Reviewed, UniProtKB/Swiss-Prot P82281 (APX4_ARATH)

Names and origin

Protein names

Recommended name:
    Probable L-ascorbate peroxidase 4, chloroplastic
    EC=1.11.1.11
Alternative name(s):
    Thylakoid lumenal 29 kDa protein
      Short name=TL29
    P29
    AtAPx07

Gene names

Name:	APX4
Ordered Locus Names:	At4g09010
ORF Names:	F23J3.40

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 › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	349 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.
Subcellular location	Plastid › chloroplast thylakoid lumen Ref.4.
Developmental stage	Down-regulated during leaf senescence. Ref.5
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Caution	Lacks the heme-binding site, the proton acceptor and the transition state stabilizer, which are conserved features of the ascorbate peroxidase.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Chloroplast Plastid Thylakoid
Domain	Transit peptide
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	chloroplast thylakoid lumen Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast thylakoid membrane Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Transit peptide	? – 82		Thylakoid Ref.4
	Chain	83 – 349	267	Probable L-ascorbate peroxidase 4, chloroplastic		PRO_0000023635
Experimental info
	Sequence conflict	96	1	S → A in AAP72143. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P82281-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: ABD439188BDA8E61	FASTA	349	37,934
	10 20 30 40 50 60 MGGVSFLSTV PSFTNTTNHQ HLTTLSSSSH RSAVIRCSKI EPQVSGESLA FHRRDVLKLA 70 80 90 100 110 120 GTAVGMELIG NGFINNVGDA KAADLNQRRQ RSEFQSKIKI LLSTTIKAKP ELVPSLLKLA 130 140 150 160 170 180 LNDAMTYDKA TKSGGANGSI RFSSELSRAE NEGLSDGLSL IEEVKKEIDS ISKGGPISYA 190 200 210 220 230 240 DIIQLAGQSA VKFTYLASAI RKCGGNEEKG NLLYTAYGSA GQWGLFDRNF GRSDATEADP 250 260 270 280 290 300 EGRVPQWGKA TVQEMKDKFI AVGLGPRQLA VMSAFLGPDQ AATEQLLATD PQVAPWVQKY 310 320 330 340 QRSRETVSQT DYEVDLITAF TKLSCLGQQI NFEAYTYPVE RINLSKLKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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: NUCLEOTIDE SEQUENCE [MRNA] OF 11-306. Strain: cv. Columbia. Tissue: Leaf.
[4]	"A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen." Kieselbach T., Bystedt M., Hynds P., Robinson C., Schroeder W.P. FEBS Lett. 480:271-276(2000) [PubMed: 11034343] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-112, SUBCELLULAR LOCATION. Strain: cv. Columbia.
[5]	"Expression of the Apx gene family during leaf senescence of Arabidopsis thaliana." Panchuk I.I., Zentgraf U., Volkov R.A. Planta 222:926-932(2005) [PubMed: 16034597] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC005359 Genomic DNA. No translation available. AL161513 Genomic DNA. Translation: CAB78025.1. AF370534 mRNA. Translation: AAK48961.1. AY072503 mRNA. Translation: AAL66918.1. AF441713 mRNA. Translation: AAP72143.1.
IPI	IPI00529692.
PIR	A85091.
RefSeq	NP_192640.1.
UniGene	At.22637 At.47549 Rra.1310
3D structure databases
SMR	P82281. Positions 95-345.
ModBase	Search...
Protein-protein interaction databases
STRING	P82281.
Protein family/group databases
PeroxiBase	3920. AtAPx07.
Proteomic databases
PRIDE	P82281.
Genome annotation databases
GeneID	826480.
GenomeReviews	Gene locus AT4G09010 in contig CT486007_GR.
KEGG	ath:AT4G09010.
NMPDR	fig|3702.1.peg.18558.
Organism-specific databases
GeneFarm	1959. 146.
TAIR	At4g09010.
Phylogenomic databases
HOGENOM	HBG318899.
InParanoid	P82281.
OMA	YQRSRET.
Enzyme and pathway databases
BRENDA	1.11.1.11. 302.
Gene expression databases
Genevestigator	P82281.
GermOnline	AT4G09010. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002207. Asc_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX4_ARATH

Accession

Primary (citable) accession number: P82281
Secondary accession number(s): Q7XZP6, Q9M0S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	February 9, 2010
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)