Q42592 (APXS_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-ascorbate peroxidase S, chloroplastic/mitochondrial
EC=1.11.1.11

Alternative name(s):
Stromal ascorbate peroxidase
Short name=AtAPx05
Short name=sAPX

Gene names

Name:	APXS
Ordered Locus Names:	At4g08390
ORF Names:	T28D5.80

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	372 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	2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-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	Mitochondrion. Plastid › chloroplast stroma Potential Ref.5.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Chloroplast Mitochondrion Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR membrane Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay Ref.5. Source: TAIR
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

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

Isoform 1 (identifier: Q42592-1)

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
	Transit peptide	1 – ?		Chloroplast and mitochondrion Potential
	Chain	? – 372		L-ascorbate peroxidase S, chloroplastic/mitochondrial		PRO_0000261326
Sites
	Active site	133	1	Proton acceptor By similarity
	Metal binding	262	1	Iron (heme axial ligand) By similarity
	Metal binding	263	1	Potassium or calcium By similarity
	Metal binding	295	1	Potassium or calcium By similarity
	Metal binding	302	1	Potassium or calcium By similarity
	Site	129	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	11	1	G → V in CAA67425. Ref.1
	Sequence conflict	75	1	S → P in CAA67425. Ref.1
	Sequence conflict	81	1	Y → C in CAA67425. Ref.1
	Sequence conflict	371	1	V → I in CAA67425. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: A5D94B9A20720B87	FASTA	372	40,407
	10 20 30 40 50 60 MAERVSLTLN GTLLSPPPTT TTTTMSSSLR STTAASLLLR SSSSSSRSTL TLSASSSLSF 70 80 90 100 110 120 VRSLVSSPRL SSSSSLSQKK YRIASVNRSF NSTTAATKSS SSDPDQLKNA REDIKELLST 130 140 150 160 170 180 KFCHPILVRL GWHDAGTYNK NIKEWPQRGG ANGSLRFDIE LKHAANAGLV NALNLIKDIK 190 200 210 220 230 240 EKYSGISYAD LFQLASATAI EEAGGPKIPM KYGRVDASGP EDCPEEGRLP DAGPPSPATH 250 260 270 280 290 300 LREVFYRMGL DDKDIVALSG AHTLGRSRPE RSGWGKPETK YTKEGPGAPG GQSWTPEWLK 310 320 330 340 350 360 FDNSYFKEIK EKRDEDLLVL PTDAAIFEDS SFKVYAEKYA ADQDAFFKDY AVAHAKLSNL 370 GAEFNPPEGI VI

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]	"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.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
[5]	"Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants." Chew O., Whelan J., Millar A.H. J. Biol. Chem. 278:46869-46877(2003) [PubMed: 12954611] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98925 mRNA. Translation: CAA67425.1. AL109819 Genomic DNA. Translation: CAB52561.1. AL161511 Genomic DNA. Translation: CAB77964.1. CP002687 Genomic DNA. Translation: AEE82634.1. CP002687 Genomic DNA. Translation: AEE82635.1. AY056319 mRNA. Translation: AAL07168.1. AY114065 mRNA. Translation: AAM45113.1.
IPI	IPI00522703.
PIR	T14193.
RefSeq	NP_192579.1. NM_116908.2. NP_974520.1. NM_202791.3.
UniGene	At.22866.
3D structure databases
HSSP	HSSP built from PDB template 1APX based on UniProtKB P48534.
ProteinModelPortal	Q42592.
SMR	Q42592. Positions 100-369.
ModBase	Search...
Protein-protein interaction databases
STRING	Q42592.
Protein family/group databases
PeroxiBase	1886. AtAPx05.
Proteomic databases
PRIDE	Q42592.
ProMEX	Q42592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G08390.1; AT4G08390.1; AT4G08390. AT4G08390.2; AT4G08390.2; AT4G08390.
GeneID	826396.
GenomeReviews	Gene locus AT4G08390 in contig CT486007_GR.
KEGG	ath:AT4G08390.
NMPDR	fig|3702.1.peg.18492.
Organism-specific databases
GeneFarm	1956. 146.
TAIR	At4g08390.
Phylogenomic databases
GeneTree	EPGT00050000027793.
HOGENOM	HBG597790.
InParanoid	Q42592.
OMA	DCPEEGR.
PhylomeDB	Q42592.
ProtClustDB	CLSN2685967.
Gene expression databases
Genevestigator	Q42592.
Family and domain databases
InterPro	IPR002207. Asc_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
KO	K00434.
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APXS_ARATH

Accession

Primary (citable) accession number: Q42592
Secondary accession number(s): Q9STM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	November 16, 2011
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program