Q42403 (TRXH3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin H3
Short name=AtTrxh3

Alternative name(s):
Thioredoxin 3
Short name=AtTRX3

Gene names

Name:	TRX3
Ordered Locus Names:	At5g42980
ORF Names:	MBD2.18

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10
Subcellular location	Cytoplasm Ref.10.
Disruption phenotype	High sensitivity to heat shock. Ref.10
Sequence similarities	Belongs to the thioredoxin family. Plant H-type subfamily. Contains 1 thioredoxin domain.
Caution	The active site contains a CPPC motif wich differs from the conserved CGPC motif.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro defense response to fungus Inferred from mutant phenotype. Source: TAIR electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro heat acclimation Inferred from mutant phenotype Ref.10. Source: UniProtKB protein folding Inferred from direct assay Ref.10. Source: UniProtKB protein oligomerization Inferred from direct assay Ref.10. Source: UniProtKB response to hydrogen peroxide Inferred from genetic interaction. Source: TAIR response to microbial phytotoxin Inferred from mutant phenotype. Source: TAIR transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay Ref.10. Source: UniProtKB mitochondrion Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR plasmodesma Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Inferred from direct assay Ref.10. Source: UniProtKB protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 118	118	Thioredoxin H3		PRO_0000120048
Regions
	Domain	2 – 113	112	Thioredoxin
Sites
	Active site	39	1	Nucleophile Potential
	Active site	42	1	Nucleophile Potential
Amino acid modifications
	Disulfide bond	39 ↔ 42		Redox-active By similarity
Experimental info
	Mutagenesis	39	1	C → S: Loss of disulfide reductase activity. Ref.10
	Mutagenesis	42	1	C → S: Loss of disulfide reductase activity. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Q42403 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7AFCE291C3EB8FE2	FASTA	118	13,109
	10 20 30 40 50 60 MAAEGEVIAC HTVEDWTEKL KAANESKKLI VIDFTATWCP PCRFIAPVFA DLAKKHLDVV 70 80 90 100 110 FFKVDVDELN TVAEEFKVQA MPTFIFMKEG EIKETVVGAA KEEIIANLEK HKTVVAAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for five divergent thioredoxin h sequences in Arabidopsis thaliana." Rivera-Madrid R., Mestres D., Marinho P., Jacquot J.-P., Decottignies P., Miginiac-Maslow M., Meyer Y. Proc. Natl. Acad. Sci. U.S.A. 92:5620-5624(1995) [PubMed: 7777559] [Abstract] 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: 8642611] [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: 9501997] [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: 14593172] [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]	"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs." Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H. Plant J. 9:101-124(1996) [PubMed: 8580968] [Abstract] 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: 14749482] [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: 19825616] [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: 19339505] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-39 AND CYS-42.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00523104.
PIR	S58118.
RefSeq	NP_199112.1. NM_123664.3.
UniGene	At.24175.
3D structure databases
ProteinModelPortal	Q42403.
SMR	Q42403. Positions 2-111.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q42403. 53 interactions.
STRING	Q42403.
Proteomic databases
PRIDE	Q42403.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G42980.1; AT5G42980.1; AT5G42980.
GeneID	834313.
GenomeReviews	Gene locus AT5G42980 in contig BA000015_GR.
KEGG	ath:AT5G42980.
NMPDR	fig|3702.1.peg.26032.
Organism-specific databases
TAIR	At5g42980.
Phylogenomic databases
GeneTree	EPGT00070000028062.
HOGENOM	HBG493509.
InParanoid	Q42403.
OMA	DVVFFKV.
PhylomeDB	Q42403.
ProtClustDB	CLSN2679888.
Gene expression databases
ArrayExpress	Q42403.
Genevestigator	Q42403.
GermOnline	AT5G42980. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR10438. Trx. 1 hit.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PIRSF	PIRSF000077. Thioredoxin. 1 hit.
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXH3_ARATH

Accession

Primary (citable) accession number: Q42403

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program