APX8_ORYSJ
ID APX8_ORYSJ Reviewed; 478 AA.
AC Q69SV0; A0A0P0VKA2; Q0E0G3; Q7XJ01;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable L-ascorbate peroxidase 8, chloroplastic {ECO:0000305};
DE EC=1.11.1.11 {ECO:0000305};
DE AltName: Full=OsAPx8 {ECO:0000303|PubMed:15599508};
DE Flags: Precursor;
GN Name=APX8 {ECO:0000303|PubMed:15599508};
GN OrderedLocusNames=Os02g0553200 {ECO:0000312|EMBL:BAS79186.1},
GN LOC_Os02g34810 {ECO:0000305};
GN ORFNames=P0470G10.5 {ECO:0000312|EMBL:BAD33296.1};
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. Nipponbare;
RA Morita S., Kotani T., Kaminaka H., Masumura T., Tanaka K.;
RT "The expression of rice chloroplastic ascorbate peroxidase genes during
RT greening.";
RL Submitted (JUL-2003) 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=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 [4]
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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
RP INDUCTION.
RX PubMed=17916638; DOI=10.1093/jxb/erm174;
RA Hong C.Y., Hsu Y.T., Tsai Y.C., Kao C.H.;
RT "Expression of ASCORBATE PEROXIDASE 8 in roots of rice (Oryza sativa L.)
RT seedlings in response to NaCl.";
RL J. Exp. Bot. 58:3273-3283(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND 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).
RN [8]
RP FUNCTION, INTERACTION WITH SWEET11/OS8N3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY XANTHOMONAS ORYZAE.
RC STRAIN=cv. Taipei 309;
RX PubMed=27185545; DOI=10.1038/srep26104;
RA Jiang G., Yin D., Zhao J., Chen H., Guo L., Zhu L., Zhai W.;
RT "The rice thylakoid membrane-bound ascorbate peroxidase OsAPX8 functions in
RT tolerance to bacterial blight.";
RL Sci. Rep. 6:26104-26104(2016).
CC -!- FUNCTION: Involved in defense response and tolerance to the bacterial
CC pathogen Xanthomonas oryzae pv. oryzae (Xoo). Plays an important role
CC in hydrogen peroxide removal during infection by Xoo. Involved in
CC response to abiotic stress. Plays a role in hydrogen peroxide removal
CC durings salt stress. {ECO:0000269|PubMed:27185545}.
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 -!- SUBUNIT: Interacts with SWEET11/OS8N3. {ECO:0000269|PubMed:27185545}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:27185545, ECO:0000305|PubMed:25546583}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers
CC (PubMed:16397796). Expressed in leaves, shoots and panicles. Expressed
CC at low levels in roots (PubMed:27185545). {ECO:0000269|PubMed:16397796,
CC ECO:0000269|PubMed:27185545}.
CC -!- INDUCTION: Induced by salt stress, abscisic acid (ABA), sodium nitrate
CC and hydrogen peroxide in roots (PubMed:17916638). Induced by infection
CC with the bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo)
CC (PubMed:27185545). Down-regulated by salt stress in leaves
CC (PubMed:16397796). Down-regulated by hydrogen peroxide in leaves
CC (PubMed:25546583). {ECO:0000269|PubMed:16397796,
CC ECO:0000269|PubMed:17916638, ECO:0000269|PubMed:25546583,
CC ECO:0000269|PubMed:27185545}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+) (By similarity). Plants over-expressing APX8 exhibit
CC increased tolerance to the bacterial pathogen Xanthomonas oryzae pv.
CC oryzae (Xoo). Plants silencing APX8 show increased sensitivity to Xoo
CC (PubMed:27185545). {ECO:0000250, ECO:0000269|PubMed:27185545}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD33296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS79186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB114856; BAC79363.1; -; mRNA.
DR EMBL; AP004876; BAD33296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF09025.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79186.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015623105.1; XM_015767619.1.
DR AlphaFoldDB; Q69SV0; -.
DR SMR; Q69SV0; -.
DR STRING; 4530.OS02T0553200-01; -.
DR PeroxiBase; 1872; OsAPx08.
DR PaxDb; Q69SV0; -.
DR PRIDE; Q69SV0; -.
DR EnsemblPlants; Os02t0553200-01; Os02t0553200-01; Os02g0553200.
DR GeneID; 4329643; -.
DR Gramene; Os02t0553200-01; Os02t0553200-01; Os02g0553200.
DR KEGG; osa:4329643; -.
DR eggNOG; ENOG502QS7Q; Eukaryota.
DR HOGENOM; CLU_036959_2_0_1; -.
DR InParanoid; Q69SV0; -.
DR OrthoDB; 1228462at2759; -.
DR BRENDA; 1.11.1.11; 4460.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q69SV0; OS.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Chloroplast; Heme; Hydrogen peroxide; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Peroxidase; Plant defense; Plastid;
KW Potassium; Reference proteome; Stress response; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 77..478
FT /note="Probable L-ascorbate peroxidase 8, chloroplastic"
FT /id="PRO_0000042658"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 246
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 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 478 AA; 51188 MW; EE5DFC9821EA87C2 CRC64;
MAERIAASLL PAASPSPAPS PPPPRPRVSA AAAASFPCCS TSAGGLRLRS RPSRFPQKAA
TTRSGRAGAG ARAVVRCMAA AAVAASDAAQ LKSAREDIRE ILKTTYCHPI MVRLGWHDSG
TYDKNIEEWP QRGGADGSLR FDAELSHGAN AGLINALKLI QPIKDKYPGI TYADLFQLAS
ATAIEEAGGP KIPMKYGRVD VTAAEQCPPE GRLPDAGPRV PADHLREVFY RMGLDDKEIV
ALSGAHTLGR SRPDRSGWGK PETKYTKDGP GEPGGQSWTV EWLKFDNSYF KDIKEQRDQD
LLVLPTDAAL FEDPSFKVYA EKYAEDQEAF FKDYAEAHAK LSDLGAKFDP PEGFSLDDEP
AVEEKDPEPA PAPAAAPPPP PVEEKKEAEP TPVPVTVGAA VASSPADDNN GAAPQPEPFV
AAKYSYGKKE LSDSMKQKIR AEYEGFGGSP DKPLQSNYFL NIMLLIGGLA FLTSLLGS
