APX2_ARATH
ID APX2_ARATH Reviewed; 251 AA.
AC Q1PER6; Q39006; Q67XB1; Q9SF39;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=L-ascorbate peroxidase 2, cytosolic;
DE EC=1.11.1.11;
DE AltName: Full=L-ascorbate peroxidase 1b;
DE Short=APX1b;
DE Short=AtAPx02;
GN Name=APX2; Synonyms=APX1B; OrderedLocusNames=At3g09640; ORFNames=F11F8_23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8580771; DOI=10.1007/bf00197587;
RA Santos M., Gosseau H., Lister C., Foyer C., Creissen G.P., Mullineaux P.M.;
RT "Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by
RT a small multigene family.";
RL Planta 198:64-69(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9144965; DOI=10.2307/3870512;
RA Karpinski S., Escobar C., Karpinski B., Creissen G.P., Mullineaux P.M.;
RT "Photosynthetic electron transport regulates the expression of cytosolic
RT ascorbate peroxidase genes in Arabidopsis during excess light stress.";
RL Plant Cell 9:627-640(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [7]
RP INDUCTION.
RX PubMed=12068123; DOI=10.1104/pp.001362;
RA Panchuk I.I., Volkov R.A., Schoffl F.;
RT "Heat stress- and heat shock transcription factor-dependent expression and
RT activity of ascorbate peroxidase in Arabidopsis.";
RL Plant Physiol. 129:838-853(2002).
RN [8]
RP INDUCTION.
RX PubMed=15086807; DOI=10.1111/j.1365-313x.2004.02066.x;
RA Chang C.C., Ball L., Fryer M.J., Baker N.R., Karpinski S., Mullineaux P.M.;
RT "Induction of ASCORBATE PEROXIDASE 2 expression in wounded Arabidopsis
RT leaves does not involve known wound-signalling pathways but is associated
RT with changes in photosynthesis.";
RL Plant J. 38:499-511(2004).
RN [9]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12609042; DOI=10.1046/j.1365-313x.2003.01656.x;
RA Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M.,
RA Baker N.R.;
RT "Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf
RT water status during excess light stress reveals a functional organisation
RT of Arabidopsis leaves.";
RL Plant J. 33:691-705(2003).
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in bundle sheath cells, the photosynthetic
CC cells that surround the phloem and xylem.
CC {ECO:0000269|PubMed:12609042}.
CC -!- INDUCTION: By excess light treatment, by wounding and by heat-shock
CC stress. {ECO:0000269|PubMed:12068123, ECO:0000269|PubMed:12609042,
CC ECO:0000269|PubMed:15086807, ECO:0000269|PubMed:9144965}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF23294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X80036; CAA56340.1; -; Genomic_DNA.
DR EMBL; X98275; CAA66925.1; -; mRNA.
DR EMBL; AC016661; AAF23294.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74791.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74792.1; -; Genomic_DNA.
DR EMBL; AK176821; BAD44584.1; -; mRNA.
DR EMBL; AK176908; BAD44671.1; -; mRNA.
DR EMBL; DQ446651; ABE65932.1; -; mRNA.
DR RefSeq; NP_001030664.1; NM_001035587.3.
DR RefSeq; NP_187575.2; NM_111798.4.
DR AlphaFoldDB; Q1PER6; -.
DR SMR; Q1PER6; -.
DR STRING; 3702.AT3G09640.1; -.
DR PeroxiBase; 1888; AtAPx02.
DR PaxDb; Q1PER6; -.
DR PRIDE; Q1PER6; -.
DR ProteomicsDB; 246597; -.
DR EnsemblPlants; AT3G09640.1; AT3G09640.1; AT3G09640.
DR EnsemblPlants; AT3G09640.2; AT3G09640.2; AT3G09640.
DR GeneID; 820121; -.
DR Gramene; AT3G09640.1; AT3G09640.1; AT3G09640.
DR Gramene; AT3G09640.2; AT3G09640.2; AT3G09640.
DR KEGG; ath:AT3G09640; -.
DR Araport; AT3G09640; -.
DR TAIR; locus:2074914; AT3G09640.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q1PER6; -.
DR OMA; RTDYVDD; -.
DR OrthoDB; 1228462at2759; -.
DR PhylomeDB; Q1PER6; -.
DR BioCyc; ARA:AT3G09640-MON; -.
DR PRO; PR:Q1PER6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PER6; baseline and differential.
DR Genevisible; Q1PER6; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; TAS:TAIR.
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:0006979; P:response to oxidative stress; IDA:TAIR.
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; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Potassium; Reference proteome.
FT CHAIN 1..251
FT /note="L-ascorbate peroxidase 2, cytosolic"
FT /id="PRO_0000261322"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 163
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 164
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 187
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 6
FT /note="Y -> F (in Ref. 6; ABE65932)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="F -> S (in Ref. 1; CAA66925 and 2; CAA56340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 28006 MW; FFC7F6D82A4EF3E0 CRC64;
MVKKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV KTKTGGPFGT
IRHPQELAHD ANNGLDIAVR LLDPIKELFP ILSYADFYQL AGVVAVEITG GPEIPFHPGR
LDKVEPPPEG RLPQATKGVD HLRDVFGRMG LNDKDIVALS GGHTLGRCHK ERSGFEGAWT
PNPLIFDNSY FKEILSGEKE GLLQLPTDKA LLDDPLFLPF VEKYAADEDA FFEDYTEAHL
KLSELGFADK E
