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Protein

Thioredoxin H4

Gene

TRX4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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
Active sitei40 – 401NucleophileSequence analysis
Active sitei43 – 431NucleophileSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H4
Short name:
AtTrxh4
Alternative name(s):
Thioredoxin 4
Short name:
AtTRX4
Gene namesi
Name:TRX4
Ordered Locus Names:At1g19730
ORF Names:F14P1.32, F6F9.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G19730.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119Thioredoxin H4PRO_0000120049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 43Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ39239.
PRIDEiQ39239.

PTM databases

SwissPalmiQ39239.

Expressioni

Gene expression databases

GenevisibleiQ39239. AT.

Interactioni

Protein-protein interaction databases

BioGridi23801. 1 interaction.
STRINGi3702.AT1G19730.1.

Structurei

3D structure databases

ProteinModelPortaliQ39239.
SMRiQ39239. Positions 3-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 115114ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiQ39239.
KOiK03671.
OMAiEFGVEAM.
PhylomeDBiQ39239.

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.

Q39239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEEGQVIG CHTNDVWTVQ LDKAKESNKL IVIDFTASWC PPCRMIAPIF
60 70 80 90 100
NDLAKKFMSS AIFFKVDVDE LQSVAKEFGV EAMPTFVFIK AGEVVDKLVG
110
ANKEDLQAKI VKHTGVTTA
Length:119
Mass (Da):13,063
Last modified:June 20, 2002 - v2
Checksum:iE2A37655F889FB24
GO

Sequence cautioni

The sequence CAA84610.1 differs from that shown. Reason: Frameshift at position 119. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101G → S in AAM67018 (Ref. 6) Curated
Sequence conflicti119 – 1191A → VVNQFEA in CAA84610 (PubMed:7777559).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35473 mRNA. Translation: CAA84610.1. Frameshift.
AC007797 Genomic DNA. Translation: AAG12565.1.
AC024609 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE29892.1.
AK118542 mRNA. Translation: BAC43145.1.
BT004710 mRNA. Translation: AAO42956.1.
AY088698 mRNA. Translation: AAM67018.1.
U35828 Genomic DNA. Translation: AAC49355.1.
PIRiD86330.
S58119.
RefSeqiNP_173403.1. NM_101829.3.
UniGeneiAt.194.
At.74168.

Genome annotation databases

EnsemblPlantsiAT1G19730.1; AT1G19730.1; AT1G19730.
GeneIDi838562.
GrameneiAT1G19730.1; AT1G19730.1; AT1G19730.
KEGGiath:AT1G19730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35473 mRNA. Translation: CAA84610.1. Frameshift.
AC007797 Genomic DNA. Translation: AAG12565.1.
AC024609 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE29892.1.
AK118542 mRNA. Translation: BAC43145.1.
BT004710 mRNA. Translation: AAO42956.1.
AY088698 mRNA. Translation: AAM67018.1.
U35828 Genomic DNA. Translation: AAC49355.1.
PIRiD86330.
S58119.
RefSeqiNP_173403.1. NM_101829.3.
UniGeneiAt.194.
At.74168.

3D structure databases

ProteinModelPortaliQ39239.
SMRiQ39239. Positions 3-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23801. 1 interaction.
STRINGi3702.AT1G19730.1.

PTM databases

SwissPalmiQ39239.

Proteomic databases

PaxDbiQ39239.
PRIDEiQ39239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G19730.1; AT1G19730.1; AT1G19730.
GeneIDi838562.
GrameneiAT1G19730.1; AT1G19730.1; AT1G19730.
KEGGiath:AT1G19730.

Organism-specific databases

TAIRiAT1G19730.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiQ39239.
KOiK03671.
OMAiEFGVEAM.
PhylomeDBiQ39239.

Miscellaneous databases

PROiQ39239.

Gene expression databases

GenevisibleiQ39239. 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: Flower bud.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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. "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] OF 1-110.
    Strain: cv. Landsberg erecta.
  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.

Entry informationi

Entry nameiTRXH4_ARATH
AccessioniPrimary (citable) accession number: Q39239
Secondary accession number(s): Q38880
, Q541W4, Q8L907, Q9FXH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 20, 2002
Last modified: February 17, 2016
This is version 125 of the entry and version 2 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.