APX4_ORYSJ
ID APX4_ORYSJ Reviewed; 291 AA.
AC Q6ZJJ1; Q0J3W2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable L-ascorbate peroxidase 4, peroxisomal {ECO:0000305};
DE EC=1.11.1.11 {ECO:0000305};
DE AltName: Full=OsAPx4 {ECO:0000303|PubMed:15599508};
GN Name=APX4 {ECO:0000303|PubMed:15599508};
GN OrderedLocusNames=Os08g0549100 {ECO:0000312|EMBL:BAT06572.1},
GN LOC_Os08g43560 {ECO:0000305};
GN ORFNames=OJ1479_B11.9 {ECO:0000312|EMBL:BAD08951.1};
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].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Immature seed;
RA Lee S.B., Yoon U.H., Jeong M.J., Suh E.J., Lee J.S.;
RT "Molecular cloning of L-ascorbate peroxidase gene in rice.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY.
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 [8]
RP INDUCTION.
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. {ECO:0000250}.
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:0000305};
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 -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q0JEQ2}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:16397796}.
CC -!- INDUCTION: Down-regulated by hydrogen peroxide in leaves.
CC {ECO:0000269|PubMed:25546583}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:15599508, it may be peroxisomal. There is
CC however no experimental evidence to prove this. {ECO:0000305}.
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DR EMBL; HQ013288; AEK99328.1; -; mRNA.
DR EMBL; AP003912; BAD08951.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24353.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06572.1; -; Genomic_DNA.
DR EMBL; AK070842; BAG92166.1; -; mRNA.
DR RefSeq; XP_015650808.1; XM_015795322.1.
DR AlphaFoldDB; Q6ZJJ1; -.
DR SMR; Q6ZJJ1; -.
DR STRING; 4530.OS08T0549100-01; -.
DR PeroxiBase; 1868; OsAPx04.
DR PaxDb; Q6ZJJ1; -.
DR PRIDE; Q6ZJJ1; -.
DR EnsemblPlants; Os08t0549100-01; Os08t0549100-01; Os08g0549100.
DR GeneID; 4346247; -.
DR Gramene; Os08t0549100-01; Os08t0549100-01; Os08g0549100.
DR KEGG; osa:4346247; -.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q6ZJJ1; -.
DR OMA; EREYTHG; -.
DR OrthoDB; 1228462at2759; -.
DR BRENDA; 1.11.1.11; 4460.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6ZJJ1; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Calcium; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Peroxidase; Peroxisome; Potassium; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Probable L-ascorbate peroxidase 4, peroxisomal"
FT /id="PRO_0000055596"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 160
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 161
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 36
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 291 AA; 31738 MW; 5B605C442EB57807 CRC64;
MAAPVVDAEY LRQVDRARRH LRALISSKGC APIMLRLAWH DAGTYDVNTK TGGANGSIRY
EEEYTHGSNA GLKIAIDLLE PIKAKSPKIT YADLYQLAGV VAVEVTGGPT VEFIPGRRDS
SVCPREGRLP DAKKGALHLR DIFYRMGLSD KDIVALSGGH TLGRAHPERS GFEGAWTQEP
LKFDNSYFLE LLKGESEGLL KLPTDKALLE DPSFRRYVDL YARDEDTFFK DYAESHKKLS
ELGFTPRSSG PASTKSDLST GAVLAQSAVG VAVAAAVVIV SYLYEASKKS K
