REHYA_ORYSJ
ID REHYA_ORYSJ Reviewed; 220 AA.
AC P0C5C9; A2YP41; A3BMM5; P52573; Q0D4A2; Q8GVH0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=1-Cys peroxiredoxin A;
DE Short=1-Cys Prx A;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Protein RAB24;
DE AltName: Full=Rice 1Cys-peroxiredoxin;
DE Short=R1C-Prx;
DE AltName: Full=Thioredoxin peroxidase A;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin A {ECO:0000305};
GN OrderedLocusNames=Os07g0638300, LOC_Os07g44430;
GN ORFNames=OJ1340_C08.107, OsJ_024297;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Yuhkara;
RA Fujino K., Tanaka K., Xu Z., Kikuta Y.;
RT "ABA-responsive 24kDa polypeptide from rice calli is related to the thiol-
RT specific antioxidant family.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yao Q., Peng R., Xiong A.;
RT "Identification a novel antioxidant enzyme from rice.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=11113447; DOI=10.1016/s0014-5793(00)02230-4;
RA Lee K.O., Jang H.H., Jung B.G., Chi Y.H., Lee J.Y., Choi Y.O., Lee J.R.,
RA Lim C.O., Cho M.J., Lee S.Y.;
RT "Rice 1Cys-peroxiredoxin over-expressed in transgenic tobacco does not
RT maintain dormancy but enhances antioxidant activity.";
RL FEBS Lett. 486:103-106(2000).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively (By similarity). Seems to contribute to the inhibition of
CC germination during stress (PubMed:11113447).
CC {ECO:0000250|UniProtKB:O04005, ECO:0000269|PubMed:11113447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O04005}. Cytoplasm
CC {ECO:0000250|UniProtKB:O04005}.
CC -!- INDUCTION: By abscisic acid (ABA) and oxidative stress.
CC {ECO:0000269|PubMed:11113447}.
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:O35244}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000305}.
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DR EMBL; D63917; BAA09947.1; -; mRNA.
DR EMBL; AY336994; AAQ01200.1; -; mRNA.
DR EMBL; AP005292; BAC45197.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22321.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02838.1; -; Genomic_DNA.
DR EMBL; CM000144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T03967; T03967.
DR RefSeq; XP_015645300.1; XM_015789814.1.
DR AlphaFoldDB; P0C5C9; -.
DR SMR; P0C5C9; -.
DR STRING; 4530.OS07T0638300-01; -.
DR Allergome; 9884; Ory s 32.
DR PeroxiBase; 4023; Os1CysPrx01.
DR PaxDb; P0C5C9; -.
DR PRIDE; P0C5C9; -.
DR EnsemblPlants; Os07t0638300-01; Os07t0638300-01; Os07g0638300.
DR GeneID; 4344045; -.
DR Gramene; Os07t0638300-01; Os07t0638300-01; Os07g0638300.
DR KEGG; osa:4344045; -.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_1_1; -.
DR InParanoid; P0C5C9; -.
DR OMA; MIDYQDT; -.
DR OrthoDB; 1129256at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; P0C5C9; baseline and differential.
DR Genevisible; P0C5C9; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR CDD; cd03016; PRX_1cys; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Nucleus; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome; Stress response.
FT CHAIN 1..220
FT /note="1-Cys peroxiredoxin A"
FT /id="PRO_0000135110"
FT DOMAIN 4..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 195..218
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT CONFLICT 55
FT /note="G -> A (in Ref. 1; BAA09947)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="I -> F (in Ref. 1; BAA09947)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..171
FT /note="HAV -> TRL (in Ref. 1; BAA09947)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="RV -> PF (in Ref. 1; BAA09947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24042 MW; E0FB43315E176780 CRC64;
MPGLTIGDTV PNLELDSTHG KIRIHDFVGD TYVILFSHPG DFTPVCTTEL AAMAGYAKEF
DKRGVKLLGI SCDDVQSHKD WIKDIEAYKP GNRVTYPIMA DPSREAIKQL NMVDPDEKDS
NGGHLPSRAL HIVGPDKKVK LSFLYPACVG RNMDEVVRAV DALQTAAKHA VATPVNWKPG
ERVVIPPGVS DDEAKEKFPQ GFDTADLPSG KGYLRFTKVG
