Q9SB81 (PER42_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxidase 42
Short name=Atperox P42
EC=1.11.1.7

Alternative name(s):
ATP1a/ATP1b
PRXR1

Gene names

Name:	PER42
Synonyms:	P42
Ordered Locus Names:	At4g21960
ORF Names:	F1N20.3, T8O5.170

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	330 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. Might function as heat shock-like defense protein.
Catalytic activity	2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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	Constitutively expressed in the whole plant, with the highest expression in roots. Ref.9
Induction	Expressed under a diurnal rhythm (circadian clock control). Ref.10
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 CAA17163.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB79151.1 differs from that shown. Reason: Erroneous initiation.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 – 23	23	Potential
	Chain	24 – 330	307	Peroxidase 42		PRO_0000023708
Sites
	Active site	71	1	Proton acceptor By similarity
	Metal binding	72	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	79	1	Calcium 1 By similarity
	Metal binding	81	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	247	1	Calcium 2 By similarity
	Metal binding	250	1	Calcium 2 By similarity
	Metal binding	255	1	Calcium 2 By similarity
	Binding site	167	1	Substrate; via carbonyl oxygen By similarity
	Site	67	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 119		By similarity
	Disulfide bond	73 ↔ 78		By similarity
	Disulfide bond	125 ↔ 323		By similarity
	Disulfide bond	204 ↔ 231		By similarity
Experimental info
	Sequence conflict	13	1	C → F Ref.2
	Sequence conflict	13	1	C → F Ref.6
	Sequence conflict	27	1	A → T Ref.2
	Sequence conflict	27	1	A → T Ref.6
	Sequence conflict	47	1	V → I Ref.2
	Sequence conflict	47	1	V → I Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9SB81 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: 3237E5DDAB9B6C45	FASTA	330	37,295
	10 20 30 40 50 60 MGGKGVMMVA ILCLWALSAT SEAVTEAEPG LMMNFYKDTC PQAEDIVREQ VKLLYKRHKN 70 80 90 100 110 120 TAFSWLRNIF HDCAVESCDA SLLLDSTRRE LGEKEHDRSF GLRNFRYIEE IKEALERECP 130 140 150 160 170 180 GVVSCSDILV LSAREGIEAV GGPYIPLKTG RRDGLKSRTD MLESYLPDHN ESISVVLEKF 190 200 210 220 230 240 KSIGIDTPGL VALLGSHSVG RTHCVKLVHR LYPEVDPSLN PDHVPHMLHK CPDSIPDPKA 250 260 270 280 290 300 VQYVRNDRGT PMVLDNNYYR NILDNKGLLL VDHQLAHDKR TRPIVKKMAK DQAYFFKEFT 310 320 330 RAIQILSENN PLTGSKGEIR KQCNLANKNH

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 [MRNA]. Strain: cv. Columbia. Tissue: Flower, Leaf, Root, Silique and Stem.
[2]	"Sequence and RT-PCR expression analysis of two peroxidases from Arabidopsis thaliana belonging to a novel evolutionary branch of plant peroxidases." Kjaersgaard I.V.H., Jespersen H.M., Rasmussen S.K., Welinder K.G. Plant Mol. Biol. 33:699-708(1997) [PubMed: 9132061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"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.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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]	"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 1-168. Tissue: Leaf.
[7]	"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana." Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B. Plant J. 4:1051-1061(1993) [PubMed: 8281187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-330. Strain: cv. Columbia. Tissue: Green siliques.
[8]	"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.
[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: TISSUE SPECIFICITY. Strain: cv. Columbia.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98313 mRNA. Translation: CAA66957.1. X98189 mRNA. Translation: CAA66862.1. AL021890 Genomic DNA. Translation: CAA17163.1. Different initiation. AL022140 Genomic DNA. No translation available. AL161556 Genomic DNA. Translation: CAB79151.1. Different initiation. CP002687 Genomic DNA. Translation: AEE84535.1. AF325015 mRNA. Translation: AAG40367.1. AF428379 mRNA. Translation: AAL16147.1. AY056809 mRNA. Translation: AAL10500.1. AY058071 mRNA. Translation: AAL24179.1. AY059810 mRNA. Translation: AAL24292.1. AY132009 mRNA. Translation: AAM91042.1. AF083767 mRNA. Translation: AAN60325.1. Z17792 mRNA. Translation: CAA79071.1.
IPI	IPI00540197.
PIR	T05478.
RefSeq	NP_567641.1. NM_118317.3.
UniGene	At.23508. At.71691.
3D structure databases
ProteinModelPortal	Q9SB81.
SMR	Q9SB81. Positions 30-329.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SB81. 1 interaction.
STRING	Q9SB81.
Protein family/group databases
PeroxiBase	208. AtPrx42.
Proteomic databases
PRIDE	Q9SB81.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G21960.1; AT4G21960.1; AT4G21960.
GeneID	828285.
GenomeReviews	Gene locus AT4G21960 in contig CT486007_GR.
KEGG	ath:AT4G21960.
NMPDR	fig|3702.1.peg.20045.
Organism-specific databases
GeneFarm	1871. 61.
TAIR	At4g21960.
Phylogenomic databases
eggNOG	COG0376.
GeneTree	EPGT00070000030884.
HOGENOM	HBG597790.
InParanoid	Q9SB81.
OMA	DRGTPMV.
PhylomeDB	Q9SB81.
ProtClustDB	CLSN2917592.
Gene expression databases
ArrayExpress	Q9SB81.
Genevestigator	Q9SB81.
GermOnline	AT4G21960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. [Graphical view]
KO	K00430.
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. False negative. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER42_ARATH

Accession

Primary (citable) accession number: Q9SB81
Secondary accession number(s): Q41937, Q42579, Q43730

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	December 6, 2002
Last modified:	November 16, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program