PRX2F_ARATH
ID PRX2F_ARATH Reviewed; 201 AA.
AC Q9M7T0; Q8LEJ1; Q8LPM1; Q941C2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peroxiredoxin-2F, mitochondrial;
DE EC=1.11.1.25 {ECO:0000269|PubMed:15632145};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIF;
DE AltName: Full=Thioredoxin peroxidase 2F;
DE Flags: Precursor;
GN Name=PRXIIF; OrderedLocusNames=At3g06050; ORFNames=F24F17.3;
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 {ECO:0000312|EMBL:AAF66133.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF66133.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAF66133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 31-37, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12492832; DOI=10.1046/j.1365-313x.2002.01474.x;
RA Sweetlove L.J., Heazlewood J.L., Herald V., Holtzapffel R., Day D.A.,
RA Leaver C.J., Millar A.H.;
RT "The impact of oxidative stress on Arabidopsis mitochondria.";
RL Plant J. 32:891-904(2002).
RN [7]
RP TISSUE SPECIFICITY.
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 [8]
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15632145; DOI=10.1074/jbc.m413189200;
RA Finkemeier I., Goodman M., Lamkemeyer P., Kandlbinder A., Sweetlove L.J.,
RA Dietz K.-J.;
RT "The mitochondrial type II peroxiredoxin F is essential for redox
RT homeostasis and root growth of Arabidopsis thaliana under stress.";
RL J. Biol. Chem. 280:12168-12180(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-149, AND
RP IDENTIFICATION BY 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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-30.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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. Reduces preferentially hydrogen peroxide
CC rather than alkyl peroxides. May be involved in mitochondrial redox
CC homeostasis. {ECO:0000269|PubMed:15632145}.
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:0000269|PubMed:15632145};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15632145}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:12492832,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15632145,
CC ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC {ECO:0000269|PubMed:12913160, ECO:0000269|Ref.7}.
CC -!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:12492832}.
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 C(P) can be reactivated by glutathione or the mitochondrial
CC glutaredoxin (Grx) or thioredoxin (Trx) systems.
CC {ECO:0000305|PubMed:15632145}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC068073; AAF66133.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74337.1; -; Genomic_DNA.
DR EMBL; AY052278; AAK96471.1; -; mRNA.
DR EMBL; AY098963; AAM19973.1; -; mRNA.
DR EMBL; AY085396; AAM62624.1; -; mRNA.
DR RefSeq; NP_566268.1; NM_111480.4.
DR AlphaFoldDB; Q9M7T0; -.
DR SMR; Q9M7T0; -.
DR BioGRID; 5113; 3.
DR STRING; 3702.AT3G06050.1; -.
DR PeroxiBase; 4354; AtPrxII06.
DR iPTMnet; Q9M7T0; -.
DR SwissPalm; Q9M7T0; -.
DR PaxDb; Q9M7T0; -.
DR PRIDE; Q9M7T0; -.
DR ProteomicsDB; 226340; -.
DR EnsemblPlants; AT3G06050.1; AT3G06050.1; AT3G06050.
DR GeneID; 819778; -.
DR Gramene; AT3G06050.1; AT3G06050.1; AT3G06050.
DR KEGG; ath:AT3G06050; -.
DR Araport; AT3G06050; -.
DR TAIR; locus:2080374; AT3G06050.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_2_1_1; -.
DR InParanoid; Q9M7T0; -.
DR OMA; VNDPYTM; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q9M7T0; -.
DR BioCyc; ARA:AT3G06050-MON; -.
DR PRO; PR:Q9M7T0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M7T0; baseline and differential.
DR Genevisible; Q9M7T0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IDA: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 GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
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; Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11743114,
FT ECO:0000269|PubMed:25732537"
FT CHAIN 31..201
FT /note="Peroxiredoxin-2F, mitochondrial"
FT /id="PRO_0000023800"
FT DOMAIN 37..201
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 89
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 16
FT /note="S -> A (in Ref. 4; AAM62624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 21445 MW; 0181FD57FF92D222 CRC64;
MAMSILKLRN LSALRSAANS ARIGVSSRGF SKLAEGTDIT SAAPGVSLQK ARSWDEGVSS
KFSTTPLSDI FKGKKVVIFG LPGAYTGVCS QQHVPSYKSH IDKFKAKGID SVICVSVNDP
FAINGWAEKL GAKDAIEFYG DFDGKFHKSL GLDKDLSAAL LGPRSERWSA YVEDGKVKAV
NVEEAPSDFK VTGAEVILGQ I
