGGLVASA
Length:118
Mass (Da):13,122
Last modified:November 1, 1996 - v1
Checksum:i164FA8CDA98FC862
GO

Sequence cautioni

The sequence AAF69169.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181A → AL in AAC49356 (PubMed:8642611).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35476 mRNA. Translation: CAA84613.1.
U35829 Genomic DNA. Translation: AAC49356.1.
AC007915 Genomic DNA. Translation: AAF69169.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32083.1.
AK118035 mRNA. Translation: BAC42666.1.
AF360227 mRNA. Translation: AAK25937.1.
AY040028 mRNA. Translation: AAK64086.1.
AK221784 mRNA. Translation: BAD93909.1.
AY087159 mRNA. Translation: AAM64717.1.
PIRiG96509.
S58120.
RefSeqiNP_175128.1. NM_103588.4.
UniGeneiAt.22939.

Genome annotation databases

EnsemblPlantsiAT1G45145.1; AT1G45145.1; AT1G45145.
GeneIDi841082.
GrameneiAT1G45145.1; AT1G45145.1; AT1G45145.
KEGGiath:AT1G45145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35476 mRNA. Translation: CAA84613.1.
U35829 Genomic DNA. Translation: AAC49356.1.
AC007915 Genomic DNA. Translation: AAF69169.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32083.1.
AK118035 mRNA. Translation: BAC42666.1.
AF360227 mRNA. Translation: AAK25937.1.
AY040028 mRNA. Translation: AAK64086.1.
AK221784 mRNA. Translation: BAD93909.1.
AY087159 mRNA. Translation: AAM64717.1.
PIRiG96509.
S58120.
RefSeqiNP_175128.1. NM_103588.4.
UniGeneiAt.22939.

3D structure databases

ProteinModelPortaliQ39241.
SMRiQ39241. Positions 4-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26307. 76 interactions.
IntActiQ39241. 3 interactions.
STRINGi3702.AT1G45145.1.

PTM databases

SwissPalmiQ39241.

Proteomic databases

PaxDbiQ39241.
PRIDEiQ39241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G45145.1; AT1G45145.1; AT1G45145.
GeneIDi841082.
GrameneiAT1G45145.1; AT1G45145.1; AT1G45145.
KEGGiath:AT1G45145.

Organism-specific databases

TAIRiAT1G45145.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiQ39241.
KOiK03671.
OMAiGREHARV.
PhylomeDBiQ39241.

Miscellaneous databases

PROiQ39241.

Gene expression databases

GenevisibleiQ39241. 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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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.
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "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].
  9. "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.
  10. "The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor."
    Laloi C., Mestres-Ortega D., Marco Y., Meyer Y., Reichheld J.P.
    Plant Physiol. 134:1006-1016(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-LRR gene in Arabidopsis."
    Sweat T.A., Wolpert T.J.
    Plant Cell 19:673-687(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-39 AND CYS-42.
  12. "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.
  13. "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 nameiTRXH5_ARATH
AccessioniPrimary (citable) accession number: Q39241
Secondary accession number(s): Q38881, Q56X92, Q9MAJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 131 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.