Reviewed, UniProtKB/Swiss-Prot Q43731 (PER50_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 50
      Short name=Atperox P50
    EC=1.11.1.7
Alternative name(s):
    PRXR2
    ATP9a

Gene names

Name:	PER50
Synonyms:	P50
Ordered Locus Names:	At4g37520
ORF Names:	F19F18.10, F6G17.9

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	329 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	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. Exhibits a Ca2+-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
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.
Tissue specificity	Expressed in roots and leaves.
Developmental stage	Up-regulated during leaf development. Ref.9
Induction	Enhanced expression in response of mechanical wounding. Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule. Expressed under a diurnal rhythm (circadian clock control). Ref.10 Ref.11
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Biological rhythms Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
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 rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: TAIR 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 – 25	25	Potential
	Chain	26 – 329	304	Peroxidase 50		PRO_0000023715
Sites
	Active site	67	1	Proton acceptor By similarity
	Metal binding	68	1	Calcium 1 By similarity
	Metal binding	71	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	73	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	75	1	Calcium 1 By similarity
	Metal binding	77	1	Calcium 1 By similarity
	Metal binding	197	1	Iron (heme axial ligand) By similarity
	Metal binding	198	1	Calcium 2 By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Metal binding	252	1	Calcium 2 By similarity
	Metal binding	257	1	Calcium 2 By similarity
	Binding site	167	1	Substrate; via carbonyl oxygen By similarity
	Site	63	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	26	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Disulfide bond	36 ↔ 119		By similarity
	Disulfide bond	69 ↔ 74		By similarity
	Disulfide bond	125 ↔ 325		By similarity
	Disulfide bond	204 ↔ 236		By similarity
Experimental info
	Sequence conflict	109	1	A → T in AAM63630. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q43731-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 167FDDA36B279B1C	FASTA	329	36,076
	10 20 30 40 50 60 MVVVNKTNLL LLLLSLCLTL DLSSAQLRRN FYAGSCPNVE QIVRNAVQKK VQQTFTTIPA 70 80 90 100 110 120 TLRLYFHDCF VNGCDASVMI ASTNNNKAEK DHEENLSLAG DGFDTVIKAK EALDAVPNCR 130 140 150 160 170 180 NKVSCADILT MATRDVVNLA GGPQYDVELG RLDGLSSTAA SVGGKLPHPT DDVNKLTSLF 190 200 210 220 230 240 AKNGLSLNDM IALSGAHTLG FAHCTKVFNR IYTFNKTTKV DPTVNKDYVT ELKASCPRNI 250 260 270 280 290 300 DPRVAINMDP TTPRQFDNVY YKNLQQGKGL FTSDQVLFTD RRSKPTVDLW ANNGQLFNQA 310 320 FINSMIKLGR VGVKTGSNGN IRRDCGAFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases." Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P. Plant Gene Register PGR96-066 Cited for: NUCLEOTIDE SEQUENCE. 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]	"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.
[4]	"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].
[5]	"Analysis of two incompletely spliced Arabidopsis cDNAs encoding novel types of peroxidase." Justesen A.F., Jespersen H.M., Welinder K.G. Biochim. Biophys. Acta 1443:149-154(1998) [PubMed: 9838086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-329. Strain: cv. Columbia. Tissue: Leaf.
[6]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206.
[7]	"Computational analyses and annotations of the Arabidopsis peroxidase gene family." Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G. FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract] Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[8]	"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana." Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C. J. Plant Physiol. 159:1165-1171(2002) Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[9]	"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array." Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X. Plant Physiol. Biochem. 39:221-242(2001) Cited for: DEVELOPMENTAL STAGE. Strain: cv. Columbia.
[10]	"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis." Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M. Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed: 11027363] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[11]	"Microarray analysis of diurnal and circadian-regulated genes in Arabidopsis." Schaffer R., Landgraf J., Accerbi M., Simon V., Larson M., Wisman E. Plant Cell 13:113-123(2001) [PubMed: 11158533] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[12]	"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	X98314 mRNA. Translation: CAA66958.1. AL035605 Genomic DNA. Translation: CAB38291.1. AL161591 Genomic DNA. Translation: CAB80417.1. AL035601 Genomic DNA. No translation available. AY062816 mRNA. Translation: AAL32894.1. AY081577 mRNA. Translation: AAM10139.1. AY086567 mRNA. Translation: AAM63630.1. X98856 Genomic DNA. Translation: CAA67362.1. AJ006960 Genomic DNA. Translation: CAA07352.1. AF083762 mRNA. Translation: AAN60320.1.
IPI	IPI00535466.
PIR	T04709.
RefSeq	NP_195468.1.
UniGene	At.22541 At.68229
3D structure databases
HSSP	HSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBase	Search...
Protein family/group databases
PeroxiBase	216. AtPrx50.
Proteomic databases
PRIDE	Q43731.
Genome annotation databases
GeneID	829907.
GenomeReviews	Gene locus AT4G37520 in contig CT486007_GR.
KEGG	ath:AT4G37520.
NMPDR	fig|3702.1.peg.21863.
Organism-specific databases
GeneFarm	1882. 61.
TAIR	At4g37520.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q43731.
GermOnline	AT4G37520. 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. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER50_ARATH

Accession

Primary (citable) accession number: Q43731
Secondary accession number(s): Q96523, Q9SBA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)