APX2_ORYSJ
ID APX2_ORYSJ Reviewed; 251 AA.
AC Q9FE01; Q0D3B8; Q40735;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=L-ascorbate peroxidase 2, cytosolic {ECO:0000305};
DE EC=1.11.1.11 {ECO:0000269|PubMed:15685422};
DE AltName: Full=APXb {ECO:0000303|PubMed:15685422};
DE AltName: Full=OsAPx2 {ECO:0000303|PubMed:15599508};
GN Name=APX2 {ECO:0000303|PubMed:15599508}; Synonyms=SS622;
GN OrderedLocusNames=Os07g0694700 {ECO:0000312|EMBL:BAT03377.1},
GN LOC_Os07g49400 {ECO:0000305};
GN ORFNames=OsJ_25704 {ECO:0000312|EMBL:EEE67880.1},
GN P0627E10.14 {ECO:0000312|EMBL:BAC84063.1};
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], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Nipponbare;
RX PubMed=15685422; DOI=10.1007/s10529-004-6587-0;
RA Lu Z., Takano T., Liu S.;
RT "Purification and characterization of two ascorbate peroxidases of rice
RT (Oryza sativa L.) expressed in Escherichia coli.";
RL Biotechnol. Lett. 27:63-67(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RA Morita S., Kaminaka H., Masumura T., Tanaka K.;
RT "The expression of two cytosolic ascorbate peroxidase genes in rice.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Structural and expression analysis of germinating seed genes in Oryza
RT sativa L.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 PROTEIN SEQUENCE OF 26-35.
RC STRAIN=cv. Nipponbare; TISSUE=Anther, Panicle, and Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-251.
RC TISSUE=Callus;
RA Uchimiya H.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14644501; DOI=10.1016/j.gene.2003.08.017;
RA Agrawal G.K., Jwa N.-S., Iwahashi H., Rakwal R.;
RT "Importance of ascorbate peroxidases OsAPX1 and OsAPX2 in the rice pathogen
RT response pathways and growth and reproduction revealed by their
RT transcriptional profiling.";
RL Gene 322:93-103(2003).
RN [9]
RP NOMENCLATURE.
RX PubMed=15599508; DOI=10.1007/s00239-004-2666-z;
RA Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.;
RT "Analysis of the molecular evolutionary history of the ascorbate peroxidase
RT gene family: inferences from the rice genome.";
RL J. Mol. Evol. 59:761-770(2004).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION BY SALT STRESS.
RX PubMed=16397796; DOI=10.1007/s00425-005-0214-8;
RA Teixeira F.K., Menezes-Benavente L., Galvao V.C., Margis R.,
RA Margis-Pinheiro M.;
RT "Rice ascorbate peroxidase gene family encodes functionally diverse
RT isoforms localized in different subcellular compartments.";
RL Planta 224:300-314(2006).
RN [11]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=22196946; DOI=10.1016/j.jplph.2011.11.012;
RA Chou T.S., Chao Y.Y., Kao C.H.;
RT "Involvement of hydrogen peroxide in heat shock- and cadmium-induced
RT expression of ascorbate peroxidase and glutathione reductase in leaves of
RT rice seedlings.";
RL J. Plant Physiol. 169:478-486(2012).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23468992; DOI=10.1371/journal.pone.0057472;
RA Zhang Z., Zhang Q., Wu J., Zheng X., Zheng S., Sun X., Qiu Q., Lu T.;
RT "Gene knockout study reveals that cytosolic ascorbate peroxidase 2(OsAPX2)
RT plays a critical role in growth and reproduction in rice under drought,
RT salt and cold stresses.";
RL PLoS ONE 8:E57472-E57472(2013).
RN [13]
RP INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=25546583; DOI=10.1016/j.jplph.2014.09.020;
RA Li Z., Su D., Lei B., Wang F., Geng W., Pan G., Cheng F.;
RT "Transcriptional profile of genes involved in ascorbate glutathione cycle
RT in senescing leaves for an early senescence leaf (esl) rice mutant.";
RL J. Plant Physiol. 176:1-15(2015).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal
CC (PubMed:15685422). Plays an important role in plant growth and
CC development by protecting the seedlings from abiotic stresses through
CC scavenging reactive oxygen species. Required for pollen viability
CC (PubMed:23468992). {ECO:0000269|PubMed:15685422,
CC ECO:0000269|PubMed:23468992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
CC Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC Evidence={ECO:0000269|PubMed:15685422};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuriphenylsulfonic acid
CC (CMPSA). {ECO:0000269|PubMed:15685422}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for ascorbate {ECO:0000269|PubMed:15685422};
CC KM=0.7 mM for H(2)O(2) {ECO:0000269|PubMed:15685422};
CC Vmax=20 mM/min/mg enzyme with ascorbate as substrate
CC {ECO:0000269|PubMed:15685422};
CC Vmax=3 mM/min/mg enzyme with H(2)O(2) as substrate
CC {ECO:0000269|PubMed:15685422};
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:15685422};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in aerial vegetative parts and
CC reproductive organs (PubMed:14644501). Expressed in roots, leaves,
CC stems and flowers (PubMed:16397796). Expressed in young leaves,
CC internodes, blade ears, stems and anthers (PubMed:23468992).
CC {ECO:0000269|PubMed:14644501, ECO:0000269|PubMed:16397796,
CC ECO:0000269|PubMed:23468992}.
CC -!- INDUCTION: By stress and hormones. By infection with rice blast fungus
CC (M.grisea). Circadian-regulation. Expression is higher during the light
CC phase than during the dark phase. Induced by salt stress
CC (PubMed:16397796, PubMed:23468992). Induced by heat shock
CC (PubMed:22196946). Induced by hydrogen peroxide in leaves
CC (PubMed:25546583). Induced by drought and cold stresses
CC (PubMed:23468992). {ECO:0000269|PubMed:14644501,
CC ECO:0000269|PubMed:16397796, ECO:0000269|PubMed:22196946,
CC ECO:0000269|PubMed:23468992, ECO:0000269|PubMed:25546583}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf plants, yellow-green leaves, leaf
CC lesion mimic phenotype, abnormal anther morphology, defects in pollen
CC viability and seed sterility. {ECO:0000269|PubMed:23468992}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+) (By similarity). Plants over-expressing APX2 have
CC increased ascorbate peroxidase activity and exhibit enhanced tolerance
CC to salt, drought and cold stresses (PubMed:23468992). {ECO:0000250,
CC ECO:0000269|PubMed:23468992}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
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DR EMBL; AB053297; BAB20889.1; -; mRNA.
DR EMBL; AB050724; BAB17666.1; -; mRNA.
DR EMBL; GQ848056; ADM86869.1; -; mRNA.
DR EMBL; AP005199; BAC84063.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22655.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT03377.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67880.1; -; Genomic_DNA.
DR EMBL; AK061715; BAG88062.1; -; mRNA.
DR EMBL; D25238; BAA04962.1; -; mRNA.
DR PIR; T04114; T04114.
DR RefSeq; XP_015646556.1; XM_015791070.1.
DR AlphaFoldDB; Q9FE01; -.
DR SMR; Q9FE01; -.
DR STRING; 4530.OS07T0694700-01; -.
DR PeroxiBase; 1866; OsAPx02.
DR PaxDb; Q9FE01; -.
DR PRIDE; Q9FE01; -.
DR EnsemblPlants; Os07t0694700-01; Os07t0694700-01; Os07g0694700.
DR GeneID; 4344397; -.
DR Gramene; Os07t0694700-01; Os07t0694700-01; Os07g0694700.
DR KEGG; osa:4344397; -.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q9FE01; -.
DR OMA; QSHGANA; -.
DR OrthoDB; 1228462at2759; -.
DR BRENDA; 1.11.1.11; 4460.
DR SABIO-RK; Q9FE01; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q9FE01; baseline and differential.
DR Genevisible; Q9FE01; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; 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 GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002207; Peroxidase_I.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide;
KW Iron; Metal-binding; Oxidoreductase; Peroxidase; Potassium;
KW Reference proteome; Stress response.
FT CHAIN 1..251
FT /note="L-ascorbate peroxidase 2, cytosolic"
FT /id="PRO_0000055594"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 164
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 165
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 39
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 202..215
FT /note="GLLQLPSDKALMAD -> PSSSCQVTKPSWLT (in Ref. 7;
FT BAA04962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 27118 MW; D6497B224285DF93 CRC64;
MGSKSYPTVS DEYLAAVGKA KRKLRGLIAE KNCAPLMLRL AWHSAGTFDV SSRTGGPFGT
MKNPGEQSHA ANAGLDIAVR LLDPIKDQLP ILSYADFYQL AGVVAVEVTG GPEVPFHPGR
QDKPEPPPEG RLPDATQGSD HLRQVFSAQM GLSDKDIVAL SGGHTLGRCH KERSGFEGAW
TSNPLIFDNS YFTELVSGEK EGLLQLPSDK ALMADPAFRP LVEKYAADED AFFADYAEAH
LKLSELGFAE E
