Reviewed, UniProtKB/Swiss-Prot Q42564 (APX3_ARATH)

Names and origin

Protein names

Recommended name:
    L-ascorbate peroxidase 3, peroxisomal
      Short name=AtAPx03
    EC=1.11.1.11

Gene names

Name:	APX3
Synonyms:	APX, APXIII
Ordered Locus Names:	At4g35000
ORF Names:	M4E13.60

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	L-ascorbate + H2O2 = dehydroascorbate + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 1 potassium or calcium ion per subunit By similarity.
Subcellular location	Peroxisome membrane; Single-pass membrane protein. Glyoxysome membrane; Single-pass membrane protein. Ref.8
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Glyoxysome Membrane Peroxisome
Domain	Transit peptide Transmembrane
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR glyoxysomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: TAIR peroxisomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Peroxisome Potential
	Chain	? – 287		L-ascorbate peroxidase 3, peroxisomal		PRO_0000261323
Regions
	Transmembrane	259 – 279	21	Potential
Sites
	Active site	40	1	Proton acceptor By similarity
	Metal binding	160	1	Iron (heme axial ligand) By similarity
	Metal binding	161	1	Potassium or calcium By similarity
	Metal binding	177	1	Potassium or calcium By similarity
	Metal binding	184	1	Potassium or calcium By similarity
	Site	36	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	182	1	K → N in CAA06823. Ref.4
	Sequence conflict	189	1	V → VR in CAA06823. Ref.4
	Sequence conflict	223	1	Missing in CAA06823. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q42564-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B348E74BA34115DE	FASTA	287	31,572
	10 20 30 40 50 60 MAAPIVDAEY LKEITKARRE LRSLIANKNC APIMLRLAWH DAGTYDAQSK TGGPNGSIRN 70 80 90 100 110 120 EEEHTHGANS GLKIALDLCE GVKAKHPKIT YADLYQLAGV VAVEVTGGPD IVFVPGRKDS 130 140 150 160 170 180 NVCPKEGRLP DAKQGFQHLR DVFYRMGLSD KDIVALSGGH TLGRAHPERS GFDGPWTQEP 190 200 210 220 230 240 LKFDNSYFVE LLKGESEGLL KLPTDKTLLE DPEFRRLVEL YAKDEDAFFR DYAESHKKLS 250 260 270 280 ELGFNPNSSA GKAVADSTIL AQSAFGVAVA AAVVAFGYFY EIRKRMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase." Jespersen H.M., Kjaersgaard I.V.H., Oestergaard L., Welinder K.G. Biochem. J. 326:305-310(1997) [PubMed: 9291097] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress." Karpinski S., Escobar C., Karpinski B., Creissen G.P., Mullineaux P.M. Plant Cell 9:627-640(1997) [PubMed: 9144965] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase." Zhang H., Wang J., Nickel U., Allen R.D., Goodman H.M. Plant Mol. Biol. 34:967-971(1997) [PubMed: 9290648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Ascorbate peroxidase III gene from Arabidopsis thaliana is regulated by light and development." Escobar C., Bradley D.J., Puente P., Harberd N., Creissen G.P., Mullineaux P.M. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The Arabidopsis ascorbate peroxidase 3 is a peroxisomal membrane-bound antioxidant enzyme and is dispensable for Arabidopsis growth and development." Narendra S., Venkataramani S., Shen G., Wang J., Pasapula V., Lin Y., Kornyeyev D., Holaday A.S., Zhang H. J. Exp. Bot. 57:3033-3042(2006) [PubMed: 16873450] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X98003 mRNA. Translation: CAA66640.1. X98276 mRNA. Translation: CAA66926.1. U69138 mRNA. Translation: AAB71493.1. AJ006030 Genomic DNA. Translation: CAA06823.1. AL022023 Genomic DNA. Translation: CAA17765.1. AL161586 Genomic DNA. Translation: CAB80217.1. AY065143 mRNA. Translation: AAL38319.1. AY081646 mRNA. Translation: AAM10208.1. AY086162 mRNA. Translation: AAM63367.1.
IPI	IPI00520415.
PIR	S71279.
RefSeq	NP_195226.1.
UniGene	At.47586
3D structure databases
HSSP	HSSP built from PDB template 1OAF based on UniProtKB Q43758.
ModBase	Search...
Protein family/group databases
PeroxiBase	1891. AtAPx03.
Proteomic databases
PRIDE	Q42564.
ProMEX	Q42564.
Genome annotation databases
GeneID	829652.
GenomeReviews	Gene locus AT4G35000 in contig CT486007_GR.
KEGG	ath:AT4G35000.
NMPDR	fig|3702.1.peg.21574.
Organism-specific databases
GeneFarm	1982. 146.
TAIR	At4g35000.
Phylogenomic databases
OMA	Q42564. PTRFSNQ.
Enzyme and pathway databases
BRENDA	1.11.1.11. 302.
Gene expression databases
GermOnline	AT4G35000. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX3_ARATH

Accession

Primary (citable) accession number: Q42564
Secondary accession number(s): O81810

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 1, 1996
Last modified:	May 5, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)