PRX2B_ARATH
ID PRX2B_ARATH Reviewed; 162 AA.
AC Q9XEX2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peroxiredoxin-2B;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIB;
DE AltName: Full=Peroxiredoxin TPx1;
DE AltName: Full=Thioredoxin peroxidase 2B;
DE AltName: Full=Thioredoxin-dependent peroxidase 1;
GN Name=PRXIIB; Synonyms=TPX1; OrderedLocusNames=At1g65980;
GN ORFNames=F12P19.14;
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 SUBUNIT, 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 [6]
RP FUNCTION, 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 [7]
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: Reduces hydrogen peroxide and alkyl hydroperoxides with
CC reducing equivalents provided through the thioredoxin or glutaredoxin
CC system. May be involved in intracellular redox signaling.
CC {ECO:0000269|PubMed:12913160}.
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:0000269|PubMed:12913160}.
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, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913160}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XEX2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues but mostly in reproductive
CC tissues such as buds, flowers, siliques and seeds.
CC {ECO:0000269|PubMed:12913160, ECO:0000269|Ref.5}.
CC -!- INDUCTION: Slightly induced by salt stress. {ECO:0000269|Ref.5}.
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) is reactivated by glutaredoxin (Grx).
CC {ECO:0000305|PubMed:12913160}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF121355; AAD28242.1; -; mRNA.
DR EMBL; AC009513; AAF06058.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34447.1; -; Genomic_DNA.
DR EMBL; AF332464; AAG48827.1; -; mRNA.
DR EMBL; AY065056; AAL57690.1; -; mRNA.
DR PIR; B96684; B96684.
DR PIR; PA0022; PA0022.
DR RefSeq; NP_176773.1; NM_105270.3. [Q9XEX2-1]
DR AlphaFoldDB; Q9XEX2; -.
DR SMR; Q9XEX2; -.
DR BioGRID; 28131; 1.
DR IntAct; Q9XEX2; 2.
DR MINT; Q9XEX2; -.
DR STRING; 3702.AT1G65980.1; -.
DR PeroxiBase; 14571; HaPNC17.
DR PeroxiBase; 4344; AtPrxII02.
DR PaxDb; Q9XEX2; -.
DR PRIDE; Q9XEX2; -.
DR ProteomicsDB; 226481; -. [Q9XEX2-1]
DR EnsemblPlants; AT1G65980.1; AT1G65980.1; AT1G65980. [Q9XEX2-1]
DR GeneID; 842910; -.
DR Gramene; AT1G65980.1; AT1G65980.1; AT1G65980. [Q9XEX2-1]
DR KEGG; ath:AT1G65980; -.
DR Araport; AT1G65980; -.
DR TAIR; locus:2009719; AT1G65980.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_1_2_1; -.
DR InParanoid; Q9XEX2; -.
DR OMA; GYINHPK; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q9XEX2; -.
DR BioCyc; ARA:AT1G65980-MON; -.
DR BioCyc; MetaCyc:AT1G65980-MON; -.
DR PRO; PR:Q9XEX2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XEX2; baseline and differential.
DR Genevisible; Q9XEX2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..162
FT /note="Peroxiredoxin-2B"
FT /id="PRO_0000282279"
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; 17428 MW; 6EB4690D17598814 CRC64;
MAPIAVGDVV PDGTISFFDE NDQLQTASVH SLAAGKKVIL FGVPGAFTPT CSMKHVPGFI
EKAEELKSKG VDEIICFSVN DPFVMKAWGK TYPENKHVKF VADGSGEYTH LLGLELDLKD
KGLGVRSRRF ALLLDDLKVT VANVESGGEF TVSSADDILK AL
