Reviewed, UniProtKB/Swiss-Prot Q05431 (APX1_ARATH)

Names and origin

Protein names

Recommended name:
    L-ascorbate peroxidase 1, cytosolic
      Short name=AP
      Short name=AtAPx01
    EC=1.11.1.11

Gene names

Name:	APX1
Ordered Locus Names:	At1g07890
ORF Names:	F24B9.2

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	250 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. Constitutes a central component of the reactive oxygen gene network.
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.
Subcellular location	Cytoplasm.
Tissue specificity	Predominantly expressed in flowers.
Induction	By ethylene, ozone, sulfur dioxide, Fe exposure, oxidative and heat-shock stresses, and by excess light treatment.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Direct protein sequencing
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449365,EBI-449157

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Notes: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q05431-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 250	249	L-ascorbate peroxidase 1, cytosolic		PRO_0000055592
Sites
	Active site	42	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	38	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 33A536D85B2CAA6C	FASTA	250	27,561
	10 20 30 40 50 60 MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ SRTGGPFGTM 70 80 90 100 110 120 RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA GVVAVEVTGG PDIPFHPGRE 130 140 150 160 170 180 DKPQPPPEGR LPDATKGCDH LRDVFAKQMG LSDKDIVALS GAHTLGRCHK DRSGFEGAWT 190 200 210 220 230 240 SNPLIFDNSY FKELLSGEKE GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM 250 KLSELGFADA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding ascorbate peroxidase from Arabidopsis thaliana." Kubo A., Saji H., Tanaka K., Tanaka K., Kondo N. Plant Mol. Biol. 18:691-701(1992) [PubMed: 1558944] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Genomic DNA structure of a gene encoding cytosolic ascorbate peroxidase from Arabidopsis thaliana." Kubo A., Saji H., Tanaka K., Kondo N. FEBS Lett. 315:313-317(1993) [PubMed: 8422923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"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.
[6]	"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 (JUL-2006) to the EMBL/GenBank/DDBJ databases 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]	"Expression of Arabidopsis cytosolic ascorbate peroxidase gene in response to ozone or sulfur dioxide." Kubo A., Saji H., Tanaka K., Kondo N. Plant Mol. Biol. 29:479-489(1995) [PubMed: 8534847] [Abstract] Cited for: INDUCTION.
[9]	"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: INDUCTION.
[10]	"The heat-shock element is a functional component of the Arabidopsis APX1 gene promoter." Storozhenko S., De Pauw P., Van Montagu M., Inze D., Kushnir S. Plant Physiol. 118:1005-1014(1998) [PubMed: 9808745] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[11]	"Iron-regulated expression of a cytosolic ascorbate peroxidase encoded by the APX1 gene in Arabidopsis seedlings." Fourcroy P., Vansuyt G., Kushnir S., Inze D., Briat J.-F. Plant Physiol. 134:605-613(2004) [PubMed: 14739345] [Abstract] Cited for: INDUCTION.
[12]	"Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis." Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J., Shulaev V., Schlauch K., Mittler R. Plant Cell 17:268-281(2005) [PubMed: 15608336] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59600 mRNA. Translation: CAA42168.1. D14442 Genomic DNA. Translation: BAA03334.1. U63815 Genomic DNA. Translation: AAB07880.1. AC007583 Genomic DNA. Translation: AAF75066.1. AY039879 mRNA. Translation: AAK63983.1. AY056395 mRNA. Translation: AAL08251.1. AY094002 mRNA. Translation: AAM16263.1. AK230096 mRNA. Translation: BAF01915.1. AY086425 mRNA. Translation: AAM63427.1.
PIR	D86214. S20866.
RefSeq	NP_001030991.2. NP_001030992.2. NP_001077482.1. NP_001117244.1. NP_172267.1. NP_849607.1. NP_973786.1.
UniGene	At.47584
3D structure databases
HSSP	HSSP built from PDB template 1OAF based on UniProtKB Q43758.
SMR	Q05431. Positions 3-250.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05431.
Protein family/group databases
PeroxiBase	1890. AtAPx01.
2-D gel databases
SWISS-2DPAGE	Q05431.
Proteomic databases
ProMEX	Q05431.
Genome annotation databases
GeneID	837304.
GenomeReviews	Gene locus AT1G07890 in contig CT485782_GR.
KEGG	ath:AT1G07890.
NMPDR	fig|3702.1.peg.984.
Organism-specific databases
GeneFarm	1942. 146.
TAIR	At1g07890.
Gene expression databases
ArrayExpress	Q05431.
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

APX1_ARATH

Accession

Primary (citable) accession number: Q05431
Secondary accession number(s): Q0WLU2, Q2V4P8, Q2V4P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)