Reviewed, UniProtKB/Swiss-Prot Q1PER6 (APX2_ARATH)

Names and origin

Protein names

Recommended name:
    L-ascorbate peroxidase 2, cytosolic
    EC=1.11.1.11
Alternative name(s):
    L-ascorbate peroxidase 1b
      Short name=APX1b
      Short name=AtAPx02

Gene names

Name:	APX2
Synonyms:	APX1B
Ordered Locus Names:	At3g09640
ORF Names:	F11F8_23

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

General annotation (Comments)

Function	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 1 potassium or calcium ion per subunit By similarity.
Subcellular location	CytoplasmBy similarity.
Tissue specificity	Detected in bundle sheath cells, the photosynthetic cells that surround the phloem and xylem.
Induction	By excess light treatment, by wounding and by heat-shock stress.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Sequence caution	The sequence AAF23294.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 251	250	L-ascorbate peroxidase 2, cytosolic		PRO_0000261322
Sites
	Active site	43	1	Proton acceptor By similarity
	Metal binding	163	1	Iron (heme axial ligand) By similarity
	Metal binding	164	1	Potassium or calcium By similarity
	Metal binding	180	1	Potassium or calcium By similarity
	Metal binding	182	1	Potassium or calcium By similarity
	Metal binding	185	1	Potassium or calcium; via carbonyl oxygen By similarity
	Metal binding	187	1	Potassium or calcium By similarity
	Site	39	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	6	1	Y → F in ABE65932. Ref.5
	Sequence conflict	231	1	F → S in CAA66925. Ref.1
	Sequence conflict	231	1	F → S in CAA56340. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q1PER6-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FFC7F6D82A4EF3E0	FASTA	251	28,006
	10 20 30 40 50 60 MVKKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV KTKTGGPFGT 70 80 90 100 110 120 IRHPQELAHD ANNGLDIAVR LLDPIKELFP ILSYADFYQL AGVVAVEITG GPEIPFHPGR 130 140 150 160 170 180 LDKVEPPPEG RLPQATKGVD HLRDVFGRMG LNDKDIVALS GGHTLGRCHK ERSGFEGAWT 190 200 210 220 230 240 PNPLIFDNSY FKEILSGEKE GLLQLPTDKA LLDDPLFLPF VEKYAADEDA FFEDYTEAHL 250 KLSELGFADK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family." Santos M., Gosseau H., Lister C., Foyer C., Creissen G.P., Mullineaux P.M. Planta 198:64-69(1996) [PubMed: 8580771] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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], INDUCTION. Strain: cv. Columbia. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations." Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P. Plant Biotechnol. J. 4:317-324(2006) [PubMed: 17147637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[6]	"Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis." Panchuk I.I., Volkov R.A., Schoffl F. Plant Physiol. 129:838-853(2002) [PubMed: 12068123] [Abstract] Cited for: INDUCTION.
[7]	"Induction of ASCORBATE PEROXIDASE 2 expression in wounded Arabidopsis leaves does not involve known wound-signalling pathways but is associated with changes in photosynthesis." Chang C.C., Ball L., Fryer M.J., Baker N.R., Karpinski S., Mullineaux P.M. Plant J. 38:499-511(2004) [PubMed: 15086807] [Abstract] Cited for: INDUCTION.
[8]	"Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves." Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R. Plant J. 33:691-705(2003) [PubMed: 12609042] [Abstract] Cited for: INDUCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X80036 Genomic DNA. Translation: CAA56340.1. X98275 mRNA. Translation: CAA66925.1. AC016661 Genomic DNA. Translation: AAF23294.1. Sequence problems. AK176821 mRNA. Translation: BAD44584.1. AK176908 mRNA. Translation: BAD44671.1. DQ446651 mRNA. Translation: ABE65932.1.
RefSeq	NP_001030664.1. NP_187575.2.
UniGene	At.129
3D structure databases
SMR	Q1PER6. Positions 4-249.
ModBase	Search...
Genome annotation databases
GeneID	820121.
KEGG	ath:AT3G09640.
NMPDR	fig|3702.1.peg.12979.
Organism-specific databases
GeneFarm	727. 146.
TAIR	At3g09640.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [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

APX2_ARATH

Accession

Primary (citable) accession number: Q1PER6
Secondary accession number(s): Q39006, Q67XB1, Q9SF39

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 23 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)