ID PRX2C_ORYSJ Reviewed; 162 AA.
AC Q9FR35; B7E2W9; Q7F529;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Peroxiredoxin-2C;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:Q9SRZ4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIC;
DE AltName: Full=Thioredoxin peroxidase 2C;
GN Name=PRXIIC; OrderedLocusNames=Os01g0675100, LOC_Os01g48420;
GN ORFNames=OJ1117_G01.9, OsJ_002891, P0485G01.43;
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. Nipponbare;
RA Alegre O., Antolin M., Imperial S.;
RT "Characterization of a new type of peroxiredoxin from Oryza sativa.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
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 -!- 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. {ECO:0000250|UniProtKB:Q9SRZ4}.
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:Q9SRZ4};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9SRZ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SRZ4}.
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}.
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DR EMBL; AF203879; AAG40130.1; -; mRNA.
DR EMBL; AP003264; BAC01192.1; -; Genomic_DNA.
DR EMBL; AP003374; BAB93323.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF05759.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS73651.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ13066.1; -; Genomic_DNA.
DR EMBL; AK058509; BAG86716.1; -; mRNA.
DR RefSeq; XP_015622003.1; XM_015766517.1.
DR AlphaFoldDB; Q9FR35; -.
DR SMR; Q9FR35; -.
DR STRING; 39947.Q9FR35; -.
DR PeroxiBase; 4017; OsPrxII03.
DR PaxDb; 39947-Q9FR35; -.
DR EnsemblPlants; Os01t0675100-01; Os01t0675100-01; Os01g0675100.
DR GeneID; 4325511; -.
DR Gramene; Os01t0675100-01; Os01t0675100-01; Os01g0675100.
DR KEGG; osa:4325511; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_1_2_1; -.
DR InParanoid; Q9FR35; -.
DR OMA; PTCHSAH; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q9FR35; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF8; PEROXIREDOXIN-2A-RELATED; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16758443"
FT CHAIN 2..162
FT /note="Peroxiredoxin-2C"
FT /id="PRO_0000282282"
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; 17291 MW; 43B5C6FB70480CB8 CRC64;
MAPVAVGDTL PDGQLGWFDG EDKLQQVSVH GLAAGKKVVL FGVPGAFTPT CSNQHVPGFI
NQAEQLKAKG VDDILLVSVN DPFVMKAWAK SYPENKHVKF LADGLGTYTK ALGLELDLSE
KGLGIRSRRF ALLADNLKVT VANIEEGGQF TISGAEEILK AL
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