Reviewed, UniProtKB/Swiss-Prot Q949U7 (PRX2E_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-2E, chloroplastic
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin IIE
    Thioredoxin reductase 2E

Gene names

Name:	PRXIIE
Ordered Locus Names:	At3g52960
ORF Names:	F8J2_130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin or glutaredoxin system. May be involved in chloroplast redox homeostasis.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Monomer. Ref.4
Subcellular location	Plastid › chloroplast stroma. Ref.4
Tissue specificity	Expressed in all tissues but predominantly in buds, siliques and seeds. Ref.4 Ref.3
Induction	Down-regulated by salt stress. Ref.3
Post-translational modification	The Cys-121-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-121 (probably Cys-SOH) rapidly reacts with Cys-146-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.
Sequence similarities	Belongs to the peroxiredoxin 2 family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from expression pattern. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	peroxiredoxin activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449344,EBI-449157

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 70	70	Chloroplast Potential
	Chain	71 – 234	164	Peroxiredoxin-2E, chloroplastic		PRO_0000282281
Regions
	Domain	73 – 234	162	Thioredoxin
Sites
	Active site	121	1	Cysteine sulfenic acid (-SOH) intermediate Potential
Amino acid modifications
	Disulfide bond	121 ↔ 146		Redox-active
Experimental info
	Sequence conflict	133	1	A → V in AAK92817. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q949U7-1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 4F66DA63CD15F003	FASTA	234	24,684
	10 20 30 40 50 60 MATSLSVSRF MSSSATVISV AKPLLSPTVS FTAPLSFTRS LAPNLSLKFR NRRTNSASAT 70 80 90 100 110 120 TRSFATTPVT ASISVGDKLP DSTLSYLDPS TGDVKTVTVS SLTAGKKTIL FAVPGAFTPT 130 140 150 160 170 180 CSQKHVPGFV SKAGELRSKG IDVIACISVN DAFVMEAWRK DLGINDEVML LSDGNGEFTG 190 200 210 220 230 KLGVELDLRD KPVGLGVRSR RYAILADDGV VKVLNLEEGG AFTNSSAEDM LKAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins." Horling F., Koenig J., Dietz K.-J. Plant Physiol. Biochem. 40:491-499(2002) Cited for: TISSUE SPECIFICITY, INDUCTION.
[4]	"Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity." Brehelin C., Meyer E.H., de Souris J.-P., Bonnard G., Meyer Y. Plant Physiol. 132:2045-2057(2003) [PubMed: 12913160] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"The plant multigenic family of thiol peroxidases." Rouhier N., Jacquot J.-P. Free Radic. Biol. Med. 38:1413-1421(2005) [PubMed: 15890615] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL132969 Genomic DNA. Translation: CAB86900.1. AY050880 mRNA. Translation: AAK92817.1. AY054638 mRNA. Translation: AAK96829.1. AY072493 mRNA. Translation: AAL66908.1. AY150397 mRNA. Translation: AAN12942.1.
IPI	IPI00533612.
PIR	PA0047. T47553.
RefSeq	NP_190864.1.
UniGene	At.9858
3D structure databases
HSSP	HSSP built from PDB template 1HD2 based on UniProtKB P30044.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q949U7. 1 interaction.
Protein family/group databases
PeroxiBase	4353. AtPrxIIE.
Proteomic databases
PRIDE	Q949U7.
ProMEX	Q949U7.
Genome annotation databases
GeneID	824462.
GenomeReviews	Gene locus AT3G52960 in contig BA000014_GR.
KEGG	ath:AT3G52960.
NMPDR	fig|3702.1.peg.16571.
Organism-specific databases
TAIR	At3g52960.
Phylogenomic databases
OMA	Q949U7. NSSAEDM.
Enzyme and pathway databases
BRENDA	1.11.1.15. 302.
Family and domain databases
InterPro	IPR013740. Redoxin. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF08534. Redoxin. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRX2E_ARATH

Accession

Primary (citable) accession number: Q949U7
Secondary accession number(s): Q9LF96

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)