PRX2C_ARATH
ID PRX2C_ARATH Reviewed; 162 AA.
AC Q9SRZ4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peroxiredoxin-2C;
DE EC=1.11.1.25 {ECO:0000269|Ref.7};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIC;
DE AltName: Full=Peroxiredoxin TPx2;
DE AltName: Full=Thioredoxin peroxidase 2C;
DE AltName: Full=Thioredoxin-dependent peroxidase 2;
GN Name=PRXIIC; Synonyms=TPX2; OrderedLocusNames=At1g65970;
GN ORFNames=F12P19.13;
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 [MRNA].
RX PubMed=10391912; DOI=10.1074/jbc.274.28.19714;
RA Verdoucq L., Vignols F., Jacquot J.-P., Chartier Y., Meyer Y.;
RT "In vivo characterization of a thioredoxin H target protein defines a new
RT peroxiredoxin family.";
RL J. Biol. Chem. 274:19714-19722(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP 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 [8]
RP INDUCTION.
RX PubMed=12529539; DOI=10.1104/pp.010017;
RA Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A.,
RA Baier M., Dietz K.-J.;
RT "Divergent light-, ascorbate-, and oxidative stress-dependent regulation of
RT expression of the peroxiredoxin gene family in Arabidopsis.";
RL Plant Physiol. 131:317-325(2003).
RN [9]
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 [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).
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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {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; Evidence={ECO:0000269|Ref.7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=8.9 nmol/min/mg enzyme for H(2)O(2) {ECO:0000269|Ref.7};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in buds and flowers. Slightly
CC expressed in green tissues. Also detected in pollen.
CC {ECO:0000269|PubMed:12913160, ECO:0000269|Ref.7}.
CC -!- INDUCTION: Highly induced by salt or oxidative stresses.
CC {ECO:0000269|PubMed:12529539, ECO:0000269|Ref.7}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF121356; AAD28243.1; -; mRNA.
DR EMBL; AC009513; AAF06057.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34446.1; -; Genomic_DNA.
DR EMBL; AF332463; AAG48826.1; -; mRNA.
DR EMBL; BT003050; AAO23615.1; -; mRNA.
DR EMBL; AY084458; AAM61030.1; -; mRNA.
DR EMBL; AK227350; BAE99360.1; -; mRNA.
DR PIR; A96684; A96684.
DR RefSeq; NP_176772.1; NM_105269.4.
DR AlphaFoldDB; Q9SRZ4; -.
DR SMR; Q9SRZ4; -.
DR STRING; 3702.AT1G65970.1; -.
DR PeroxiBase; 14574; HaPNC20.
DR PeroxiBase; 4347; AtPrxII03.
DR PaxDb; Q9SRZ4; -.
DR PRIDE; Q9SRZ4; -.
DR ProteomicsDB; 226339; -.
DR EnsemblPlants; AT1G65970.1; AT1G65970.1; AT1G65970.
DR GeneID; 842909; -.
DR Gramene; AT1G65970.1; AT1G65970.1; AT1G65970.
DR KEGG; ath:AT1G65970; -.
DR Araport; AT1G65970; -.
DR TAIR; locus:2009709; AT1G65970.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_1_2_1; -.
DR InParanoid; Q9SRZ4; -.
DR OMA; GTPIHFI; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q9SRZ4; -.
DR BioCyc; ARA:AT1G65970-MON; -.
DR PRO; PR:Q9SRZ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRZ4; baseline and differential.
DR Genevisible; Q9SRZ4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:TAIR.
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; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..162
FT /note="Peroxiredoxin-2C"
FT /id="PRO_0000282280"
FT DOMAIN 4..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
SQ SEQUENCE 162 AA; 17414 MW; 7EEBEA0B56666E0A CRC64;
MAPITVGDVV PDGTISFFDE NDQLQTVSVH SIAAGKKVIL FGVPGAFTPT CSMSHVPGFI
GKAEELKSKG IDEIICFSVN DPFVMKAWGK TYPENKHVKF VADGSGEYTH LLGLELDLKD
KGLGIRSRRF ALLLDNLKVT VANVESGGEF TVSSAEDILK AL
