Reviewed, UniProtKB/Swiss-Prot O23474 (PER40_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 40
      Short name=Atperox P40
    EC=1.11.1.7

Gene names

Name:	PER40
Synonyms:	P40
Ordered Locus Names:	At4g16270
ORF Names:	dl4175w, FCAALL.329

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	348 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	Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted By similarity.
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Sequence caution	The sequence CAB10406.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78669.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity 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
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 348	327	Peroxidase 40		PRO_0000023706
Sites
	Active site	90	1	Proton acceptor By similarity
	Metal binding	91	1	Calcium 1 By similarity
	Metal binding	94	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	96	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	98	1	Calcium 1 By similarity
	Metal binding	100	1	Calcium 1 By similarity
	Metal binding	217	1	Iron (heme axial ligand) By similarity
	Metal binding	218	1	Calcium 2 By similarity
	Metal binding	269	1	Calcium 2 By similarity
	Metal binding	272	1	Calcium 2 By similarity
	Metal binding	277	1	Calcium 2 By similarity
	Binding site	187	1	Substrate; via carbonyl oxygen By similarity
	Site	86	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	26	1	N-linked (GlcNAc...) Potential
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 139		By similarity
	Disulfide bond	92 ↔ 97		By similarity
	Disulfide bond	145 ↔ 344		By similarity
	Disulfide bond	224 ↔ 256		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O23474-1 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: 1B438813818178E5	FASTA	348	37,460
	10 20 30 40 50 60 MKNLFNLFLM FFFAMPILSL SENPTNFSES CEDGSGETGS SFGIGFDLVL DFGLYRNSCP 70 80 90 100 110 120 EAESIVYSWV ETTVLEDPRM AASLLRLHFH DCFVNGCDAS VLLDDTEGLV GEKTAPPNLN 130 140 150 160 170 180 SLRGFEVIDS IKSDIESVCP ETVSCADILA MAARDSVVVS GGPRWEVEVG RKDSRTASKQ 190 200 210 220 230 240 AATNGLPSPN STVSTLISTF QNLGLSQTDM VALSGGHTLG KARCTSFTAR LQPLQTGQPA 250 260 270 280 290 300 NHGDNLEFLE SLQQLCSTVG PSVGITQLDL VTPSTFDNQY YVNLLSGEGL LPSDQALAVQ 310 320 330 340 DPGTRAIVET YATDQSVFFE DFKNAMVKMG GIPGGSNSEI RKNCRMIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M., Shinozaki K., Ecker J.R. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z97340 Genomic DNA. Translation: CAB10406.1. Sequence problems. AL161543 Genomic DNA. Translation: CAB78669.1. Sequence problems. BT011747 mRNA. Translation: AAS49110.1. AK175661 mRNA. Translation: BAD43424.1. AK175982 mRNA. Translation: BAD43745.1.
IPI	IPI00543045.
UniGene	At.50347 At.67828
3D structure databases
HSSP	HSSP built from PDB template 1SCH based on UniProtKB P22195.
ModBase	Search...
Protein family/group databases
PeroxiBase	206. AtPrx40.
Genome annotation databases
GenomeReviews	Gene locus AT4G16270 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.19392.
Organism-specific databases
GeneFarm	1869. 61.
TAIR	At4g16270.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	O23474.
GermOnline	AT4G16270. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER40_ARATH

Accession

Primary (citable) accession number: O23474
Secondary accession number(s): Q53XE3, Q67ZY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 6, 2002
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)