PRX2D_ARATH
ID PRX2D_ARATH Reviewed; 162 AA.
AC O22711; Q67ZB5; Q8LDV2; Q9XEX3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxiredoxin-2D;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IID;
DE AltName: Full=Thioredoxin peroxidase 2D;
GN Name=PRXIID; OrderedLocusNames=At1g60740; ORFNames=F8A5.25;
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=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 [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].
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 [4]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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).
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 intracellular redox signaling (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:0000250|UniProtKB:A9PCL4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12913160}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in buds and flowers. Also
CC detected in pollen. {ECO:0000269|PubMed:12913160}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB71961.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002292; AAB71961.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33727.1; -; Genomic_DNA.
DR EMBL; AY085779; AAM62996.1; -; mRNA.
DR EMBL; AK176203; BAD43966.1; -; mRNA.
DR PIR; G96632; G96632.
DR RefSeq; NP_564763.1; NM_104757.4.
DR AlphaFoldDB; O22711; -.
DR SMR; O22711; -.
DR STRING; 3702.AT1G60740.1; -.
DR PeroxiBase; 4355; AtPrxII04.
DR PaxDb; O22711; -.
DR PRIDE; O22711; -.
DR ProteomicsDB; 226297; -.
DR EnsemblPlants; AT1G60740.1; AT1G60740.1; AT1G60740.
DR GeneID; 842368; -.
DR Gramene; AT1G60740.1; AT1G60740.1; AT1G60740.
DR KEGG; ath:AT1G60740; -.
DR Araport; AT1G60740; -.
DR TAIR; locus:2036531; AT1G60740.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_1_2_1; -.
DR InParanoid; O22711; -.
DR OMA; HVPEYIQ; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; O22711; -.
DR BioCyc; ARA:AT1G60740-MON; -.
DR PRO; PR:O22711; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22711; baseline and differential.
DR Genevisible; O22711; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; 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 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..162
FT /note="Peroxiredoxin-2D"
FT /id="PRO_0000056611"
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"
FT CONFLICT 70
FT /note="G -> V (in Ref. 3; AAM62996)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Q -> T (in Ref. 3; AAM62996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17472 MW; 6A759F0B5667DFBA CRC64;
MAPITVGDVV PDGTISFFDE NDQLQTVSVH SIAAGKKVIL FGVPGAFTPT CSMSHVPGFI
GKAEELKSKG IDEIICFSVN DPFVMKAWGK TYQENKHVKF VADGSGEYTH LLGLELDLKD
KGLGIRSRRF ALLLDNLKVT VANVENGGEF TVSSAEDILK AL
