PRX2E_ARATH
ID PRX2E_ARATH Reviewed; 234 AA.
AC Q949U7; Q9LF96;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Peroxiredoxin-2E, chloroplastic;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIE;
DE AltName: Full=Thioredoxin peroxidase 2E;
DE Flags: Precursor;
GN Name=PRXIIE; OrderedLocusNames=At3g52960; ORFNames=F8J2_130;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX DOI=10.1016/S0981-9428(02)01396-7;
RA Horling F., Koenig J., Dietz K.-J.;
RT "Type II peroxiredoxin C, a member of the peroxiredoxin family of
RT Arabidopsis thaliana: its expression and activity in comparison with other
RT peroxiredoxins.";
RL Plant Physiol. Biochem. 40:491-499(2002).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12913160; DOI=10.1104/pp.103.022533;
RA Brehelin C., Meyer E.H., de Souris J.-P., Bonnard G., Meyer Y.;
RT "Resemblance and dissemblance of Arabidopsis type II peroxiredoxins:
RT similar sequences for divergent gene expression, protein localization, and
RT activity.";
RL Plant Physiol. 132:2045-2057(2003).
RN [6]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
RA Rouhier N., Jacquot J.-P.;
RT "The plant multigenic family of thiol peroxidases.";
RL Free Radic. Biol. Med. 38:1413-1421(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides (By similarity). May be involved in
CC chloroplast redox homeostasis (Probable).
CC {ECO:0000250|UniProtKB:A9PCL4, ECO:0000305|PubMed:15890615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-
CC COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.25;
CC Evidence={ECO:0000250|UniProtKB:A9PCL4};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12913160}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12913160}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues but predominantly in buds,
CC siliques and seeds. {ECO:0000269|PubMed:12913160, ECO:0000269|Ref.4}.
CC -!- INDUCTION: Down-regulated by salt stress. {ECO:0000269|Ref.4}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {ECO:0000250|UniProtKB:A9PCL4}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL132969; CAB86900.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79018.1; -; Genomic_DNA.
DR EMBL; AY050880; AAK92817.1; -; mRNA.
DR EMBL; AY054638; AAK96829.1; -; mRNA.
DR EMBL; AY072493; AAL66908.1; -; mRNA.
DR EMBL; AY150397; AAN12942.1; -; mRNA.
DR PIR; PA0047; PA0047.
DR PIR; T47553; T47553.
DR RefSeq; NP_190864.1; NM_115156.3.
DR AlphaFoldDB; Q949U7; -.
DR SMR; Q949U7; -.
DR BioGRID; 9779; 4.
DR IntAct; Q949U7; 2.
DR STRING; 3702.AT3G52960.1; -.
DR PeroxiBase; 4353; AtPrxII05.
DR iPTMnet; Q949U7; -.
DR MetOSite; Q949U7; -.
DR SwissPalm; Q949U7; -.
DR PaxDb; Q949U7; -.
DR PRIDE; Q949U7; -.
DR ProteomicsDB; 226382; -.
DR EnsemblPlants; AT3G52960.1; AT3G52960.1; AT3G52960.
DR GeneID; 824462; -.
DR Gramene; AT3G52960.1; AT3G52960.1; AT3G52960.
DR KEGG; ath:AT3G52960; -.
DR Araport; AT3G52960; -.
DR TAIR; locus:2085181; AT3G52960.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_0_0_1; -.
DR InParanoid; Q949U7; -.
DR OMA; TPSCHAN; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q949U7; -.
DR BioCyc; ARA:AT3G52960-MON; -.
DR PRO; PR:Q949U7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q949U7; baseline and differential.
DR Genevisible; Q949U7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Chloroplast; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Plastid; Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..234
FT /note="Peroxiredoxin-2E, chloroplastic"
FT /id="PRO_0000282281"
FT DOMAIN 73..234
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 121
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 133
FT /note="A -> V (in Ref. 3; AAK92817)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 24684 MW; 4F66DA63CD15F003 CRC64;
MATSLSVSRF MSSSATVISV AKPLLSPTVS FTAPLSFTRS LAPNLSLKFR NRRTNSASAT
TRSFATTPVT ASISVGDKLP DSTLSYLDPS TGDVKTVTVS SLTAGKKTIL FAVPGAFTPT
CSQKHVPGFV SKAGELRSKG IDVIACISVN DAFVMEAWRK DLGINDEVML LSDGNGEFTG
KLGVELDLRD KPVGLGVRSR RYAILADDGV VKVLNLEEGG AFTNSSAEDM LKAL
