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 24-JAN-2024, entry version 184. 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=10.1105/tpc.9.4.627; 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; 9. DR IntAct; Q05431; 4. DR MINT; Q05431; -. DR STRING; 3702.Q05431; -. DR PeroxiBase; 1890; AtAPx01. DR iPTMnet; Q05431; -. DR MetOSite; Q05431; -. DR PaxDb; 3702-AT1G07890-8; -. 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; AT1G07890; APX1. DR eggNOG; ENOG502QR1E; Eukaryota. DR HOGENOM; CLU_036959_3_0_1; -. DR InParanoid; Q05431; -. DR OrthoDB; 168803at2759; -. DR PhylomeDB; Q05431; -. DR BioCyc; ARA:AT1G07890-MONOMER; -. DR BRENDA; 1.11.1.11; 399. DR PRO; PR:Q05431; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q05431; baseline and differential. 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:0034599; P:cellular response to oxidative stress; IEA:InterPro. 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 CDD; cd00691; ascorbate_peroxidase; 1. DR Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. 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:SF60; L-ASCORBATE PEROXIDASE 1, CYTOSOLIC; 1. DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00459; ASPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. DR SWISS-2DPAGE; Q05431; -. DR Genevisible; Q05431; AT. 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 //