APX1_ARATH
ID APX1_ARATH Reviewed; 250 AA.
AC Q05431; Q0WLU2; Q2V4P8; Q2V4P9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=L-ascorbate peroxidase 1, cytosolic;
DE Short=AP;
DE Short=AtAPx01;
DE EC=1.11.1.11 {ECO:0000305|PubMed:15608336};
GN Name=APX1; OrderedLocusNames=At1g07890; ORFNames=F24B9.2;
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 [MRNA], AND PROTEIN SEQUENCE OF 2-17.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=1558944; DOI=10.1007/bf00020011;
RA Kubo A., Saji H., Tanaka K., Tanaka K., Kondo N.;
RT "Cloning and sequencing of a cDNA encoding ascorbate peroxidase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 18:691-701(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8422923; DOI=10.1016/0014-5793(93)81185-3;
RA Kubo A., Saji H., Tanaka K., Kondo N.;
RT "Genomic DNA structure of a gene encoding cytosolic ascorbate peroxidase
RT from Arabidopsis thaliana.";
RL FEBS Lett. 315:313-317(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INDUCTION.
RX PubMed=8534847; DOI=10.1007/bf00020979;
RA Kubo A., Saji H., Tanaka K., Kondo N.;
RT "Expression of Arabidopsis cytosolic ascorbate peroxidase gene in response
RT to ozone or sulfur dioxide.";
RL Plant Mol. Biol. 29:479-489(1995).
RN [10]
RP INDUCTION.
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 [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9808745; DOI=10.1104/pp.118.3.1005;
RA Storozhenko S., De Pauw P., Van Montagu M., Inze D., Kushnir S.;
RT "The heat-shock element is a functional component of the Arabidopsis APX1
RT gene promoter.";
RL Plant Physiol. 118:1005-1014(1998).
RN [12]
RP INDUCTION.
RX PubMed=14739345; DOI=10.1104/pp.103.029876;
RA Fourcroy P., Vansuyt G., Kushnir S., Inze D., Briat J.-F.;
RT "Iron-regulated expression of a cytosolic ascorbate peroxidase encoded by
RT the APX1 gene in Arabidopsis seedlings.";
RL Plant Physiol. 134:605-613(2004).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15608336; DOI=10.1105/tpc.104.026971;
RA Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J.,
RA Shulaev V., Schlauch K., Mittler R.;
RT "Cytosolic ascorbate peroxidase 1 is a central component of the reactive
RT oxygen gene network of Arabidopsis.";
RL Plant Cell 17:268-281(2005).
RN [14]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal. Constitutes a
CC central component of the reactive oxygen gene network.
CC {ECO:0000269|PubMed:15608336}.
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|PubMed:15608336};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- INTERACTION:
CC Q05431; Q42403: TRX3; NbExp=2; IntAct=EBI-449365, EBI-449157;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q05431-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers.
CC {ECO:0000269|PubMed:9808745}.
CC -!- INDUCTION: By ethylene, ozone, sulfur dioxide, Fe exposure, oxidative
CC and heat-shock stresses, and by excess light treatment. Induced by
CC cadmium (PubMed:16502469). {ECO:0000269|PubMed:14739345,
CC ECO:0000269|PubMed:16502469, ECO:0000269|PubMed:8534847,
CC ECO:0000269|PubMed:9144965, ECO:0000269|PubMed:9808745}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59600; CAA42168.1; -; mRNA.
DR EMBL; D14442; BAA03334.1; -; Genomic_DNA.
DR EMBL; U63815; AAB07880.1; -; Genomic_DNA.
DR EMBL; AC007583; AAF75066.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28200.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28201.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28202.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28203.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28204.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28206.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28207.1; -; Genomic_DNA.
DR EMBL; AY039879; AAK63983.1; -; mRNA.
DR EMBL; AY056395; AAL08251.1; -; mRNA.
DR EMBL; AY094002; AAM16263.1; -; mRNA.
DR EMBL; AK230096; BAF01915.1; -; mRNA.
DR EMBL; AY086425; AAM63427.1; -; mRNA.
DR PIR; D86214; D86214.
DR PIR; S20866; S20866.
DR RefSeq; NP_001030991.2; NM_001035914.2. [Q05431-1]
DR RefSeq; NP_001077482.1; NM_001084013.1. [Q05431-1]
DR RefSeq; NP_001117244.1; NM_001123772.2. [Q05431-1]
DR RefSeq; NP_001318949.1; NM_001331739.1. [Q05431-1]
DR RefSeq; NP_172267.1; NM_100663.4. [Q05431-1]
DR RefSeq; NP_849607.1; NM_179276.2. [Q05431-1]
DR RefSeq; NP_973786.1; NM_202057.2. [Q05431-1]
DR AlphaFoldDB; Q05431; -.
DR SMR; Q05431; -.
DR BioGRID; 22545; 8.
DR IntAct; Q05431; 4.
DR MINT; Q05431; -.
DR STRING; 3702.AT1G07890.8; -.
DR PeroxiBase; 1890; AtAPx01.
DR iPTMnet; Q05431; -.
DR MetOSite; Q05431; -.
DR SWISS-2DPAGE; Q05431; -.
DR PaxDb; Q05431; -.
DR PRIDE; Q05431; -.
DR ProteomicsDB; 244428; -. [Q05431-1]
DR EnsemblPlants; AT1G07890.1; AT1G07890.1; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.2; AT1G07890.2; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.3; AT1G07890.3; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.4; AT1G07890.4; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.5; AT1G07890.5; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.7; AT1G07890.7; AT1G07890. [Q05431-1]
DR EnsemblPlants; AT1G07890.8; AT1G07890.8; AT1G07890. [Q05431-1]
DR GeneID; 837304; -.
DR Gramene; AT1G07890.1; AT1G07890.1; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.2; AT1G07890.2; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.3; AT1G07890.3; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.4; AT1G07890.4; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.5; AT1G07890.5; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.7; AT1G07890.7; AT1G07890. [Q05431-1]
DR Gramene; AT1G07890.8; AT1G07890.8; AT1G07890. [Q05431-1]
DR KEGG; ath:AT1G07890; -.
DR Araport; AT1G07890; -.
DR TAIR; locus:2026616; AT1G07890.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q05431; -.
DR PhylomeDB; Q05431; -.
DR BioCyc; ARA:AT1G07890-MON; -.
DR BRENDA; 1.11.1.11; 399.
DR PRO; PR:Q05431; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q05431; baseline and differential.
DR Genevisible; Q05431; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046409; F:p-coumarate 3-hydroxylase activity; IDA:TAIR.
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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IDA:TAIR.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
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 Alternative splicing; Calcium; Cytoplasm; Direct protein sequencing; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Potassium; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1558944"
FT CHAIN 2..250
FT /note="L-ascorbate peroxidase 1, cytosolic"
FT /id="PRO_0000055592"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
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 38
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
SQ SEQUENCE 250 AA; 27561 MW; 33A536D85B2CAA6C CRC64;
MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ SRTGGPFGTM
RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA GVVAVEVTGG PDIPFHPGRE
DKPQPPPEGR LPDATKGCDH LRDVFAKQMG LSDKDIVALS GAHTLGRCHK DRSGFEGAWT
SNPLIFDNSY FKELLSGEKE GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM
KLSELGFADA
