APX3_ARATH
ID APX3_ARATH Reviewed; 287 AA.
AC Q42564; O81810;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=L-ascorbate peroxidase 3;
DE Short=AtAPx03;
DE EC=1.11.1.11;
GN Name=APX3; Synonyms=APX, APXIII; OrderedLocusNames=At4g35000;
GN ORFNames=M4E13.60;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9291097; DOI=10.1042/bj3260305;
RA Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G.;
RT "From sequence analysis of three novel ascorbate peroxidases from
RT Arabidopsis thaliana to structure, function and evolution of seven types of
RT ascorbate peroxidase.";
RL Biochem. J. 326:305-310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
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 [MRNA].
RX PubMed=9290648; DOI=10.1023/a:1005814109732;
RA Zhang H., Wang J., Nickel U., Allen R.D., Goodman H.M.;
RT "Cloning and expression of an Arabidopsis gene encoding a putative
RT peroxisomal ascorbate peroxidase.";
RL Plant Mol. Biol. 34:967-971(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Escobar C., Bradley D.J., Puente P., Harberd N., Creissen G.P.,
RA Mullineaux P.M.;
RT "Ascorbate peroxidase III gene from Arabidopsis thaliana is regulated by
RT light and development.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [6]
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 [7]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=16873450; DOI=10.1093/jxb/erl060;
RA Narendra S., Venkataramani S., Shen G., Wang J., Pasapula V., Lin Y.,
RA Kornyeyev D., Holaday A.S., Zhang H.;
RT "The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound
RT antioxidant enzyme and is dispensable for Arabidopsis growth and
RT development.";
RL J. Exp. Bot. 57:3033-3042(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [11]
RP SUBCELLULAR LOCATION, INTERACTION WITH AKR2A AND AKR2B, AKR2A-BINDING
RP SEQUENCE, AND DOMAIN.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [12]
RP AKR2A-BINDING SEQUENCE, INTERACTION WITH AKR2A, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- SUBUNIT: Interacts via its C-terminal region with AKR2A and AKR2B.
CC {ECO:0000269|PubMed:20215589, ECO:0000269|PubMed:21057222}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:16873450,
CC ECO:0000269|PubMed:20215589}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16873450}. Glyoxysome membrane
CC {ECO:0000269|PubMed:16873450}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16873450}.
CC -!- DOMAIN: The transmembrane plays critical roles in migration to the
CC peroxisome and/or subsequent insertion into the membrane.
CC {ECO:0000269|PubMed:20215589}.
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}.
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DR EMBL; X98003; CAA66640.1; -; mRNA.
DR EMBL; X98276; CAA66926.1; -; mRNA.
DR EMBL; U69138; AAB71493.1; -; mRNA.
DR EMBL; AJ006030; CAA06823.1; -; Genomic_DNA.
DR EMBL; AL022023; CAA17765.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80217.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86445.1; -; Genomic_DNA.
DR EMBL; AY065143; AAL38319.1; -; mRNA.
DR EMBL; AY081646; AAM10208.1; -; mRNA.
DR EMBL; AY086162; AAM63367.1; -; mRNA.
DR PIR; S71279; S71279.
DR RefSeq; NP_195226.1; NM_119666.4.
DR AlphaFoldDB; Q42564; -.
DR SMR; Q42564; -.
DR BioGRID; 14934; 3.
DR STRING; 3702.AT4G35000.1; -.
DR PeroxiBase; 1891; AtAPx03.
DR iPTMnet; Q42564; -.
DR PaxDb; Q42564; -.
DR PRIDE; Q42564; -.
DR ProteomicsDB; 241020; -.
DR EnsemblPlants; AT4G35000.1; AT4G35000.1; AT4G35000.
DR GeneID; 829652; -.
DR Gramene; AT4G35000.1; AT4G35000.1; AT4G35000.
DR KEGG; ath:AT4G35000; -.
DR Araport; AT4G35000; -.
DR TAIR; locus:2131586; AT4G35000.
DR eggNOG; ENOG502QR1E; Eukaryota.
DR HOGENOM; CLU_036959_3_0_1; -.
DR InParanoid; Q42564; -.
DR OMA; ANDCTIL; -.
DR OrthoDB; 1228462at2759; -.
DR PhylomeDB; Q42564; -.
DR BioCyc; ARA:AT4G35000-MON; -.
DR PRO; PR:Q42564; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42564; baseline and differential.
DR Genevisible; Q42564; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0046861; C:glyoxysomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; ISS: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; IMP: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 1: Evidence at protein level;
KW Acetylation; Calcium; Glyoxysome; Heme; Hydrogen peroxide; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Peroxidase; Peroxisome; Potassium;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..287
FT /note="L-ascorbate peroxidase 3"
FT /id="PRO_0000261323"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..287
FT /note="AKR2A-binding sequence (ABS) required for peroxisome
FT membrane targeting"
FT /evidence="ECO:0000269|PubMed:20215589"
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 182
FT /note="K -> N (in Ref. 4; CAA06823)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="V -> VR (in Ref. 4; CAA06823)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Missing (in Ref. 4; CAA06823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 31572 MW; B348E74BA34115DE CRC64;
MAAPIVDAEY LKEITKARRE LRSLIANKNC APIMLRLAWH DAGTYDAQSK TGGPNGSIRN
EEEHTHGANS GLKIALDLCE GVKAKHPKIT YADLYQLAGV VAVEVTGGPD IVFVPGRKDS
NVCPKEGRLP DAKQGFQHLR DVFYRMGLSD KDIVALSGGH TLGRAHPERS GFDGPWTQEP
LKFDNSYFVE LLKGESEGLL KLPTDKTLLE DPEFRRLVEL YAKDEDAFFR DYAESHKKLS
ELGFNPNSSA GKAVADSTIL AQSAFGVAVA AAVVAFGYFY EIRKRMK
