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Peroxiredoxin-2F, mitochondrial (EC 1.11.1.15) (Peroxiredoxin IIF) (Thioredoxin peroxidase 2F)

 PRX2F_ARATH             Reviewed;         201 AA.
Q9M7T0; Q8LEJ1; Q8LPM1; Q941C2;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
25-OCT-2017, entry version 132.
RecName: Full=Peroxiredoxin-2F, mitochondrial;
EC=1.11.1.15;
AltName: Full=Peroxiredoxin IIF;
AltName: Full=Thioredoxin peroxidase 2F;
Flags: Precursor;
Name=PRXIIF; OrderedLocusNames=At3g06050; ORFNames=F24F17.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAF66133.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF66133.1}
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF66133.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305}
PROTEIN SEQUENCE OF 31-37, AND SUBCELLULAR LOCATION.
TISSUE=Leaf, and Stem;
PubMed=11743114; DOI=10.1104/pp.127.4.1694;
Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
"Proteomic approach to identify novel mitochondrial proteins in
Arabidopsis.";
Plant Physiol. 127:1694-1710(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=12492832; DOI=10.1046/j.1365-313X.2002.01474.x;
Sweetlove L.J., Heazlewood J.L., Herald V., Holtzapffel R., Day D.A.,
Leaver C.J., Millar A.H.;
"The impact of oxidative stress on Arabidopsis mitochondria.";
Plant J. 32:891-904(2002).
[7]
TISSUE SPECIFICITY.
DOI=10.1016/S0981-9428(02)01396-7;
Horling F., Koenig J., Dietz K.-J.;
"Type II peroxiredoxin C, a member of the peroxiredoxin family of
Arabidopsis thaliana: its expression and activity in comparison with
other peroxiredoxins.";
Plant Physiol. Biochem. 40:491-499(2002).
[8]
TISSUE SPECIFICITY.
PubMed=12913160; DOI=10.1104/pp.103.022533;
Brehelin C., Meyer E.H., de Souris J.-P., Bonnard G., Meyer Y.;
"Resemblance and dissemblance of Arabidopsis type II peroxiredoxins:
similar sequences for divergent gene expression, protein localization,
and activity.";
Plant Physiol. 132:2045-2057(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=14671022; DOI=10.1105/tpc.016055;
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome
highlights signaling and regulatory components, provides assessment of
targeting prediction programs, and indicates plant-specific
mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[10]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
Rouhier N., Jacquot J.-P.;
"The plant multigenic family of thiol peroxidases.";
Free Radic. Biol. Med. 38:1413-1421(2005).
[11]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15632145; DOI=10.1074/jbc.M413189200;
Finkemeier I., Goodman M., Lamkemeyer P., Kandlbinder A.,
Sweetlove L.J., Dietz K.-J.;
"The mitochondrial type II peroxiredoxin F is essential for redox
homeostasis and root growth of Arabidopsis thaliana under stress.";
J. Biol. Chem. 280:12168-12180(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-149, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE
AFTER PHE-30.
PubMed=25732537; DOI=10.1093/jxb/erv064;
Carrie C., Venne A.S., Zahedi R.P., Soll J.;
"Identification of cleavage sites and substrate proteins for two
mitochondrial intermediate peptidases in Arabidopsis thaliana.";
J. Exp. Bot. 66:2691-2708(2015).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides. Reduces preferentially
hydrogen peroxide rather than alkyl peroxides. May be involved in
mitochondrial redox homeostasis. {ECO:0000269|PubMed:15632145}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:15632145}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15632145}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:12492832,
ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15632145,
ECO:0000305|PubMed:25732537}.
-!- TISSUE SPECIFICITY: Expressed in the whole plant.
{ECO:0000269|PubMed:12913160, ECO:0000269|Ref.7}.
-!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:12492832}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. C(P) can be reactivated by
glutathione or the mitochondrial glutaredoxin (Grx) or thioredoxin
(Trx) systems. {ECO:0000305|PubMed:15632145}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF66133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC068073; AAF66133.1; ALT_INIT; Genomic_DNA.
EMBL; CP002686; AEE74337.1; -; Genomic_DNA.
EMBL; AY052278; AAK96471.1; -; mRNA.
EMBL; AY098963; AAM19973.1; -; mRNA.
EMBL; AY085396; AAM62624.1; -; mRNA.
RefSeq; NP_566268.1; NM_111480.4.
UniGene; At.20442; -.
ProteinModelPortal; Q9M7T0; -.
SMR; Q9M7T0; -.
BioGrid; 5113; 1.
MINT; MINT-8060333; -.
STRING; 3702.AT3G06050.1; -.
PeroxiBase; 4354; AtPrxII06.
iPTMnet; Q9M7T0; -.
SwissPalm; Q9M7T0; -.
PaxDb; Q9M7T0; -.
PRIDE; Q9M7T0; -.
EnsemblPlants; AT3G06050.1; AT3G06050.1; AT3G06050.
GeneID; 819778; -.
Gramene; AT3G06050.1; AT3G06050.1; AT3G06050.
KEGG; ath:AT3G06050; -.
Araport; AT3G06050; -.
TAIR; locus:2080374; AT3G06050.
eggNOG; KOG0541; Eukaryota.
eggNOG; COG0678; LUCA.
HOGENOM; HOG000255884; -.
InParanoid; Q9M7T0; -.
OMA; VNDPYTM; -.
OrthoDB; EOG09360ND6; -.
PhylomeDB; Q9M7T0; -.
BioCyc; ARA:AT3G06050-MONOMER; -.
PRO; PR:Q9M7T0; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9M7T0; baseline and differential.
Genevisible; Q9M7T0; AT.
GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IDA:TAIR.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Antioxidant; Complete proteome; Direct protein sequencing;
Mitochondrion; Oxidoreductase; Peroxidase; Phosphoprotein;
Redox-active center; Reference proteome; Stress response;
Transit peptide.
TRANSIT 1 30 Mitochondrion.
{ECO:0000269|PubMed:11743114,
ECO:0000269|PubMed:25732537}.
CHAIN 31 201 Peroxiredoxin-2F, mitochondrial.
/FTId=PRO_0000023800.
DOMAIN 37 201 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 89 89 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:A9PCL4}.
MOD_RES 37 37 Phosphothreonine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
CONFLICT 16 16 S -> A (in Ref. 4; AAM62624).
{ECO:0000305}.
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


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